Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

Differentiation of bloodstream-form trypanosomes into procyclic (midgut) forms is an important first step in the establishment of an infection within the tsetse fly. This complex process is mediated by a wide variety of factors, including those associated with the vector itself, the trypanosomes and the bloodmeal. As part of an on-going project in our laboratory, we recently isolated and characterized a bloodmeal-induced molecule with both lectin and trypsin activities from midguts of the tsetse fly, Glossina longipennis [Osir, E.O., Abubakar, L., Imbuga, M.O., 1995. Purification and characterization of a midgut lectin-trypsin complex from the tsetse fly, Glossina longipennis. Parasitol. Res. 81, 276-281]. The protein (lectin-trypsin complex) was found to be capable of stimulating differentiation of bloodstream trypanosomes in vitro. Using polyclonal antibodies to the complex, we screened a G. fuscipes fuscipes cDNA midgut expression library and identified a putative proteolytic lectin gene. The cDNA encodes a putative mature polypeptide with 274 amino acids (designated Glossina proteolytic lectin, Gpl). The deduced amino acid sequence includes a hydrophobic signal peptide and a highly conserved N-terminal sequence motif. The typical features of serine protease trypsin family of proteins found in the sequence include the His/Asp/Ser active site triad with the conserved residues surrounding it, three pairs of cysteine residues for disulfide bridges and an aspartate residue at the specificity pocket. Expression of the gene in a bacterial expression system yielded a protein (M(r) approximately 32,500). The recombinant protein (Gpl) bound d(+) glucosamine and agglutinated bloodstream-form trypanosomes and rabbit red blood cells. In addition, the protein was found to be capable of inducing transformation of bloodstream-form trypanosomes into procyclic forms in vitro. Antibodies raised against the recombinant protein showed cross-reactivity with the alpha subunit of the lectin-trypsin complex. These results support our earlier hypothesis that this molecule is involved in the establishment of trypanosome infections in tsetse flies.

The purpose of the paper is to examine the effect of demographic diversity in Top Management Team (TMT) on financial
reporting quality in commercial state corporations. The study adopted correlational and longitudinal research design and
stepwise regression analysis of FRQ variables on a set of demographic diversity variables in TMT. The findings provide
considerable evidence to suggest that TMT demographic diversity are associated with financial reporting quality
measured by fundamental qualitative characteristics of accounting information, earnings management, timeliness in
reporting and disclosure quality. The research implication is that; in general, demographic diversity in TMT- gender, age,
education, tenure and functional background may have important implication for financial reporting quality under
different measures. The value of this paper is to extend Prior research by addressing the potential effects of TMT
demographic diversity on FRQ. The findings reported in this paper provide novel insight to empirical financial reporting
quality literature in commercial state corporations.

ABSTRACT A suite of sediment samples from the Romanche Fracture Zone in the equatorial Atlantic has been subjected to bulk and partition chemical and mineralogical analyses, together with radiometric dating, in order to study the main controls on composition and origin.The interelement relationships in the sediments revealed by geostatistical analysis indicate that (1) Ca, Sr and P, (2) Al, Fe, Ti, V, Zn, Li, Be and K, (3) Mn, Co, Ni and Cu and (4) Mg, Cr and Ni are associated. Partition chemical data suggest that these element associations represent respectively biogenic, terrigenous, igneous and hydrogenic phases of the sediment.Surface and downcore sediment data indicate that the distribution of the biogenic component of the sediment is influenced by water depth. The distribution of the igneous component is largely controlled by a contribution from ultramafic sources and shows the influence of subsea erosion on the surface sediments. The distribution of the hydrogenic component is influenced by contribution from the water column. Sediment accumulation rate data indicate that these sediments have accumulated fairly rapidly. Bottom topography and turbidity current activity are probably the main factors controlling their accumulation. Metal accumulation rate data indicate that there is no significant hydrothermal contribution to the deposits as has been suggested by other workers.

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

Twenty variceal banding sessions were performed in eight patients between February 1995 and September 1996. A total of 69 rings were used to band the varices and at each session between two to six rings were used. Two of the eight had active bleeding and both underwent variceal banding to successfully arrest their bleeding as inpatients. Sixteen other variceal banding sessions were performed on an outpatient basis to obliterate their varices. Four of the eight patients had had sclerotherapy before and varices were still present. No acute or long term complications were noted. In one patient, variceal banding could not be performed as he developed stridor upon placement of the overtube. All the patients had advanced varices (Grade III or IV) and extended for more than 15 cms in the oesophagus. Endoscopic variceal obliteration remains the treatment of choice for patients with portal hypertension with variceal bleeding. Variceal banding is associated with a superior outcome when compared with sclerotherapy; the variceal kill time is shorter, infective complications less, rebleeding occurs less commonly and transfusion requirements are lower.

Isolated mouse interstitial cells were incubated with different concentrations of khat (Catha edulis) extract (0.06 mg/ml, 0.6 mg/ml. 6 mg/ml. 30 mg/ml and 60 mg/ml) and cell viability as well as testosterone concentration measured at 30 min intervals over a 3 h incubation period. High concentrations of khat extract (30 mg/ml and 60 mg/ml) significantly inhibited testosterone production while low concentrations (0.06 mg/ml. 0.6 mg/ml and 6 mg/ml) significantly stimulated (P < 0.05) testosterone production by mouse interstitial cells. Similarly, at concentrations of 30 mg/ml and 60 mg/ml, there was a significant decrease in interstitial cell viability, whereas at 0.06 mg/ml, 0.6 mg/ml and 6 mg/ml there was no significant decrease. There was only a weak correlation (r= 0.39) between testosterone production and viable interstitial cells. We postulate that khat extract at high concentrations may cause reproductive function impairment in the user but at low concentrations. may enhance testosterone production with accompanying effects on reproductive functions in male mice. @2006 Publishedby Elsevier Ireland Ltd. Kel'lVords: In dtro; Khat; Testosterone; Interstitial cells; Mouse

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ABSTRACT
This paper is a brief description of how the University of Nairobi through distance learning is empowering and developing the communities through distance education. The paper outlines the background against which the paper is based and the problem statement. The objectives of this paper will be to examine the role of adult education in community empowerment and development; and to explore how distance education has closed the chasm of access to education by the adults from remote communities. The paper stresses the indisputable need for promoting community- driven development and educational approaches as an important starting point for adult education and learning as well as poverty reduction.

Key words: Adult education, closing the chasm, Poverty, community empowerments

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