Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Trypsin production in the malaria vector Anopheles tessellatus Theobald peaks between 12 and 21 h after a blood meal. The presence of leupeptin or soybean trypsin inhibitor in a blood meal delayed the onset of maximal trypsin activity. Trypsin inhibitors in an infective blood meal increased the infectivity of Plasmodium vivax Grassi and decreased infectivity of P. falciparum Welch to An tessellatus. The opposite effects of trypsin inhibitors on infectivity of the 2 malaria parasites were attributed to differences in the biology of the parasites within the midgut of the vector, particularly the time of ookinete formation and the requirement for activation of a chitinase.
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PMID:Different effects of modulation of mosquito (Diptera:Culicidae) trypsin activity on the infectivity of two human malaria (Hemosporidia:Plasmodidae) parasites. 884 Jun 84

Microsomal chitinase from yeast and hyphal cells of Candida albicans was activated endogenously by incubation at 30 degrees C and exogenously by trypsin. The putative activating factor of yeast cells was separated from chitinase activity by fractionation of lysed protoplasts on an Iodixanol density gradient. The vacuole fraction contained no significant chitinase activity, but was enriched in chitinase activating factor. Activity of microsomal chitinase increased upon incubation with this, but no other gradient factor. Results suggest that the regulatory system governing microsomal chitinase activity, like that governing chitin synthase, involves a 'vacuolar' activating factor in Candida albicans.
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PMID:Potential chitinase activating factor from yeast cells of Candida albicans. 886 20

The abilities of isolates of saprophytes (Neurospora crassa, Aspergillus nidulans), an opportunistic human pathogen (Aspergillus fumigatus), an opportunistic insect pathogen (Aspergillus flavus), plant pathogens (Verticillium albo-atrum, Verticillium dahliae, Nectria haematococca), a mushroom pathogen (Verticillium fungicola) and entomopathogens (Verticillium lecanii, Beauveria bassiana, Metarhizium anisopliae) to utilize plant cell walls and insect cuticle components in different nutrient media were compared. The pathogens showed enzymic adaptation to the polymers present in the integuments of their particular hosts. Thus, the plant pathogens produced high levels of enzymes capable of degrading pectic polysaccharides, cellulose and xylan, as well as cutinase substrate, but secreted little or no chitinase and showed no proteolytic activity against elastin and mucin. The entomopathogens and V. fungicola degraded a broad spectrum of proteins (including elastin and mucin) but, except for chitinase, cellulase (V. lecanii and V. fungicola only) and cutinase (B. bassiana only), produced very low levels of polysaccharidases. The saprophytes (Neu. crassa and A. nidulans) and the opportunistic pathogens (A. fumigatus and A. flavus) produced the broadest spectrum of protein and polysaccharide degrading enzymes, indicative of their less specialized nutritional status. V. lecanii and V. albo-atrum were compared in more detail to identity factors that distinguish plant and insect pathogens. V. albo-atrum, but not V. lecanii, grew well on different plant cell wall components. The major class of proteases produced in different media by isolates of V. albo-atrum and V. dahliae were broad spectrum basic (pI > 10) trypsins which degrade Z-AA-AA-Arg-NA substrates (Z, benzoyl; AA, various amino acids; Na, nitroanilide), hide protein azure and insect (Manduca sexta) cuticles. Analogous peptidases were produced by isolates of V. lecanii and V. fungicola but they were specific for Z-Phe-Val-Arg-NA. V. albo-atrum and V. dahliae also produced low levels of neutral (pI ca 7) and basic (pI ca 9.5) subtilisin-like proteases active against a chymotrypsin substrate (Succinyl-Ala2-Pro-Phe-NA) and insect cuticle. In contrast, subtilisins comprised the major protease component secreted by V. lecanii and V. fungicola. Both V. lecanii and V. albo-atrum produced the highest levels of subtilisin and trypsin-like activities during growth on collagen or insect cuticle. Results are discussed in terms of the adaptation of fungi to the requirements of their ecological niches.
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PMID:Adaptation of proteases and carbohydrates of saprophytic, phytopathogenic and entomopathogenic fungi to the requirements of their ecological niches. 920 74

Present understanding of the development of sexual stages of the human malaria parasites Plasmodium vivax and P.falciparum in the Anopheles vector is reviewed, with particular reference to the role of the mosquito midgut in establishing an infection. The sexual stages of the parasite, the gametocytes, are formed in human erythrocytes. The changes in temperature and pH encountered by the gametocyte induce gametogenesis in the lumen of the midgut. Macromolecules derived from mosquito tissue and second messenger pathways regulate events leading to fertilization. In An.tessellatus the movement of the ookinete from the lumen to the midgut epithelium is linked to the release of trypsin in the midgut and the peritrophic matrix is not a firm barrier to this movement. The passage of the P.vivax ookinete through the peritrophic matrix may take place before the latter is fully formed. The late ookinete development in P.falciparum requires chitinase to facilitate penetration of the peritrophic matrix. Recognition sites for the ookinetes are present on the midgut epithelial cells. N-acetyl glucosamine residues in the oligosaccharide side chains of An.tessellatus midgut glycoproteins and peritrophic matrix proteoglycan may function as recognition sites for P.vivax and P.falciparum ookinetes. It is possible that ookinetes penetrating epithelial cells produce stress in the vector. Mosquito molecules may be involved in oocyst development in the basal lamina, and encapsulation of the parasite occurs in vectors that are refractory to the parasite. Detailed knowledge of vector-parasite interactions, particularly in the midgut and the identification of critical mosquito molecules offers prospects for manipulating the vector for the control of malaria.
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PMID:Interactions of human malaria parasites, Plasmodium vivax and P.falciparum, with the midgut of Anopheles mosquitoes. 933 Feb 62

Chitinases that function in the molting of the larval exoskeleton have been characterized previously. However, chitinase expression in an adult insect gut has not been described. Here we report on the initial characterization and cloning of a novel chitinase gene that is expressed specifically in the midgut of adult Anopheles gambiae females. Upon feeding, chitinase is secreted into the gut lumen as an inactive pro-enzyme that is later activated by trypsin. Thus, temporal regulation of chitinase activity is tightly coupled to the temporal pattern of trypsin secretion. The enzyme may play a role in structuring the chitin-containing extracellular peritrophic matrix, whose formation is also induced by feeding. A chitinase cDNA was cloned from a library enriched for gut-specific sequences. The open reading frame encodes a 525-amino acid protein comprised of a putative catalytic domain at the N terminus, a putative chitin-binding domain at the C terminus, and a threonine/serine/proline-rich amino acid stretch in between them. Northern analysis indicates that this chitinase is expressed exclusively in the guts of adult females and not in adult carcasses or in any larval or pupal tissues. The present findings suggest the possibility of using this chitinase as an antigen for a malaria transmission-blocking vaccine.
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PMID:Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae. 936 Sep 58

Secretion of proteolytic and chitinolytic enzymes is a hallmark of infection processes of Metralhizium anisopliae in response to host (insect) cuticular signals. The regulation of these enzymes (subtilisin-like proteases [Pr1a and Pr1b], trypsin-like proteases [Pr2], metalloproteases, aspartyl proteases, aminopeptidase, and chitinases) and a hydrophobin was investigated by Northern analysis and/or enzyme assay. The production of each enzyme showed a differential expression pattern in response to ambient pH; enzymes were synthesized only at pHs at which they function effectively, irrespective of whether the medium contained an inductive cuticle substrate. Three aspartyl proteases (pH optimum, 3), and chitinase (pH optimum, 5) showed maximal accumulation at acidic pHs. The highest level of aminopeptidase (pH optimum, 7) was detected at pH 7. The highest levels of five metalloproteases (pH optima, ca. 7) were detected over the pH range 6 to 8. Two trypsins and several subtilisin-like Pr1 isoforms with pH optima of ca. 8 were produced only under alkaline conditions. Northern analysis of RNA species corresponding to seven cDNA sequences encoding proteases and chitinase confirmed that the ambient pH played a major role in gene expression of secreted proteins. Hydrophobin was expressed almost equally at pHs 5 and 8 but was not expressed at pH 3. During fungal penetration, the pH of infected cuticle rises from about 6.3 to 7.7. Consistent with pH regulation of enzyme production, serine and metalloproteases were produced in situ during infection, but no production of aspartyl proteases was found. We propose that the alkalinity of infected cuticle represents a physiological signal that triggers the production of virulence factors.
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PMID:Ambient pH is a major determinant in the expression of cuticle-degrading enzymes and hydrophobin by Metarhizium anisopliae. 946 12

We have isolated a full-length chitinase complementary DNA from the tiger shrimp Penaeus monodon that encodes a 621 amino acid protein possessing the functional domains of the chitinase protein family. The Penaeus monodon chitinase 1 (PmChi-1) gene product is 81.8% identical to a chitinase 1 protein expressed in the hepatopancreas of Penaeus japonicus. Analysis by reverse transcription-polymerase chain reaction (RT-PCR) indicates that PmChi-1 messenger RNA is detectable in the hepatopancreas and the gut. PmChi-1 expression during the molt cycle fluctuates markedly, with lowest mRNA levels at stages A(1), C, and D(3); there is a dramatic increase in transcript abundance at the D(2) stage. Using the same tissues and molt stages, RT-PCR analyses of genes encoding other digestive enzymes (trypsin, chymotrypsin, and cathepsin L), a muscle structural protein (tropomyosin II), and housekeeping proteins (elongation factor II and GTP-binding protein) indicate that PmChi-1 is expressed in a distinct tissue-specific and stage-specific manner. The other digestive enzyme genes are expressed in a similar spatiotemporal pattern, but none exhibited a dramatic increase in transcript abundance at stage D(2). Increased expression of PmChi-1 at D(2) suggests that hepatopancreas-expressed chitinase is involved in the degradation of endogenous chitin in the gut peritrophic membrane prior to molting.
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PMID:The Penaeus monodon Chitinase 1 Gene Is Differentially Expressed in the Hepatopancreas During the Molt Cycle. 1081 51

The use of trypsin to break proteins covalently linked to the yeast walls of Candida albicans released approx. 50% of the proteins, but also glucose and N-acetylglucosamine. Analysis by affinity chromatography indicated that glucose and/or N-acetylglucosamine formed part of the same supramolecular complexes with mannoproteins. These complexes would represent a new type of cell wall structuration in which beta-1,6 glucan and chitin are linked to proteins. An internal peptide from a 50-kDa protein released by trypsin was sequenced, showing 100% identity with chitinase 2 protein and 92% with chitinase 3. The electrophoretic mobility of the chitinase 2 protein was changed by treatment with EndoH or beta-elimination, indicating that the enzyme was both N- and O-mannosylated.
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PMID:The use of trypsin to solubilize wall proteins from Candida albicans led to the identification of chitinase 2 as an enzyme covalently linked to the yeast wall structure. 1206 94

In order to define the cellular site of synthesis for hemocyanin and digestive enzymes in the decapod hepatopancreas, we studied the expression of messenger ribonucleic acids (RNAs) for these molecules in the epithelium lining hepatopancreas tubules. In situ hybridisation of gene probes for the digestive enzymes amylase, cathepsin-L, cellulase, chitinase-1 and trypsin to tissue sections of the shrimp hepatopancreas confirmed that the F-cells lining tertiary, secondary and primary ducts are the sites of synthesis for digestive enzyme messenger RNA (mRNA). The F-cells also contained mRNA for the hemocyanin gene. This finding raises important questions on the mechanism by which mature hemocyanin accumulates in the shrimp hemolymph. Our in situ hybridisation studies further showed that Penaeus monodon F-cells remain transcriptionally active for digestive enzyme mRNAs during periods of starvation.
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PMID:Expression of hemocyanin and digestive enzyme messenger RNAs in the hepatopancreas of the Black Tiger Shrimp Penaeus monodon. 1238 78

We examined the mycoparasitic and saprotrophic behavior of isolates representing groups of Trichoderma harzianum to establish a mechanism for the aggressiveness towards Agaricus bisporus in infested commercial compost. Mycoparasitic structures were infrequently observed in interaction zones on various media, including compost, with cryoscanning electron microscopy. T. harzianum grows prolifically in compost in the absence or presence of A. bisporus, and the aggressive European (Th2) and North American (Th4) isolates produced significantly higher biomasses (6.8- and 7.5-fold, respectively) in compost than did nonaggressive, group 1 isolates. All groups secreted depolymerases that could attack the cell walls of A. bisporus and of wheat straw, and some were linked to aggressiveness. Growth on mushroom cell walls in vitro resulted in rapid production of chymoelastase and trypsin-like proteases by only the Th2 and Th4 isolates. These isolates also produced a dominant protease isoform (pI 6.22) and additional chitinase isoforms. On wheat straw, Th4 produced distinct isoforms of cellulase and laminarinase, but there was no consistent association between levels or isoforms of depolymerases and aggressiveness. Th3's distinctive profiles confirmed its reclassification as Trichoderma atroviride. Proteases and glycanases were detected for the first time in sterilized compost colonized by T. harzianum. Xylanase dominated, and some isoforms were unique to compost, as were some laminarinases. We hypothesize that aggressiveness results from competition, antagonism, or parasitism but only as a component of, or following, extensive saprotrophic growth involving degradation of wheat straw cell walls.
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PMID:Saprotrophic and mycoparasitic components of aggressiveness of Trichoderma harzianum groups toward the commercial mushroom Agaricus bisporus. 1283 99


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