Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adherence of Candida albicans to a fibrin-platelet matrix formed in vitro was studied. Platelet-rich plasma obtained from rabbits was incubated with thrombin and CaCl2 to form a clot in tissue culture dishes. Such clots were then infected with 3 x 10(7) C. albicans cells per 0.3 ml prelabeled with [U14C]-glucose, and the percent adherence was measured after 30 min of incubation by counting the radioactivity in saline washes of the clot as well as a streptokinase-streptodornase digest of the corresponding clot. Heat- and formaldehyde-killed cells did not adhere as well as viable cells. Pretreatment of C. albicans with trypsin, chymotrypsin, and pronase reduced adherence to the clots. Normal rabbit serum and anti-Candida antiserum also inhibited adherence 40 and 100%, respectively, Diethylaminoethyl-purified anti-Candida gamma globulin (1:8) completely inhibited adherence, whereas purified normal serum gamma globulin did not. Several Candida spp. and Saccharomyces cerevisiae showed differences in their ability to adhere to clots. C. albicans and C. stellatoidea presented the highest adherence, whereas C. krusei, C. guilliermondii, and S. cerevisiae adhered less readily. Other species were intermediate in their ability to adhere.
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PMID:Adherence of Candida albicans to a fibrin-platelet matrix formed in vitro. 699 22

Factors that may influence adherence of Candida albicans to exfoliated human vaginal and buccal epithelial cells were studied in vitro. Factors that enhanced germination enhanced adherence. Heat-killed, germinated Candida organisms demonstrated poorer adherence than viable Candida organisms and no better adherence than nonviable, ungerminated Candida organisms. The difference between adherence of C. albicans to buccal epithelial cells and that to vaginal epithelial cells was significant, as were differences among volunteers. Preincubation in fucose but not mannose, glucose or galactose solutions, preincubation of germinated yeast or of epithelial cells in chymotrypsin or trypsin, a culture supernatant of germinated yeast killed by ultraviolet light, or precoating of epithelial cells with lactobacilli each inhibited adherence. These studies indicate that adherence of C. albicans is enhanced by a surface component of germinated yeast, probably a surface protein that binds to the epithelial receptor, possibly a glycoprotein.
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PMID:Adherence of Candida albicans to human vaginal and buccal epithelial cells. 701 45

Glomerular basement membrane (GBM) preparations were enzymatically glucosylated and applied to proteolytic degradation by several enzymes. The split products were then characterized and quantitatively estimated by high pressure liquid chromatography. For this purpose, GBMs were isolated by a sieving and sonication method, incubated with glucose and digested with the proteases trypsin, chymotrypsin, papain, pepsin and a lysosomal preparation. Comparison of the concentrations of split products obtained by proteolytic degradation of normal and nonenzymatically glucosylated membranes showed a remarkable reduced susceptibility of the nonenzymatically glucosylated membranes, possibly due to steric hindrance or altered electrical charge of the glucosylated membrane proteins. This could be interpreted as an additional factor for accumulation of basement membrane material in the diabetic state, that not only increased basement membrane synthesis may occur but also reduced catabolism could possibly contribute to the diabetic changes.
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PMID:Reduced susceptibility of nonenzymatically glucosylated glomerular basement membrane to proteases: is thickening of diabetic glomerular basement membranes due to reduced proteolytic degradation? 703 96

Aerolysin, a cytolytic bacterial exotoxin, was radioiodinated by using the Iodogen reagent. Binding of the labeled toxin to rat erythrocytes was inhibited by the native protein and by anti-aerolysin antibody. Toxin, once bound, was not removed by the addition of a large excess of free aerolysin. Binding of the radioactive toxin to erythrocytes of different species paralleled the hemolytic specificity of the unlabeled toxin. Pretreatment of the rat erythrocytes with trypsin, which removed a major membrane glycoprotein, resulted in a dramatic decrease in binding, whereas chymotrypsin treatment had no effect. Binding was inhibited by a glycoprotein fraction isolated from these cells but not by a total rat erythrocyte glycolipid preparation. Aerolysin caused the formation of holes in erythrocytes which were sized by measuring the release of labeled molecular weight markers. Glucagon (molecular weight 3550) and smaller molecules entrapped in human or rat erythrocytes were released by treatment with aerolysin, whereas methoxyinulin (molecular weight 5500) and larger molecules were not. Aerolysin also caused the release of glucose from large unilamellar lipid vesicles. The results indicate that a specific glycoprotein receptor facilitates the interaction of aerolysin with erythrocyte membranes. Binding is followed by the formation of discrete holes or pores, and this results in cell rupture by a colloid-osmotic process.
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PMID:Membrane glycoprotein receptor and hole-forming properties of a cytolytic protein toxin. 708 38

The proteases trypsin, alpha-chymotrypsin and papain were incubated with glucose for a period of 10 days at 37 degrees C and activity was tested in comparison to the enzymes incubated with the puffer solution only without glucose addition. Papain additionally was incubated for 10 days at 37 degrees C with the carbohydrates galactose, sucrose, lactose, glucosamine, galactosamine and mannosamine. While trypsin and chymotrypsin showed no change in enzymatic activity after incubation with glucose, the activity of papain was reduced by 70% to 90% (mean 84%). Incubation with galactose also inhibited papain activity but to a lesser extent (25% to 60%, mean 43%). Incubation with the other carbohydrates failed to inhibit papain activity. The mechanism inferred is nonenzymatic glucosylation of papain possibly as ketoamine linkage at the lysine residues situated close to the active site of papain causing steric or allosteric hindrance of the papain activity. The serine hydrolases trypsin and chymotrypsin without lysine residues near their active sites revealed unchanged activity after incubation with glucose.
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PMID:[Enzyme activities of native non-enzymatically glucosylated trypsin, chymotrypsin and papain]. 709 95

Immunoelectrophoresis of glomerular basement membrane antigens in the urine of 20 Type 1 (insulin-dependent) diabetic and 10 healthy children was performed. In 10 of the diabetic children, there was altered alpha-1-mobility, while the other diabetic and normal children showed alpha-2-mobility. After incubation with glucose, glomerular basement membrane antigens in the urine of healthy children showed alpha-1-mobility. Isolated human kidney glomerular basement membrane split products obtained by proteolytic degradation (papain, trypsin, chymotrypsin) were also investigated by immunoelectrophoresis. A difference was observed in the immunoelectrophoretic pattern of native and glycosylated glomerular basement membrane split products. A distinct increase of thiobarbituric acid assay positive glomerular basement membrane structures after incubation with glucose provides suggestive evidence for the occurrence of non-enzymatic glycosylation of glomerular basement membrane proteins. Glycosylated glomerular basement membrane proteins may contribute to both functional and morphological changes in diabetic glomerulosclerosis.
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PMID:Glycosylation of glomerular basement membrane in Type 1 (insulin-dependent) diabetic children. 715 60

From poly(vinyl alcohol) precursors, various reactive carriers for the immobilization of enzymes were synthesized. As insoluble starting polymers, the following products were used: poly(vinyl alcohol), gels crosslinked with terephthalaldehyde, hydrolyzed beads of crosslinked poly(vinyl acetate), poly(vinyl acetate-co- ethylene) tubes coated with poly(vinyl alcohol), and poly(vinyl alcohol)-containing synthetic pulp. Reactive groups introduced into these carriers or methods for their activation included the diazonium- and isothiocyanato group, and the glutardialdehyde-, BrCN, 2, 4, 6-trichloro-s-triazien, and p-benzoquinone methods. Furthermore, SH-specific reactive groups such as N-substituted maleimide groups or activated mixed disulfides with 2-thiopyridyl groups could be introduced into PVA-polymers. Enzymes like hydrolases (e.g. papain, trypsin, chymotrypsin, urease), oxidoreductases (e.g. glucose oxydase, catalase, glucose-6-phosphate dehydrogenase) as well as the example of transferase hexokinase coimmobilized with glucose-6-phosphate dehydrogenase, were immobilized by reactive poly(vinyl alcohol) carriers. The properties of the immobilized enzymes were investigated.
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PMID:Some new reactive polymers for the immobilization of enzymes. 741 95

The exocrine and endocrine pathophysiology of chronic calcific pancreatitis of the tropics (CCPT) remains elusive. The objective of this study was to evaluate the spectrum and correlates of the exocrine and endocrine pancreatic dysfunction in CCPT. Thirty-seven consecutive patients with a clinico-radiological diagnosis of CCPT were stratified into three subgroups: CCPT-normal glucose tolerance (NGT), CCPT-abnormal glucose tolerance (IGT) and CCPT-diabetes mellitus (DM). Ten ketosis resistant young diabetic (KRDY) patients, 10 classical insulin dependent diabetes mellitus (IDDM) patients and 18 healthy matched controls were included for comparison. Fecal chymotrypsin (FCT) levels and blood C-peptide levels (basal and post i.v. glucagon stimulation) were estimated for assessing the exocrine and endocrine pancreatic functions, respectively. Sonography was performed to evaluate the pancreatic size and ductal diameter. Pancreatic exocrine-endocrine correlation was examined by studying the C-peptide/fecal chymotrypsin ratio (CP/FCT) (CP/FCT of normal controls = 1). Mean FCT levels in all 3 subgroups of CCPT (NGT: 3.4 micrograms/g; IGT: 0.82 microgram/g; DM: 2.4 micrograms/g) were very low (87-96% reduction in exocrine pancreatic dysfunction; mean FCT in healthy controls was 22.8 micrograms/g) (P < 0.0001). In contrast, KRDY and IDDM patients displayed 50-54% reduction in pancreatic acinar function (P < 0.001). Basal and stimulated C-peptide levels progressively fell in the 3 CCPT subsets (NGT: 0.23 and 0.46 > IGT: 0.14 and 0.29 > DM 0.10 and 0.14) (P < 0.01). CCPT patients exhibited pancreatic atrophy and ductal dilation (> 3 mm).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chronic calcific pancreatitis of the tropics (CCPT): spectrum and correlates of exocrine and endocrine pancreatic dysfunction. 760 50

It is well known that oral administration of camostate induces hyperplasia and hypertrophy of the rat pancreas. It is not clear, however, whether pancreatic hormone and enzyme secretion are affected by camostate treatment. In rats, daily administration of 200 mg camostate/kg b. wt for 14 days significantly increased pancreatic weight and pancreatic content of DNA, protein, amylase, lipase, trypsin and chymotrypsin, as well as the amount of insulin, glucagon and somatostatin. In the intact animal, blood glucose levels and serum concentrations of insulin and glucagon in response to an oral glucose load were not impaired after camostate treatment. In the isolated perfused pancreas, however, insulin and glucagon secretions were reduced, whereas somatostatin release was not affected. The volume of pancreatic juice produced by the unstimulated isolated perfused organ, as well as protein and enzyme secretion, were increased after camostate treatment. Likewise, the isolated perfused pancreas from camostate-treated rats secreted a larger volume of pancreatic juice and more protein in response to cholecystokinin (CCK), while enzyme secretion was affected in a non-parallel manner: amylase release was markedly reduced, lipase release was unchanged, and release of trypsin and chymotrypsin was increased.
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PMID:Endocrine and exocrine pancreatic function after camostate-induced growth of the organ. 760 95

In order to isolate glucose-starvation-related cDNAs in maize (Zea mays L.) root tips, a cDNA library was constructed with poly(A)+ mRNA from 24 h starved root tips. After differential screening of the library, we isolated six different cDNAs (named pZSS2 and pZSS7) which were expressed during glucose starvation. Time course analysis revealed that maximum expression of five of these genes occurs 30 h after the onset of the starvation treatment. On the contrary, the expression of mRNAs corresponding to pZSS4 was maximal at an early stage of starvation and then dramatically decreased. The expression of this gene did not seem to be specific for glucose starvation. The pattern of induction of the genes corresponding to pZSS2, pZSS3, pZSS5, pZSS6 and pZSS7 revealed that non-metabolizable sugars such as L-glucose and mannitol induce mRNA transcription similarly to glucose starvation. When D-glucose or any other metabolizable sugar was supplied, the level of transcripts was reduced. Nucleotide sequence analyses of the six cDNAs allowed identification of five of them by comparison with sequence data bases. The protein encoded by clone pZSS2 is analogous to a wound-induced protein from barley. Clones pZSS4 to pZSS7 encode, respectively, a transmembrane protein, a cysteine protease, a metallothionein-like protein and a chymotrypsin/subtilisin-like protease inhibitor. Clone pZSS3 shares no significant homology with any known sequence.
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PMID:Molecular cloning and characterization of six cDNAs expressed during glucose starvation in excised maize (Zea mays L.) root tips. 763 17


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