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)

Brain microtubules are found to disperse rods of skeletal muscle myosin and become decorated with amorphous aggregates of myosin. Then microtubules are partially depolymerized by myosin. Myosin shows high Mg2+-GTPase activity which is not influenced by microtubules, and induces the partial depolymerization of microtubules by exhaustion of GTP in the solution. H-meromyosin depolymerizes microtubules like myosin does. H-meromyosin is, however, contaminated with a trace amount of trypsin, which irreversibly depolymerizes microtubules.
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PMID:Depolymerization of brain microtubules by skeletal muscle myosin. 15 54

The rate of 32P incorporation into phospholipids of EHSVi transformed fibroblasts was studied by pulse experiments (2 hours) in cells which are detached from the support by trypsin and either maintained in suspension or replated and in the process of adhering. This is performed comparatively to cells in monolayers. Cells are taken during or after the log phase. Both global incorporation into phospholipids and, in the case of cells in log phase, percentage of incorporation into phosphatidylinositol are lowered, after detachment from the support, in suspended cells. They are stimulated by a new contact with the support. In the same conditions, percentages of incorporation into phosphatidylethanolamine and phosphatidylcholine remain at values they have in cells in monolayers. These values are characteristic of the physiological state of cells in monolayers, in relation with medium factors exhaustion.
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PMID:[32P incorporation into phospholipids of EHSVi transformed fibroblasts, with regard to adherence to the support]. 71 46

Secretion of trypsin, chymotrypsin, lipase and amylase was measured in male rats under urethane anaesthesia using a method of continuous perfusion of the duodenum. Prolonged infusion of cholecystokinin-pancreozymin (CCK-PZ) over a period lasting 200-360 min was administered either alone or together with a submaximal dose of secretin (1 unit/100 g - 10 min). Infusion of CCK-PZ was carried out using maximal doses (1--1.5 unit/100 g - 10 min) with and without secretin. Supramaximal doses of CCK-PZ (2 and 4 units/100 g - 10 min) were used only in combination with secretin. In all experiments secretion of enzymes showed a triphasic pattern including an initial peak followed by a plateau secretion after 10--20 min (phase 1), a decreasing second phase and finally base-line secretion (phase 3), thus demonstrating exhaustion of enzyme output from the gland with time. With increasing and supramaximal dose of CCK-PZ the cumulative output of enzymes from start to baseline secretion decreased progressively. Under the same conditions the levels of peak and plateau secretion were lower, the duration of plateau secretion was longer and the decreasing phase of secretion was shortened. These features indicate inhibition of secretion with increasing supramaximal doses of CCK-PZ infusion. Whereas the proteolytic enzymes and lipase reacted in a parallel way always amylase secretion was sustained on a higher level, implicating an alternative pathway for secretion.
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PMID:Effect of prolonged infusion of maximal and supramaximal doses of pancreozymin on pancreatic enzyme secretion in the rat--exhaustion or inhibition? 94 24

We previously documented both the spontaneous acceleration of growth hormone (GH) and prolactin (PRL) production by GH3 cells during perifusion and the suppression of their production during plate culture. We here present the role played by medium flow itself in this differential behavior. Increasing rates of perifusion flow (pump rates of 1 to 5 ml/h, equivalent to chamber flow rates of 0.19 to 1.3 microliters.min-1.mm-2 of cross-sectional area) were associated with enhanced GH and PRL secretion. Flow rate-dependent basal hormone secretion rates were established quickly and were stable for the first 10 to 14 h of perifusion. The previously documented independent, spontaneous, and continuously accelerating production of both hormones that followed during the subsequent 40 (PRL) to 60 (GH) h of perifusion was also shown to be flow-rate related. Any time the rate of medium flow was changed within an experiment, the rate of hormone secretion was modulated. However, that modulation did not interrupt ongoing flow-associated acceleration of hormone production once the latter had begun. In addition, GH3 cell product(s) from one cell column reversibly inhibited secretion from cells in a downstream column. The inhibition did not occur when cells in the downstream column had been exposed to trypsin. Other work had suggested that neither GH, PRL, insulinlike growth factor-I, leucine, nor nutrient exhaustion were responsible for the effect. These data are consistent with autocrine-paracrine feedback regulation of GH3 cells by a secretory product(s). Feedback would thus provide a mechanism to effect flow-rate-dependent modulation of GH and PRL release, and to explain accelerating hormone production during perifusion.
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PMID:Medium flow rate modulates autocrine-paracrine feedback of GH and PRL release by perifused GH3 cells. 235 41

Determination of antitryptic activity of blood serum and exudate in patients with tuberculous pleurisy revealed that concentrations of trypsin inhibitors were significantly increased while their activity was markedly decreased (2-3-fold) in the exudate. This indicated exhaustion of the adaptation mechanisms in the inflammatory areas, which required their local correction. Intrapleural administration of contrical increased the body's protective and adaptation potentials and treatment efficiency such as shorter times of intoxication and pleural exudation and less frequency of pronounced concomitant pleural lesions.
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PMID:[The clinical value of determining the general antitrypsin activity of the blood and exudate in tuberculous pleurisy]. 247 69

The effects of bilateral nephrectomy or a sham operation on plasma angiotensinogen and on the different kininogens were studied in the rat. Total plasma kininogen was measured by RIA of kinins after trypsin hydrolysis. In addition, the high molecular weight (HMW) kininogen and the low molecular weight (T)-kininogen were specifically quantified by using direct RIAs. Angiotensinogen was measured by RIA of angiotensin I after exhaustion by renin. Three groups of control, nonoperated, bilaterally nephrectomized and sham-operated rats were studied in each experiment. Twenty-four hours after either a bilateral nephrectomy or a sham operation total plasma kininogen was elevated approximately 5 times when compared to control rats. Time course measurements from 0 to 48 h in 3 other groups of control, bilaterally nephrectomized and sham-operated rats demonstrated that kininogen gradually increased at 12, 24, and 48 h after the surgery and that the elevation observed in plasma kininogen appeared to be entirely due to an increase in T-kininogen levels. There was no difference in T-kininogen levels between bilaterally nephrectomized and sham-operated animals. By contrast HMW kininogen was neither influenced by surgery nor by nephrectomy. Angiotensinogen increased more than 8 times in bilaterally nephrectomized rats but displayed only little changes in sham-operated animals. During the course of this experiment it was observed that also in control animals submitted to repeated skin incision and venipuncture for blood sampling at the jugular vein, T-kininogen increased dramatically in plasma, but reached values lower than in sham-operated or bilaterally nephrectomized rats. In a third experiment performed in normal rats it was found that T-kininogen levels were more than 3 times elevated over initial values 24 h after a single blood sampling at the jugular vein. These results indicate that T-kininogen but not HMW kininogen is very sensitive to surgery, perhaps as a result of increased T-kininogen synthesis due to an inflammatory reaction. The T-kininogen might participate in the inflammatory reaction that occurs at the site of tissue injury and in the healing process. As there was no difference in T-kininogen, and in HMW kininogen levels between bilaterally nephrectomized and sham-operated rats, the kidneys do not seem to play an important role in the regulation of plasma kininogens. Angiotensinogen, HMW kininogen, and T-kininogen are therefore regulated separately after nephrectomy or surgery.
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PMID:Differential effects of nephrectomy and surgery on plasma kininogens and angiotensinogen in the rat. 337 Dec 63

Streptomyces exfoliatus SMF13 sequentially produced leupeptin, leupeptin-inactivating enzyme (LIE) and trypsin-like protease (TLP). TLP was produced upon exhaustion of glucose. Autolysis of mycelium was accompanied by an increase in TLP activity. However, in three bld mutants isolated from S. exfoliatus SMF13 after UV-mutagenesis, mycelium autolysis did not occur, and neither LIE nor TLP was produced, although leupeptin was produced. Production of both LIE and TLP was restored in a spontaneous Spo+ revertant of a bld mutant. In contrast, two whi mutants sequentially produced leupeptin, LIE and TLP. The molecular mass of TLP produced during morphological differentiation was estimated to be 31.8 kDa by SDS-PAGE. The N-terminal amino acid sequence was RVGGTxAAQGNFPFQQxLSM. TLP was competitively inhibited by leupeptin; the inhibition constant was 0.015 microM. TLP effectively hydrolysed the mycelial protein extract of S. exfoliatus SMF13, but the hydrolytic activity was inhibited by leupeptin. It was concluded that morphological differentiation and production of TLP are coordinately regulated, that TLP may function as an enzyme in the metabolism of mycelial proteins, and that the hydrolytic activity of TLP is regulated by autogenous leupeptin in S. exfoliatus SMF13.
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PMID:Trypsin-like protease of Streptomyces exfoliatus SMF13, a potential agent in mycelial differentiation. 875 42

H+,K+-ATPase preparations from pig stomach were modified with a sulfhydryl fluorescence reagent, N-[p-(2-benzimidazolyl)phenyl] maleimide (BIPM). The addition of ATP to the modified enzyme preparations in the presence of Mg2+ decreased the BIPM fluorescence but increased the Trp fluorescence. After exhaustion of ATP, the fluorescence intensities increased and decreased to the original levels, respectively. The results of stopped flow and rapid quenching experiments suggested that the decrease in BIPM fluorescence (36/s) was accompanied by binding of Mg2+ and ATP or phosphorylation (35 36/s) which was followed by slower increases in Trp fluorescence (24/s) and light scattering (20/s). Tosylphenylalanyl chloromethyl ketone-trypsin treatment of the modified preparations, which showed an about 1% decrease in BIPM fluorescence accompanying phosphorylation, gave one major fluorescent peptide peak on reverse-phase chromatography. Amino acid sequence analysis of the peptide revealed the following sequence, Ser-Pro-Glu-X-Thr-His-Glu-Ser-Pro-Leu-Glu-Thr-Arg. On comparison with the amino acid sequence deduced from cDNA from pig stomach [Maeda, M., Ishizaki, J., and Futai, M. (1988) Biochem. Biophys. Res. Commun. 157, 203-209], X was shown to correspond to Cys241 of the alpha-chain in H+,K+-ATPase. These data and others suggest that the decrease in BIPM fluorescence at Cys241 reflects some molecular event triggered by the binding of ATP with Mg2+ and/or phosphorylation, whereas the increases in the intrinsic Trp fluorescence and light scattering reflect one after phosphorylation.
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PMID:ATP-induced dynamic fluorescence changes of a N-[p-(2-benzimidazolyl)phenyl]maleimide probe at Cys241 in the alpha-chain of pig stomach H+,K+-ATPase. 934 99

The plasma globulins which produce the vasoactive polypeptides, bradykinin, kallidin and angiotensin, have been compared. After incubation of plasma with kallikrein and exhaustion of its kallidinogen, subsequent incubation with trypsin did not result in formation of bradykinin, showing that bradykininogen had also been exhausted and suggesting that kallikrein and trypsin use the same substrate. Kallidin and bradykinin formation was not prevented by acid-treatment of plasma, though heat-denatured substrate produced kallidin less readily. Kallikrein could exhaust plasma bradykininogen without affecting levels of angiotensinogen. Following nephrectomy of dogs, plasma angiotensinogen levels rose whereas bradykininogen levels did not. These results confirm the belief that bradykininogen differs from angiotensinogen but not from kallidinogen.
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PMID:BRADYKININOGEN, ANGIOTENSINOGEN AND KALLIDINOGEN. 1408 56

Because consumption of whey protein hydrolysates is on the increase, the possibility that prolonged ingestion of whey protein hydrolysates affect the digestive system of mammals has prompted us to evaluate the enzymatic activities of pepsin, leucine-aminopeptidase, chymotrypsin, trypsin, and glutaminase in male Wistar rats fed diets containing either a commercial whey isolate or a whey protein hydrolysate with medium degree of hydrolysis and to compare the results with those produced by physical training (sedentary, sedentary-exhausted, trained, and trained-exhausted) in the treadmill for 4 weeks. The enzymatic activities were determined by classical procedures in all groups. No effect due to the form of the whey protein in the diet was seen in the activities of pepsin, trypsin, chymotrypsin, and leucine-aminopeptidase. Training tended to increase the activity of glutaminase, but exhaustion promoted a decrease in the trained animals, and consumption of the hydrolysate decreased it even further. The results are consistent with the conclusion that chronic consumption of a whey protein hydrolysate brings little or no modification of the proteolytic digestive system and that the lowering of glutaminase activity may be associated with an antistress effect, counteracting the effect induced by training in the rat.
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PMID:Prolonged ingestion of prehydrolyzed whey protein induces little or no change in digestive enzymes, but decreases glutaminase activity in exercising rats. 2048 82


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