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:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Quiescent, contact inhibited H-35 rat hepatoma cell cultures maintained in minimal essential medium contain a very low level of ornithine decarboxylase activity. However, 2 h after the addition of 10% fetal calf serum to the culture medium, the enzyme activity increases by approx. 100-fold. This increase can be completely inhibited by the simultaneous addition of 10(-2) M putrescine. The presence of putrescine elicits the appearance of an intracellular inhibitor of ornithine decarboxylase. This inhibitor of ornithine decarboxylase has a molecular weight of 26500, is sensitive to the action of chymotrypsin and is noncompetitive with respect to ornithine. The intracellular appearance of this inhibitor is sensitive to cycloheximide but is only partially inhibited by actinomycin D.
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PMID:The appearance of an ornithine decarboxylase inhibitory protein upon the addition of putrescine to cell cultures. 17 75

1,4-Diaminobutanone, a competitive inhibitor of ornithine decarboxylase in Aspergillus nidulans, is able to increase the half-life of this enzyme and thus stimulate an increase in its activity in vivo. It also protects ornithine decarboxylase against proteolysis by chymotrypsin in vitro.
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PMID:The effect of 1,4-diaminobutanone on the stability of ornithine decarboxylase from Aspergillus nidulans. 33 10

The ornithine decarboxylase-inducing factor (ODC factor) was purified about 1,000-fold in 42% yield from the ascites fluids of an Ehrlich ascites tumor by a combination of centrifugation and concanavalin A (ConA) treatment. A single ip injection of 0.5 micrograms of the purified factor per mouse resulted in half-maximum induction of liver ODC. The factor was found to be a trypsin- and chymotrypsin-resistant, acidic glycoprotein (pI about 4.43) with a minimum molecular weight of about 70 kilodaltons, containing a disulfide bond(s) in its functional domain. It did not react with ConA. This factor induced retrodifferentiation of liver function, causing a marked increase of prototype M2 isozyme of pyruvate kinase. It reduced liver catalase activity, and also modified thyroid hormone metabolism, reducing the serum levels of T4 and T3. These results suggest that the ODC factor is multifunctional and induces many of the changes observed in a tumor-bearing host.
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PMID:Purification of ornithine decarboxylase-inducing factor from cell-free ascites fluid of Ehrlich ascites tumor and its characteristics. 170 56

We examined the role of physiologic plasma concentrations of cholecystokinin (CCK) in the regulation of rat pancreatic gene expression. Postprandial plasma CCK concentrations, as determined by bioassay, were achieved by intraduodenal perfusion with soybean trypsin inhibitor (SBTI) or intravenous infusion of CCK-8. SBTI administration for 48h resulted in nonparallel regulation of digestive enzyme gene expression, as assessed by slot-blot analysis using cloned cDNA probes for trypsin, chymotrypsin, amylase and ribonuclease. As an indicator for pancretic growth stimulation, ornithine decarboxylase (ODC) gene expression was stimulated appr. 2-fold over the SBTI infusion period. Identical effects were seen with i.v. infusion of CCK-8. The CCK receptor antagonist L-364, 718 blocked the effects on pancreatic gene expression of both CCK infusion and SBTI administration. These data therefore indicate that postprandial plasma CCK concentrations regulate pancreatic digestive enzyme and ODC gene expression at a pretranslational level.
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PMID:Cholecystokinin as a regulator of rat pancreatic gene expression. 171 83

The current study examines the effects of alpha-difluoromethylornithine (DFMO), an irreversible ornithine decarboxylase inhibitor, on pancreatic growth and development of rat neonates. Newborn rats were given daily subcutaneous injections of 300 or 500 mg kg-1 DFMO and killed after 7, 14, 21, and 28 days of treatment. Pancreatic weights and DNA, RNA, protein, amylase and chymotrypsin total contents (per pancreas) and concentrations were evaluated at the end of each period. Inhibition of body weight gain (30%) was maximal after 14 days of the 500 mg DFMO treatment. Pancreatic weight increase of 20% was significant after 7 days of the 300 mg DFMO treatment while deficits of 15, 20, and 14% were significant after 21 days of 300 mg DFMO and 14 and 21 days of 500 mg DFMO. Total DNA was already subnormal after one week of 500 mg DFMO with a maximal reduction of 30% after 28 days while a significant decrease of 15% was observed only after 3 weeks of 300 mg DFMO. Pancreatic hypertrophy was observed after 7 and 28 days of the 500 mg and after 14 days of the 300 mg DFMO treatment. Chymotrypsin total contents and concentrations were always preferentially affected over those of amylase. These data support the view that ornithine decarboxylase (ODC) and polyamines play an important role in cell replication and growth of the pancreatic tissue during the neonatal period.
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PMID:Implication of ornithine decarboxylase and polyamines in pancreatic growth of neonatal rats. 311 41

The ability of an extract derived from Triticum vulgare, the common wheat plant, to stimulate cellular proliferation of mouse 3T3 fibroblast cells was investigated. Cellular response to Triticum extract (TE) was most evident in sparse cultures made quiescent by growing cells on low concentrations (0.6%) of calf serum. The growth-promoting activity in the extract was lost after dialysis but was resistant to heat treatment and digestion with trypsin or chymotrypsin, suggesting a low-molecular-weight non-protein substance(s). Growth-curve experiments showed that TE was capable of supporting continuous cell division. Cellular proliferation showed a dose-dependent response in the range of 2%-10% TE, and addition of 10% TE to cell culture medium caused a level of cell-growth stimulation approximately 72% that of 20 ng/ml fibroblast growth factor (FGF). Measurement of ornithine decarboxylase (ODC) activity of 3T3 cells after addition of 10% TE showed a significant rise in the specific activity of the enzyme.
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PMID:Stimulation of cell division in mouse fibroblast line 3T3 by an extract derived from Triticum vulgare. 374 20

The role of ornithine decarboxylase and of polyamines was investigated on caerulein-induced pancreatic growth by the use of alpha-difluoromethylornithine (DFMO), an enzyme-activated irreversible inhibitor of ornithine decarboxylase. By itself, DFMO did not affect the pancreatic gland at all but when combined with caerulein, it reduced the increases in DNA synthesis and DNA content initiated by the cholecystokinin analog. The general hypertrophic action of caerulein was not affected by DFMO but specific increases in amylase and chymotrypsin concentrations were observed after 2 days of caerulein. The effect on amylase concentration was further increased after 4 days but that on chymotrypsin was reversed, showing a significant decrease. These data suggest that the polyamines might be involved in pancreatic growth that is stimulated by caerulein and that their action could be mainly oriented towards cellularity. The specific decreases obtained in DNA synthesis and content brought about by DFMO support this observation.
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PMID:Effects of alpha-difluoromethylornithine on pancreatic growth induced by caerulein. 608 57

The time required to induce two inducible hepatic enzymes, ornithine decarboxylase (ODC) and tyrosine aminotransferase (TAT), by growth hormone and dexamethasone, respectively, increases with age. Specific activity at the peak of induction is the same for all ages. On the other hand, for basal TAT the specific activity per unit of TAT antigen was found to decrease considerably with age. The half-life of ODC was determined after cycloheximide administration. The apparent half-life at the peak of ODC induction increases from 15 minutes in 3-4-month-old mice to 30 minutes in 24-month-old animals. Loss of efficiency in the protein degradation system is implicated in this phenomenon as no apparent differences could be observed in the susceptibility of ODC and TAT from young or old mice to chymotrypsin. ODC and TAT are activated by temperatures of up to 37 degrees C and 50 degrees C, respectively. ODC is inactivated at 50 degrees C while TAT is inactivated at 76 degrees C. "Young" ODC and TAT are more readily activated or inactivated by heating than the "old" enzymes.
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PMID:Age-related changes in inducible mouse liver enzymes: ornithine decarboxylase and tyrosine aminotransferase. 610 55

Histidine 57 of the catalytic triad of trypsin was replaced with alanine to determine whether the resulting variant would be capable of substrate-assisted catalysis [Carter, P., & Wells, J. A. (1987) Science 237, 394-9]. A 2.5-fold increase in kcat/Km was observed on tri- or tetrapeptide substrates containing p-nitroanilide leaving groups and histidine at P2. In contrast, hydrolysis of peptide substrates extending from P6 to P6' is improved 70-300-fold by histidine in the P2 or P1' position. This preference creates new protease specificities for sequences HR decreases, R decreases H, HK decreases, and K decreases H. The ability of histidine from either the P2 or the P1' position of substrate to participate in catalysis emphasizes the considerable variability of proteolytically active orientations which can be assumed by the catalytic triad. Trypsin H57A is able to hydrolyze fully folded ornithine decarboxylase with complete specificity at a site containing the sequence HRH. Trypsin H57A was compared to enteropeptidase in its ability to cleave a propeptide from trypsinogen. Trypsin H57A cleaved the propeptide of a variant trypsinogen containing an introduced FPVDDDHR cleavage site only 100-fold slower than enteropeptidase cleaved trypsinogen. The selective cleavage of folded proteins suggests that trypsin H57A can be used for specific peptide and protein cleavage. The extension of substrate-assisted catalysis to the chymotrypsin family of proteolytic enzymes indicates that it may be possible to apply this strategy to a wide range of serine proteases and thereby develop various unique specificities for peptide and protein hydrolysis.
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PMID:Trypsin specificity increased through substrate-assisted catalysis. 754 82

Trypanosoma brucei ornithine decarboxylase was reconstituted by coexpression of two polypeptides corresponding to residues 1-305 and residues 306-425 in Escherichia coli. The two peptides were coexpressed, at wild-type levels, from a single transcriptional unit that was separated by a 15-nucleotide untranslated region containing a ribosome binding site. The fragmented enzyme was purified and analyzed. The N- and C-terminal peptides are tightly associated into a fully active tetramer which has the same molecular weight as the native dimer. The kinetic constants (Km and kcat) measured for the decarboxylation of ornithine are identical to those obtained for the wild-type enzyme. These results suggest that the enzyme is organized into two structural domains, with a domain boundary in the region of amino acid 305. In contrast, the individual N- and C-terminal peptides are expressed primarily as inclusion bodies. Small quantities of soluble N-terminal peptide could be purified. This truncated protein is capable of inhibiting the wild-type enzyme, suggesting that it is folded into a native-like structure. Limited proteolysis with trypsin or chymotrypsin identifies a likely surface loop at amino acids 160-170, present in both the mouse and T. brucei enzyme, which positions one or more functionally important active site residues (e.g., Lys169). Kinetic analysis of a chimeric enzyme composed of T. brucei and mouse ornithine decarboxylase suggests that the substrate carboxylate binding determinant is located between residues 1 and 170.
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PMID:Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase. 757 30


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