Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.3.5.5 (CPS)
 1,262 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Disulfide S-monoxide (DSMO) and disulfide S-dioxide (DSDO) have been proposed as proximal mediators for the oxidant-mediated modification of proteins. These disulfide S-oxides (DSOs) derived from glutathione (GSH) and captopril (CPSH) were synthesized by iron- or methyltrioxorhenium (VII)-catalyzed oxidation of the thiols with H2O2. Treatment of mouse hippocampal extracts with [35S]GS-DSOs revealed that a large number of proteins were susceptible to thionylation; however, only a limited number of the them were detectable by the commonly used antibody against GS-associated proteins. Using protein kinase C (PKC) as a model, we found that DSOs derived from different thiols modified this kinase with different efficacy and specificity; for example, the inhibitory potency of the kinase was glutathione disulfide S-dioxide (GS-DSDO) (IC50, approximately 30 microM) > captopril disulfide S-dioxide (CPS-DSDO) (IC50, approximately 450 microM) > glutathione disulfide S-monoxide (GS-DSMO) and captopril disulfide S-monoxide (CPS-DSMO). The stoichiometries of thionylation of PKC beta mediated by [35S]GS-DSMO and [35S]GS-DSDO were approximately 1 and 5 mol/mol, respectively, and at least four glutathionylation sites were identified in the GS-DSDO-treated kinase. Modification of PKC by GS-DSDO and CPS-DSDO rendered the kinase very susceptible to limited proteolysis; the former preferentially caused the degradation of the catalytic and the latter the regulatory domain of the kinase. Furthermore, CPS-DSDO-mediated modification of PKC increased the autonomous kinase activity; this was not the case for GS-DSDO-mediated modification. Since DSOs of different oxidative states as well as those derived from different thiols exert different effects on a target protein, these molecules could cause distinct cellular responses if derived from endogenous cellular reactions or even if they arise from exogenous sources.
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PMID:Modification of protein by disulfide S-monoxide and disulfide S-dioxide: distinctive effects on PKC. 1724 96

CPS [corn (Zea mays) peptides] were prepared from corn gluten meal by proteolysis with alcalase, an alkaline protease. The molecular-mass distribution of CPS is from 200 to 1000 Da as determined by MS. The amino acid composition of CPS was also analysed by HPLC. CPS contains almost no free amino acids. The protective effect of CPS against acute hepatic injuries induced by alcohol was verified in NH mice that were fed with different dosages of CPS for 30 days and subsequently given an acute dose of alcohol orally. As a result, CPS reduced both hepatic malondialdehyde and triacylglycerol levels, along with enhanced hepatic GSH (glutathione) levels, relative to the control. Hepatic histological changes were also observed. The result indicates that CPS is capable of attenuating ethanol-induced hepatic injury. The effect of CPS on removing superoxide anion in vitro was also studied as an additional proof that CPS is capable of abating hepatic superoxidant stress.
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PMID:Preparation of corn (Zea mays) peptides and their protective effect against alcohol-induced acute hepatic injury in NH mice. 1729 Nov 96