Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0024591 (malignant hyperthermia)
 2,353 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pigs, crossbreeds of Swedish Landrace and Yorkshire, about 6 months old and susceptible to develop malignant hyperthermia when exposed to halothane, were subjected to a 12-min experimental stress provoked by the myorelaxant succinylcholine. The experimental pigs were pre-treated before the stress: five were given propranolol for one week, six were given alpha-tocopherol (vitamin E) combined with selenium for 11 days, and five pigs were pre-treated with zinc (ZnSO4) for 1 month. A total of 12 untreated, stress-susceptible pigs served as controls. The blood levels of noradrenaline and adrenaline recorded during the stress were significantly reduced in the groups pre-treated with propranolol or alpha-tocopherol combined with selenium. The results show significant reduction of myocardial necrosis by beta-adrenoceptor-blocking agents and free-radical scavengers during stress-induced increased sympathetic activity.
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PMID:Reduction of heart lesions after experimental restraint stress: a study in stress-susceptible pigs. 765 10

The protease prostate-specific antigen (PSA) is a marker widely used clinically for monitoring prostatic malignancies. Under normal conditions, this enzyme is mainly involved in the post ejaculation degradation of the major human seminal protein, the seminal plasma motility inhibitor precursor/semenogelin I (SPMIP/SgI), which is the predominant protein component of human semen coagulum. PSA primary structure and activity on synthetic substrates predict a chymotrypsin-like activity whose specificity remains to be established. The present study was aimed at characterizing the proteolytic processing of the SPMIP/SgI by PSA. Purified SPMIP/SgI was incubated with PSA in the presence or absence of protease inhibitors. General serine protease inhibitors, heavy metal cations (Zn2+ and Hg2+), and the heavy metal chelator 1,10-phenanthroline partially or totally inhibited the proteolytic activity of PSA toward SPMIP/SgI. Under identical conditions, other proteins, such as bovine serum albumin, ovalbumin, and casein, were very poor substrates for PSA. Hydrolysis products were separated by reverse-phase high-performance liquid chromatography, assayed for sperm motility inhibitory activity, and analyzed by immunoblotting and mass spectrometry. The region responsible for the sperm motility inhibitory activity and containing an SPMI antiserum epitope was localized to the N-terminal portion of the molecule between residues 85 and 136. On the other hand, a monoclonal antibody against a seminal vesicle-specific antigen (MHS-5) recognized fragments derived from the central part of the SPMIP/SgI (residues 198-223). PSA hydrolysis occurred almost exclusively at either leucine or tyrosine residues, demonstrating directly for the first time a restricted chymotrypsin-like activity on a physiological substrate. The results suggest that PSA is the main enzyme responsible for the processing of SPMIP/SgI in human semen and that this protease manifests unusual specificity with respect to hydrolyzable substrates and sites of hydrolysis.
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PMID:Characterization of prostate-specific antigen proteolytic activity on its major physiological substrate, the sperm motility inhibitor precursor/semenogelin I. 909 10