pubmed-article:2530215 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:2530215 | lifeskim:mentions | umls-concept:C0056801 | lld:lifeskim |
pubmed-article:2530215 | pubmed:issue | 30 | lld:pubmed |
pubmed-article:2530215 | pubmed:dateCreated | 1989-11-27 | lld:pubmed |
pubmed-article:2530215 | pubmed:abstractText | The mycotoxin, cyclopiazonic acid (CPA), inhibits the Ca2+-stimulated ATPase (EC 3.6.1.38) and Ca2+ transport activity of sarcoplasmic reticulum (Goeger, D. E., Riley, R. T., Dorner, J. W., and Cole, R. J. (1988) Biochem. Pharmacol. 37, 978-981). We found that at low ATP concentrations (0.5-2 microM) the inhibition of ATPase activity was essentially complete at a CPA concentration of 6-8 nmol/mg protein, indicating stoichiometric reaction of CPA with the Ca2+-ATPase. Cyclopiazonic acid caused similar inhibition of the Ca2+-stimulated ATP hydrolysis in intact sarcoplasmic reticulum and in a purified preparation of Ca2+-ATPase. Cyclopiazonic acid also inhibited the Ca2+-dependent acetylphosphate, p-nitrophenylphosphate and carbamylphosphate hydrolysis by sarcoplasmic reticulum. ATP protected the enzyme in a competitive manner against inhibition by CPA, while a 10(5)-fold change in free Ca2+ concentration had only moderate effect on the extent of inhibition. CPA did not influence the crystallization of Ca2+-ATPase by vanadate or the reaction of fluorescein-5'-isothiocyanate with the Ca2+-ATPase, but it completely blocked at concentrations as low as 1-2 mol of CPA/mol of ATPase the fluorescence changes induced by Ca2+ and [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) in FITC-labeled sarcoplasmic reticulum and inhibited the cleavage of Ca2+-ATPase by trypsin at the T2 cleavage site in the presence of EGTA. These observations suggest that CPA interferes with the ATP-induced conformational changes related to Ca2+ transport. The effect of CPA on the sarcoplasmic reticulum Ca2+-ATPase appears to be fairly specific, since the kidney and brain Na+,K+-ATPase (EC 3.6.1.37), the gastric H+,K+-ATPase (EC 3.6.1.36), the mitochondrial F1-ATPase (EC 3.6.1.34), the Ca2+-ATPase of erythrocytes, and the Mg2+-activated ATPase of T-tubules and surface membranes of rat skeletal muscle were not inhibited by CPA, even at concentrations as high as 1000 nmol/mg protein. | lld:pubmed |
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pubmed-article:2530215 | pubmed:language | eng | lld:pubmed |
pubmed-article:2530215 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2530215 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2530215 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2530215 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2530215 | pubmed:month | Oct | lld:pubmed |
pubmed-article:2530215 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2530215 | pubmed:author | pubmed-author:MartonosiAA | lld:pubmed |
pubmed-article:2530215 | pubmed:author | pubmed-author:JonaII | lld:pubmed |
pubmed-article:2530215 | pubmed:author | pubmed-author:SeidlerN WNW | lld:pubmed |
pubmed-article:2530215 | pubmed:author | pubmed-author:VegaTT | lld:pubmed |
pubmed-article:2530215 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2530215 | pubmed:day | 25 | lld:pubmed |
pubmed-article:2530215 | pubmed:volume | 264 | lld:pubmed |
pubmed-article:2530215 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2530215 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2530215 | pubmed:pagination | 17816-23 | lld:pubmed |
pubmed-article:2530215 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:2530215 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2530215 | pubmed:articleTitle | Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum. | lld:pubmed |
pubmed-article:2530215 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, State University of New York Health Science Center, Syracuse 13210. | lld:pubmed |
pubmed-article:2530215 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2530215 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2530215 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2530215 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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