| pubmed-article:10378480 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0014792 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:10378480 | lifeskim:mentions | umls-concept:C2346521 | lld:lifeskim |
| pubmed-article:10378480 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:10378480 | pubmed:dateCreated | 1999-7-6 | lld:pubmed |
| pubmed-article:10378480 | pubmed:abstractText | Recent investigations suggest that Ca2(+)-ATPase from fish gills is very sensitive to Zn2+ (Hogstrand et al., 1996. Am. J. Physiol. 270, R1141-R1147). The effect of free Zn2+ ion on the human erythrocyte plasma membrane Ca2(+)-ATPase was investigated to explore the possible extension of this finding to humans. Membrane vesicles were prepared and the Ca2(+)-ATPase activity was measured as Ca2(+)-stimulated ATP hydrolysis and as ATP-dependent Ca2+ transport. The Zn2+ ion inhibited the erythrocyte Ca2(+)-ATPase by reducing Vmax and increasing the K0.5. While in the Ca2+ transport assay only the Vmax was affected at lower Zn2+ concentrations (50-100 pM), reduction of Vmax was always accompanied by an affinity decrease in the ATP hydrolysis assay. The Ca2(+)-ATPase was found to be inhibited by Zn2+ at extremely low concentrations. The IC10 and IC50 for Zn2+, at a Ca2+ concentration of 1.0 microM, were estimated at 4 and 80 pM, respectively. Although the Ca2(+)-ATPase might be more sensitive in vitro than in vivo conditions, the results suggest that physiological concentrations of Zn2+ may reduce the activity of the erythrocyte Ca2(+)-ATPase. Furthermore, disturbance of Ca homeostasis may be a mechanism causing Zn toxicity during exposure. | lld:pubmed |
| pubmed-article:10378480 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10378480 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10378480 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10378480 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10378480 | pubmed:issn | 0300-483X | lld:pubmed |
| pubmed-article:10378480 | pubmed:author | pubmed-author:Wendelaar... | lld:pubmed |
| pubmed-article:10378480 | pubmed:author | pubmed-author:HogstrandCC | lld:pubmed |
| pubmed-article:10378480 | pubmed:author | pubmed-author:VerbostP MPM | lld:pubmed |
| pubmed-article:10378480 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10378480 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10378480 | pubmed:volume | 133 | lld:pubmed |
| pubmed-article:10378480 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10378480 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10378480 | pubmed:pagination | 139-45 | lld:pubmed |
| pubmed-article:10378480 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
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| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
| pubmed-article:10378480 | pubmed:meshHeading | pubmed-meshheading:10378480... | lld:pubmed |
| pubmed-article:10378480 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10378480 | pubmed:articleTitle | Inhibition of human erythrocyte Ca2+-ATPase by Zn2+. | lld:pubmed |
| pubmed-article:10378480 | pubmed:affiliation | T.H. Morgan School of Biological Sciences, University of Kentucky, Lexington 40506-0225, USA. hogstra@pop.uky.edu | lld:pubmed |
| pubmed-article:10378480 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10378480 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10378480 | lld:pubmed |
