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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1983-5-27
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pubmed:abstractText |
Islet cell plasma membranes contain a calcium-stimulated and magnesium-dependent ATPase (Ca2+ + Mg2+)-ATPase) which requires calmodulin for maximum enzyme activity (Kotagal, N., Patke, C., Landt, M., McDonald, J., Colca, J., Lacy, P., and McDaniel, M. (1982) FEBS Lett. 137, 249-252). Investigations indicated that exogenously added calmodulin increases the velocity and decreases the Km for Ca2+ of the high affinity (Ca2+ + Mg2+)-ATPase. These studies routinely employed the chelator ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) to maintain Ca2+ concentrations in the submicromolar range. During the course of these investigations, it was found unexpectedly that increasing the concentrations of EGTA (0.1-4 mM) and total calcium in the media, while maintaining constant free Ca2+ levels, increased the velocity of the high affinity (Ca2+ + Mg2+)-ATPase. The free calcium concentrations under these conditions were verified by a calcium-sensitive electrode. The (Ca2+ + Mg2+)-ATPase maximally activated by 2-4 mM EGTA was not further stimulated by calmodulin, whereas camodulin stimulation increased as the concentration of EGTA in the media was decreased. A similar enhancement by Ca-EGTA was observed on active calcium transport by the plasma membrane-enriched fraction. Moreover, Ca-EGTA had a negligible effect on both active calcium transport as well as Ca2+-stimulated ATPase activity by the islet cell endoplasmic reticulum, processes which are not stimulated by calmodulin. The results indicate that stimulation by Ca-EGTA may be used to differentiate calcium transport systems by these subcellular organelles. Furthermore, the concentration of EGTA routinely employed to maintain free Ca2+ levels may itself obscure effects of calmodulin and other physiological agents on calcium-dependent activities.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylene Glycols
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4808-13
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:6131899-Animals,
pubmed-meshheading:6131899-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:6131899-Calcium,
pubmed-meshheading:6131899-Calcium-Binding Proteins,
pubmed-meshheading:6131899-Calcium-Transporting ATPases,
pubmed-meshheading:6131899-Calmodulin,
pubmed-meshheading:6131899-Cell Membrane,
pubmed-meshheading:6131899-Dose-Response Relationship, Drug,
pubmed-meshheading:6131899-Egtazic Acid,
pubmed-meshheading:6131899-Enzyme Activation,
pubmed-meshheading:6131899-Ethylene Glycols,
pubmed-meshheading:6131899-Islets of Langerhans,
pubmed-meshheading:6131899-Male,
pubmed-meshheading:6131899-Rats,
pubmed-meshheading:6131899-Rats, Inbred Strains
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pubmed:year |
1983
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pubmed:articleTitle |
Activation of an islet cell plasma membrane (Ca2+ + Mg2+)-ATPase by calmodulin and Ca-EGTA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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