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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1992-2-12
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pubmed:abstractText |
Triorganotins have been reported to affect heme metabolism as well as the cardiovascular system. Our recent studies indicated that these organotins inhibit cardiac sarcoplasmic reticulum Ca(2+)-transport and cAMP-stimulated phosphorylation of specific proteins involved in Ca2+ transport, suggesting their interference with cardiac adrenergic function. The present study determines the effect of three organotins--tributyltin bromide (TBT), triethyltin bromide (TET) and trimethyltin chloride (TMT)--on rat cardiac ATPases and catecholamine binding, since these phenomena are involved in cardiac function. Cardiac membrane fraction was prepared from heart ventricles of male Sprague-Dawley rats. All three organotins inhibited cardiac Na+,K(+)-ATPase, [3H]ouabain binding, K(+)-activated p-nitrophenyl phosphatase (K(+)-PNPPase) and oligomycin-sensitive (OS) and oligomycin-insensitive (OI) Mg(2+)-ATPase in a concentration-dependent manner. K(+)-PNPPase was less sensitive to these triorganotins when compared to Na+K(+)-ATPase, suggesting that triorganotins affect the Na(+)-pump activity by acting on the Na(+)-dependent phosphorylation process. OS Mg(2+)-ATPase was more sensitive to these organotins when compared to OI Mg(2+)-ATPase, confirming their potent effect on the enzymes of oxidative phosphorylation. The order of potency is TBT greater than TET greater than TMT. TET and TMT, but not TBT, inhibited [3H]norepinephrine and [3H]dopamine binding to cardiac membranes in a concentration-dependent manner, the effect being more with TET. These results suggest that triorganotins inhibit sodium pump activity as well as ATP synthesis. Since Na+,K(+)-ATPase is involved in the active transport of catecholamines, triorganotins not only inhibited the catecholamine transport but also to some extent affected catecholamine binding, thus interfering with cardiac function.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Catecholamines,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Trialkyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Triethyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Trimethyltin Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/tributyltin,
http://linkedlifedata.com/resource/pubmed/chemical/triethyltin,
http://linkedlifedata.com/resource/pubmed/chemical/trimethyltin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0260-437X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
403-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1662243-Adenosine Triphosphatases,
pubmed-meshheading:1662243-Animals,
pubmed-meshheading:1662243-Catecholamines,
pubmed-meshheading:1662243-Heart,
pubmed-meshheading:1662243-Male,
pubmed-meshheading:1662243-Myocardium,
pubmed-meshheading:1662243-Rats,
pubmed-meshheading:1662243-Rats, Inbred Strains,
pubmed-meshheading:1662243-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:1662243-Trialkyltin Compounds,
pubmed-meshheading:1662243-Triethyltin Compounds,
pubmed-meshheading:1662243-Trimethyltin Compounds
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pubmed:year |
1991
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pubmed:articleTitle |
Triorganotin inhibition of rat cardiac adenosine triphosphatases and catecholamine binding.
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pubmed:affiliation |
Department of Biology, Jackson State University, MS 39217.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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