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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1991-2-28
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pubmed:abstractText |
Certain heavy metal actions such as Cd2+ and Pb2+ mimic Ca2+ effectively in stimulating calmodulin (CaM). We now show that these cations also activate skeletal muscle troponin C (TnC), a Ca2(+)-binding protein highly homologous to CaM. Like Ca2+, these cations allow TnC to alter its electrophoretic mobility on polyacrylamide gels, and to bind to phenyl-Sepharose. Moreover, they activate TnC to stimulate myofibrillar ATPase. When TnC was removed from the skeletal myofibrils by treatment with trans-1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid (CDTA), the ATPase activity was no longer stimulated by the cations. However, after reconstitution of CDTA-treated skeletal myofibril with TnC, the response of ATPase to Ca2+, Cd2+ or Pb2+ was restored. These findings suggest that the activation of myofibrillar ATPase by Cd2+ and Pb2+ is mediated through TnC. The ability of the heavy metals to stimulate TnC-supported ATPase activity correlated quite well with the ability to increase the extent of the myofibrillar superprecipitation. The activation of TnC by Cd2+ or Pb2+ could constitute a possible molecular basis for their toxicity.
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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/Cadmium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Lead,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin C
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pubmed:status |
MEDLINE
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pubmed:issn |
0340-5761
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
490-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2148867-Adenosine Triphosphatases,
pubmed-meshheading:2148867-Animals,
pubmed-meshheading:2148867-Cadmium,
pubmed-meshheading:2148867-Calcium,
pubmed-meshheading:2148867-Calmodulin,
pubmed-meshheading:2148867-Enzyme Activation,
pubmed-meshheading:2148867-Lead,
pubmed-meshheading:2148867-Metals,
pubmed-meshheading:2148867-Muscle Proteins,
pubmed-meshheading:2148867-Myofibrils,
pubmed-meshheading:2148867-Rabbits,
pubmed-meshheading:2148867-Spectrometry, Fluorescence,
pubmed-meshheading:2148867-Troponin,
pubmed-meshheading:2148867-Troponin C
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pubmed:year |
1990
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pubmed:articleTitle |
Activation of troponin C by Cd2+ and Pb2+.
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pubmed:affiliation |
Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, TN 38101.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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