Linked Life Data

1764103

Source:http://linkedlifedata.com/resource/pubmed/id/1764103

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pubmed-article:1764103pubmed:abstractTextCalmodulin plays an important role in regulating cell proliferation and intranuclear processes (J. Biol. Chem. 265: 18595, 1990). Therefore we studied the association of 125I-calmodulin with highly purified rat hepatocyte nuclear preparations which were characterized by marker enzymes and electron microscopy. Steady-state association of 125I-calmodulin was reached within 5 minutes. Half-maximal binding was achieved at approximately 7.1 microM. This association was partially Ca(2+)-dependent, but was not influenced by ATP, GTP or wheat germ agglutinin. Ultrastructural autoradiography showed specific association of 125I-calmodulin with peripheral and non-peripheral heterochromatin, nuclear membranes, and nucleoli. Specific binding (ratio of the grain density of 125I-calmodulin to Na125I) was greatest in the regions of the nucleoli and non-peripheral heterochromatin. The data indicate that exogenous calmodulin can associate with specific nuclear components in an energy-independent and Ca(2+)-dependent manner.lld:pubmed
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pubmed-article:1764103pubmed:authorpubmed-author:McDonaldJ MJMlld:pubmed
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pubmed-article:1764103pubmed:pagination1548-56lld:pubmed
pubmed-article:1764103pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:1764103pubmed:articleTitleAssociation of calmodulin with isolated nuclei from rat hepatocytes.lld:pubmed
pubmed-article:1764103pubmed:affiliationDepartment of Pathology, Washington University School of Medicine, St. Louis, MO 63110.lld:pubmed
pubmed-article:1764103pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1764103pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:1764103pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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