Linked Life Data

1764103

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

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-2-7
pubmed:abstractText
Calmodulin 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
181
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1548-56
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Association of calmodulin with isolated nuclei from rat hepatocytes.
pubmed:affiliation
Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't