Linked Life Data

3371546

Source:http://linkedlifedata.com/resource/pubmed/id/3371546

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1988-6-24
pubmed:abstractText
We have used an 125I-calmodulin gel overlayer assay to identify calmodulin-binding component in the rat pituitary. Tissue-specific and Ca2+ -dependent patterns of 125I-calmodulin binding were observed, with five major Ca2+-dependent 125I-calmodulin-labeled components of subunit Mr greater than 205,000, 200,000, 135,000, 60,000, and 52,000. Ca2+-dependent binding was defined as that which was abolished in the presence of 1 mM EGTA. Calmodulin binding was inhibited by calmodulin antagonists such as penfluridol (1 microM) or pimozide (1 microM). Some Ca2+-independent binding was observed and appears to be due to (nonspecific) hydrophobic interaction of calmodulin with acid-soluble proteins, principally histones. Subcellular fractionation revealed that the Ca2+-dependent calmodulin-binding components are localized primarily in the cytosolic fraction. Separation of dispersed anterior pituitary cells by a linear metrizamide gradient yielded gonadotrope-enriched fractions; these contained all five 125I-calmodulin-binding components corresponding to the major bands in the pituitary homogenate. Studies with ovariectomized and steroid-replaced animals indicated that the tissue content of calmodulin-binding components, like those of calmodulin itself, did not appear to be differentially regulated by steroids. A comparison of rat and bovine pituitary tissue homogenates revealed that binding components migrating at the same apparent Mrs were found for four of the components (the largest component is lacking in the bovine system).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterization of calmodulin-binding components in the pituitary gonadotrope.
pubmed:affiliation
Department of Pharmacology, University of Iowa College of Medicine, Iowa City 52242.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't