Linked Life Data

2656700

Source:http://linkedlifedata.com/resource/pubmed/id/2656700

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1989-7-5
pubmed:abstractText
The present experiments were performed to identify calmodulin-binding proteins phosphorylated in response to insulin. Homogenates were prepared from 32Pi-labeled rat adipocytes. After centrifugation, the supernatants (+/- Ca2+) were applied to calmodulin-Sepharose columns. The bound proteins were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and phosphoproteins were visualized by autoradiography. Several proteins bound to the affinity resin in the presence of Ca2+, two bound +/- Ca2+, but only one protein, Mr = 170,000 (denoted pp170), bound in the absence of Ca2+. Binding of pp170 was inhibited by adding calmodulin (micromolar) or Ca2+ (nanomolar) to extracts prior to affinity chromatography. Physiological concentrations of insulin rapidly and reversibly increased (by as much as 4-fold) 32P-labeled pp170. Phorbol 12-myristate 13-acetate (PMA) increased (up to 3-fold) phosphorylation of pp170; but 4 alpha-phorbol 12,13-didecanoate was without effect. Phosphorylation of pp170 in response to insulin and PMA occurred predominantly on serine residues; no phosphotyrosine was detected. Protein kinase C inhibitors attenuated PMA-stimulated phosphorylation of pp170, but had no effect on insulin-stimulated phosphorylation. Peptide mapping indicated that pp170 was phosphorylated on multiple sites and that insulin stimulated the phosphorylation of at least one site not phosphorylated in response to PMA. The results indicate that insulin and PMA stimulate the phosphorylation of pp170 via different pathways, the latter presumably via protein kinase C.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9611-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Identification of an adipocyte protein that binds to calmodulin in the absence of Ca2+ and is phosphorylated in response to insulin and tumor-promoting phorbol esters.
pubmed:affiliation
Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't