Linked Life Data

11943200

Source:http://linkedlifedata.com/resource/pubmed/id/11943200

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2002-4-10
pubmed:abstractText
p21-activated protein kinase gamma-PAK phosphorylates prolactin (PRL) in rat pituitary secretory granules on Ser-177 and on the equivalent site, Ser-179, in recombinant human PRL. This is shown by comparison of phosphopeptide maps with the human PRL mutant S179D. gamma-PAK is present in rat and bovine granules as identified by in-gel phosphorylation of histone H4, and by immunoblotting. Thus, phosphorylation of PRL by gamma-PAK in granules produces the PRL molecule that has been shown to antagonize the growth-promoting activity of unmodified PRL, and is consistent with the identified role of gamma-PAK in the induction and maintenance of cytostasis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
515
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
p21-activated protein kinase gamma-PAK in pituitary secretory granules phosphorylates prolactin.
pubmed:affiliation
Department of Biochemistry, University of California at Riverside, 92521, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.