Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-12
pubmed:abstractText
Pleiotrophin (PTN) is a heparin-binding cytokine that functions as a neurite outgrowth promoting and mitogenic activity in vitro. PTN is highly conserved and its gene is widely expressed in mammalian tissues during development, suggesting important roles of PTN in vivo. However, the mechanisms by which PTN mediates its functional activities are unknown. We now report that an approximately 200 kDa (p200) protein is phosphorylated (pp200) in PTN stimulated NIH 3T3 and NB41A3 cells five minutes after stimulation with PTN. Phosphorylation is maximum at 15 minutes and is PTN concentration dependent. pp200 is recognized by antiphosphotyrosine antibodies and contains both phosphotyrosine and phosphoserine by phosphoamino acid analysis. The results suggest that PTN functions in part through activation of protein kinase(s) in NIH 3T3 and NB41A3 cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1089-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Pleiotrophin stimulates tyrosine phosphorylation in NIH 3T3 and NB41A3 cells.
pubmed:affiliation
Department of Medicine, Washington University School of Medicine, Jewish Hospital, St. Louis, Missouri 63110.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't