Linked Life Data

2160972

Source:http://linkedlifedata.com/resource/pubmed/id/2160972

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1990-7-2
pubmed:databankReference
pubmed:abstractText
The tumor promoter phorbol 12-myristate 13-acetate (PMA) inhibits the growth of human endothelial cells and induces differentiation into capillary-like, tubular structures. We have isolated cDNA clones induced by PMA in the presence of cycloheximide and report the characterization of a novel immediate-early cDNA clone, termed edg-1, from human endothelial cells. The 3-kilobase edg-1 transcript is rapidly induced when endothelial cells are treated with PMA and superinduced in the presence of cycloheximide. While superinduction is due, at least in part, to the stabilization of the edg-1 transcript, nuclear run-on analysis demonstrates that the transcription of edg-1 is stimulated by PMA. Although the edg-1 transcript is very abundant in endothelial cells, transcripts related to human edg-1 are also detected at lower levels in vascular smooth muscle cells, fibroblasts, melanocytes, and cells of epithelioid origin. The deduced polypeptide sequence of edg-1 contains seven transmembrane domains with significant structural similarities to G-protein-coupled receptors (GPRs). Although the identity of the ligand for edg-1 is presently unknown, the structure of edg-1 polypeptide strongly implies that the edg-1 translation product is an inducible endothelial cell GPR. Since GPRs are involved in diverse biological processes such as signal transduction, cell proliferation, and differentiation, the characterization of human edg-1 as a highly inducible and abundant endothelial cell GPR suggest that it may be involved in the processes that regulate the differentiation of endothelial cells.
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
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9308-13
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2160972-Amino Acid Sequence, pubmed-meshheading:2160972-Base Sequence, pubmed-meshheading:2160972-Cell Differentiation, pubmed-meshheading:2160972-Cells, Cultured, pubmed-meshheading:2160972-Cycloheximide, pubmed-meshheading:2160972-Dactinomycin, pubmed-meshheading:2160972-Endothelium, Vascular, pubmed-meshheading:2160972-GTP-Binding Proteins, pubmed-meshheading:2160972-Humans, pubmed-meshheading:2160972-Molecular Sequence Data, pubmed-meshheading:2160972-Nucleic Acid Hybridization, pubmed-meshheading:2160972-RNA, Messenger, pubmed-meshheading:2160972-Receptors, Cell Surface, pubmed-meshheading:2160972-Sequence Homology, Nucleic Acid, pubmed-meshheading:2160972-Tetradecanoylphorbol Acetate, pubmed-meshheading:2160972-Transcription, Genetic, pubmed-meshheading:2160972-Umbilical Veins
pubmed:year
1990
pubmed:articleTitle
An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors.
pubmed:affiliation
Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, Maryland 20855.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't