Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-3-6
pubmed:databankReference
pubmed:abstractText
We have isolated by polymerase chain reaction-amplified subtractive hybridization technique, several cDNA clones that are induced by phorbol myristic acetate in human umbilical vein endothelial cells (HUVEC). One such clone, termed edg-2, was sequenced and was found to encode a human homologue of a Xenopus maternal transcript G10. The deduced amino acid sequence of edg-2 contains a putative nuclear translocation sequence, an N-terminal acidic domain and a cysteine-rich C-terminal domain containing a putative Zinc-finger structure. The structure of edg-2 polypeptide suggests that it may be a nuclear regulator of transcription. The edg-2 mRNA was expressed ubiquitously in cell lines of epithelial and mesenchymal lineages. In addition, the edg-2 polypeptide sequence is highly conserved in evolution and is expressed by lower organisms such as yeast and C. elegans, suggesting that it may be an important regulator of general nuclear function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
1260
pubmed:geneSymbol
edg-2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization of edg-2, a human homologue of the Xenopus maternal transcript G10 from endothelial cells.
pubmed:affiliation
Department of Molecular Biology, Holland Laboratory, American Red Cross, Rockville, MD 20855.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.