Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2002-3-6
pubmed:databankReference
pubmed:abstractText
The family of human angiopoietins comprises factors with important roles in vascular development and angiogenesis. All angiopoietins bind with similar affinity to the endothelial cell-specific receptor, Tie2. The mechanism by which they contribute to angiogenesis is thought to involve regulation of endothelial cell interactions with supporting perivascular cells. In this study the genomic structures of all three human angiopoietins were characterised by direct sequencing of human genomic DNA from the appropriate P1 artificial chromosome (PAC) clones. The exact positions at the intron/exon boundaries and the lengths of all eight introns were determined. As would be expected from the homology of these three proteins, the positions of the introns in the three genes are highly conserved. The putative RNA transcription start site for each angiopoietin gene was also determined. Intron-specific primers were used to amplify each exon of angiopoietin-1 and angiopoietin-2 from individual genomic DNAs. Although no polymorphism has been detected in the coding region of angiopoietin-1, three independent polymorphisms have been identified for angiopoietin-2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-0171
pubmed:author
pubmed:copyrightInfo
Copyright 2002 S. Karger AG, Basel
pubmed:issnType
Print
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
147-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Genomic structures of the human angiopoietins show polymorphism in angiopoietin-2.
pubmed:affiliation
Molecular Medicine Unit, University of Leeds, St James's University Hospital, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't