Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-3-1
pubmed:databankReference
pubmed:abstractText
Transgenic animal studies have linked the expression of the HIV-1 tat gene to the appearance of Kaposi's sarcoma (KS)-like lesions. We have recently shown that recombinant tat is angiogenic in vivo, and that tat angiogenic response is enhanced by heparin. Also in the rabbit cornea model, recombinant HIV-1 tat alone is poorly angiogenic, but gives a good response when combined with heparin. Like many angiogenic growth factors, tat has a basic domain similar to that of several heparin binding angiogenic factors, including FGF, VEGF and HGF, suggesting that this region is important in endothelial cell activation. We show that tat binds heparin sepharose with a high affinity, similar to bFGF. Binding of tat to the cell surface is also modulated by heparin. Biological activities of tat, such as induction of endothelial cell growth, migration and invasion in vitro are all enhanced by low concentrations and inhibited by high concentrations of heparin, as has been shown for other heparin-binding angiogenic factors. Heparan sulfate is also effective, whereas the unsulfated polysaccharide K5 does not enhance tat activity. Furthermore, a peptide encompassing the tat basic domain is able to induce growth and migration of endothelial cells, while an adjacent peptide is not. Our data indicate that the tat basic domain plays a key role in its vascular cell activation properties, and strongly suggest that extracellular HIV-tat is essentially a 'new' heparin-binding angiogenic factor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
289-97
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
HIV-tat protein is a heparin-binding angiogenic growth factor.
pubmed:affiliation
Istituto Nazionale per la Ricerca sul Cancro, Genova, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't