Linked Life Data

7529203

Source:http://linkedlifedata.com/resource/pubmed/id/7529203

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-2-7
pubmed:abstractText
Ischemic eye disease often results in ocular neovascularization, presumably due to the elaboration of growth factors. Diabetic retinopathy is a classic example in which dramatic retinal neovascularization arises after ischemic retinal damage. The characterization of vascular endothelial growth factor (VEGF) as an angiogenic molecule whose expression is markedly induced by hypoxia makes it a promising candidate for mediating ischemic retinal neovascularization. Thus, we have characterized the structure, binding, and regulation of VEGF receptors in bovine retinal (BREC) and aortic endothelial cells (BAEC). VEGF stimulated a 2.1-fold increase in BREC number and DNA content at 0.6 nmol/l VEGF (P < 1 x 10(-7)). Scatchard binding analysis demonstrated specific high-affinity VEGF receptors on BREC with a Kd of 4.9 +/- 0.6 x 10(-11) mmol/l, similar to that observed for BAEC at 5.1 +/- 0.4 x 10(-11) mmol/l. BREC, however, possess 1.5 x 10(5) high-affinity receptors/cell, threefold more than BAEC (P < 0.003) and more than any cell type reported previously. 125I-VEGF affinity cross-linking revealed complexes at 220 and 170 kDa in BREC, but only a 220-kDa band of lesser intensity in BAEC. Cross-linking was displaceable in a dose-dependent manner by VEGF (P < 0.01) but not by other hormones. Hypoxia increased VEGF receptor number 50% in BREC without altering affinity. Antiphosphotyrosine immunoblotting showed VEGF-stimulated tyrosine autophosphorylation of VEGF receptor bands at 225 and 220 kDa and another band at 80 kDa within 1 min.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
98-103
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7529203-Animals, pubmed-meshheading:7529203-Anoxia, pubmed-meshheading:7529203-Aorta, pubmed-meshheading:7529203-Cattle, pubmed-meshheading:7529203-Cell Division, pubmed-meshheading:7529203-Cells, Cultured, pubmed-meshheading:7529203-Diabetic Retinopathy, pubmed-meshheading:7529203-Endothelial Growth Factors, pubmed-meshheading:7529203-Endothelium, Vascular, pubmed-meshheading:7529203-Lymphokines, pubmed-meshheading:7529203-Neovascularization, Pathologic, pubmed-meshheading:7529203-Phosphorylation, pubmed-meshheading:7529203-Receptor, Epidermal Growth Factor, pubmed-meshheading:7529203-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:7529203-Receptors, Growth Factor, pubmed-meshheading:7529203-Receptors, Vascular Endothelial Growth Factor, pubmed-meshheading:7529203-Retinal Vessels, pubmed-meshheading:7529203-Vascular Endothelial Growth Factor A, pubmed-meshheading:7529203-Vascular Endothelial Growth Factors
pubmed:year
1995
pubmed:articleTitle
Comparative analysis of vascular endothelial growth factor receptors on retinal and aortic vascular endothelial cells.
pubmed:affiliation
Research Division, Joslin Diabetes Center, Boston, MA 02215.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't