The splice variants of vascular endothelial growth factor (VEGF) and their receptors.

2.50
Hdl Handle:
http://hdl.handle.net/10541/85753
Title:
The splice variants of vascular endothelial growth factor (VEGF) and their receptors.
Authors:
Robinson, Christopher J; Stringer, Sally E
Abstract:
Vascular endothelial growth factor (VEGF) is a secreted mitogen highly specific for cultured endothelial cells. In vivo VEGF induces microvascular permeability and plays a central role in both angiogenesis and vasculogenesis. VEGF is a promising target for therapeutic intervention in certain pathological conditions that are angiogenesis dependent, most notably the neovascularisation of growing tumours. Through alternative mRNA splicing, a single gene gives rise to several distinct isoforms of VEGF, which differ in their expression patterns as well as their biochemical and biological properties. Two VEGF receptor tyrosine kinases (VEGFRs) have been identified, VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1). VEGFR-2 seems to mediate almost all observed endothelial cell responses to VEGF, whereas roles for VEGFR-1 are more elusive. VEGFR-1 might act predominantly as a ligand-binding molecule, sequestering VEGF from VEGFR-2 signalling. Several isoform-specific VEGF receptors exist that modulate VEGF activity. Neuropilin-1 acts as a co-receptor for VEGF(165), enhancing its binding to VEGFR-2 and its bioactivity. Heparan sulphate proteoglycans (HSPGs), as well as binding certain VEGF isoforms, interact with both VEGFR-1 and VEGFR-2. HSPGs have a wide variety of functions, such as the ability to partially restore lost function to damaged VEGF(165) and thereby prolonging its biological activity.
Affiliation:
The Cancer Research Campaign Department of Drug Development and the CRC and University of Manchester Department of Medical Oncology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, M20 4BX, UK.
Citation:
The splice variants of vascular endothelial growth factor (VEGF) and their receptors. 2001, 114 (Pt 5):853-65 J. Cell. Sci.
Journal:
Journal of Cell Science
Issue Date:
Mar-2001
URI:
http://hdl.handle.net/10541/85753
PubMed ID:
11181169
Type:
Article
Language:
en
ISSN:
0021-9533
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorRobinson, Christopher Jen
dc.contributor.authorStringer, Sally Een
dc.date.accessioned2009-11-10T10:07:10Z-
dc.date.available2009-11-10T10:07:10Z-
dc.date.issued2001-03-
dc.identifier.citationThe splice variants of vascular endothelial growth factor (VEGF) and their receptors. 2001, 114 (Pt 5):853-65 J. Cell. Sci.en
dc.identifier.issn0021-9533-
dc.identifier.pmid11181169-
dc.identifier.urihttp://hdl.handle.net/10541/85753-
dc.description.abstractVascular endothelial growth factor (VEGF) is a secreted mitogen highly specific for cultured endothelial cells. In vivo VEGF induces microvascular permeability and plays a central role in both angiogenesis and vasculogenesis. VEGF is a promising target for therapeutic intervention in certain pathological conditions that are angiogenesis dependent, most notably the neovascularisation of growing tumours. Through alternative mRNA splicing, a single gene gives rise to several distinct isoforms of VEGF, which differ in their expression patterns as well as their biochemical and biological properties. Two VEGF receptor tyrosine kinases (VEGFRs) have been identified, VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1). VEGFR-2 seems to mediate almost all observed endothelial cell responses to VEGF, whereas roles for VEGFR-1 are more elusive. VEGFR-1 might act predominantly as a ligand-binding molecule, sequestering VEGF from VEGFR-2 signalling. Several isoform-specific VEGF receptors exist that modulate VEGF activity. Neuropilin-1 acts as a co-receptor for VEGF(165), enhancing its binding to VEGFR-2 and its bioactivity. Heparan sulphate proteoglycans (HSPGs), as well as binding certain VEGF isoforms, interact with both VEGFR-1 and VEGFR-2. HSPGs have a wide variety of functions, such as the ability to partially restore lost function to damaged VEGF(165) and thereby prolonging its biological activity.en
dc.language.isoenen
dc.subject.meshAlternative Splicing-
dc.subject.meshAnimals-
dc.subject.meshEndothelial Growth Factors-
dc.subject.meshHeparan Sulfate Proteoglycans-
dc.subject.meshHumans-
dc.subject.meshLymphokines-
dc.subject.meshNerve Tissue Proteins-
dc.subject.meshNeuropilin-1-
dc.subject.meshProto-Oncogene Proteins-
dc.subject.meshReceptor Protein-Tyrosine Kinases-
dc.subject.meshReceptors, Growth Factor-
dc.subject.meshReceptors, Vascular Endothelial Growth Factor-
dc.subject.meshSignal Transduction-
dc.subject.meshVascular Endothelial Growth Factor A-
dc.subject.meshVascular Endothelial Growth Factor Receptor-1-
dc.subject.meshVascular Endothelial Growth Factors-
dc.titleThe splice variants of vascular endothelial growth factor (VEGF) and their receptors.en
dc.typeArticleen
dc.contributor.departmentThe Cancer Research Campaign Department of Drug Development and the CRC and University of Manchester Department of Medical Oncology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, M20 4BX, UK.en
dc.identifier.journalJournal of Cell Scienceen

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