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dc.contributor.authorRobinson, Christopher J
dc.contributor.authorStringer, Sally E
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.
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
html.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.


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