Linked Life Data

16909199

Source:http://linkedlifedata.com/resource/pubmed/id/16909199

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2006-9-8
pubmed:abstractText
The development of functional blood and lymphatic vessels requires spatio-temporal coordination of the production and release of growth factors such as vascular endothelial growth factors (VEGFs). VEGF family proteins are produced in multiple isoforms with distinct biological properties and bind to three types of VEGF receptors. A VEGF-A splice variant, VEGF-A(165)b, has recently been isolated from kidney epithelial cells. This variant is identical to VEGF-A(165) except for the last six amino acids encoded by an alternative exon. VEGF-A(165)b and VEGF-A(165) bind VEGF receptors 1 and 2 with similar affinity. VEGF-A(165)b elicits drastically reduced activity in angiogenesis assays and even counteracts signaling by VEGF-A(165). VEGF-A(165)b weakly binds to heparan sulfate and does not interact with neuropilin-1, a coreceptor for VEGF receptor 2. To determine the molecular basis for altered signaling by VEGF-A(165)b we measured VEGF receptor 2 and ERK kinase activity in endothelial cells in culture. VEGF-A(165) induced strong and sustained activation of VEGF receptor 2 and ERK-1 and -2, while activation by VEGF-A(165)b was only weak and transient. Taken together these data show that VEGF-A(165)b has attenuated signaling potential through VEGF receptor 2 defining this new member of the VEGF family as a partial receptor agonist.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1420-682X
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2067-77
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
A VEGF-A splice variant defective for heparan sulfate and neuropilin-1 binding shows attenuated signaling through VEGFR-2.
pubmed:affiliation
Paul Scherrer Institut, Laboratory of Biomolecular Research, Molecular Cell Biology, 5232 Villigen-PSI, Switzerland.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't