Title : Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration*.

Pub. Date : 2008 Mar 31

PMID : 18377662






4 Functional Relationships(s)
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1 However, the mechanism by which SHP-1 executes KDR dephosphorylation, the targeted tyrosine residue(s) of KDR and also overall downstream signaling or phenotypic change(s) caused, is not defined. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
2 Knockdown of SHP-1 by siRNA or inhibition of c-Src by an inhibitor, results in augmented DNA synthesis perhaps due to increased phosphorylation of at least three tyrosine residues of KDR 996, 1059 and 1175. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
3 CONCLUSION: Taken together our results define the tyrosine residues of KDR that are regulated by SHP-1 and also elucidates a novel feed back loop where SHP-1 is activated upon VEGF treatment through c-Src and controls KDR induced DNA synthesis, eventually leading to controlled angiogenesis. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens
4 CONCLUSION: Taken together our results define the tyrosine residues of KDR that are regulated by SHP-1 and also elucidates a novel feed back loop where SHP-1 is activated upon VEGF treatment through c-Src and controls KDR induced DNA synthesis, eventually leading to controlled angiogenesis. Tyrosine protein tyrosine phosphatase non-receptor type 6 Homo sapiens