Heat shock protein 70-1A is a novel angiogenic regulator.
Heat shock protein 70-1A (HSP70-1A) is a stress-inducible protein that provides an essential intracellular molecular chaperone function; however, the mechanism of HSP70-1A in angiogenesis has not been clarified. Herein, HSP70-1A gene silencing implicated this protein in angiogenesis. Additionally, recombinant human HSP70-1A (rhHSP70-1A) was able to stimulate human umbilical vein endothelial cell (HUVEC) migration and tube formation in vitro and microvessel formation in vivo similarly to recombinant human vascular endothelial growth factor (rhVEGF). Furthermore, rhHSP70-1A was tightly bound to the surface of HUVECs and participated in extracellular signal-related kinase (ERK)-dependent angiogenesis. Together, these results implicate HSP70-1A as a novel angiogenic regulator.
['Kim|Taek-Keun|TK|', 'Na|Hee Jun|HJ|', 'Lee|Woo Ran|WR|', 'Jeoung|Mee Hyun|MH|', 'Lee|Sukmook|S|']
D001808:Blood Vessels D002478:Cells, Cultured D042783:Endothelial Cells D018507:Gene Expression Regulation, Developmental D015971:Gene Expression Regulation, Enzymologic D018840:HSP70 Heat-Shock Proteins D006801:Humans D018919:Neovascularization, Physiologic
HSP70-1A Angiogenesis ERK