Regulation of vascular endothelial cell polarization and migration by Hsp70/Hsp90-organizing protein.

PloS One
Jingyu LiMin Liu

Abstract

Hsp70/Hsp90-organizing protein (HOP) is a member of the co-chaperone family, which directly binds to chaperones to regulate their activities. The participation of HOP in cell motility and endothelial cell functions remains largely unknown. In this study, we demonstrate that HOP is critically involved in endothelial cell migration and angiogenesis. Tube formation and capillary sprouting experiments reveal that depletion of HOP expression significantly inhibits vessel formation from endothelial cells. Wound healing and transwell migration assays show that HOP is important for endothelial cell migration. By examination of centrosome reorientation and membrane ruffle dynamics, we find that HOP plays a crucial role in the establishment of cell polarity in response to migratory stimulus. Furthermore, our data show that HOP interacts with tubulin and colocalizes with microtubules in endothelial cells. These findings indicate HOP as a novel regulator of angiogenesis that functions through promoting vascular endothelial cell polarization and migration.

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Citations

Apr 3, 2014·Experimental Cell Research·Luiz Eduardo Rizzo de SouzaSilvio Marques Zanata
Feb 14, 2013·PloS One·Yunfan YangMin Liu
Nov 10, 2012·PloS One·Alexander F BrunsSreenivasan Ponnambalam
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Oct 16, 2016·Arteriosclerosis, Thrombosis, and Vascular Biology·Kerstin KickStefan Zahler
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Aug 2, 2017·Experimental Animals·Min LiuJun Zhou
Nov 24, 2019·Journal of Clinical Medicine·Patrizia LeoneVito Racanelli
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May 6, 2020·International Journal of Molecular Sciences·Samantha Joy BeckleyAdrienne Lesley Edkins
Nov 17, 2020·Frontiers in Plant Science·René ToribioM Mar Castellano

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Methods Mentioned

BETA
pulldown
transfection
immunoprecipitation

Software Mentioned

ImageJ
LASAF

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