78 kDa Glucose-Regulated Protein Attenuates Protein Aggregation and Monocyte Adhesion Induced by Angiotensin II in Vascular Cells.

International Journal of Molecular Sciences
Stephanie CicaleseSatoru Eguchi

Abstract

Investigations of vascular smooth muscle cell (VSMC) phenotypic modulation due to angiotensin II (AngII) stimulation are important for understanding molecular mechanisms contributing to hypertension and associated vascular pathology. AngII induces endoplasmic reticulum (ER) stress in VSMCs, which has been implicated in hypertensive vascular remodeling. Under ER stress, 78 kDa glucose-regulated protein (GRP78) acts as an endogenous chaperone, as well as a master controller of unfolded protein response (UPR) to maintain protein quality control. However, the potential downstream consequences of ER stress induced by AngII on protein quality control and pro-inflammatory phenotype in VSMCs remain elusive. This study aims to identify protein aggregation as evidence of the disruption of protein quality control in VSMCs, and to test the hypothesis that preservation of proteostasis by overexpression of GRP78 can attenuate the AngII-induced pro-inflammatory phenotype in VSMCs. Increases in protein aggregation and enhanced UPR were observed in VSMCs exposed to AngII, which were mitigated by overexpression of GRP78. Moreover, GRP78 overexpression attenuated enhanced monocyte adhesion to VSMCs induced by AngII. Our results thus indicate that...Continue Reading

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Citations

Oct 21, 2020·Journal of Cardiovascular Pharmacology·Stephanie CicaleseSatoru Eguchi
Feb 13, 2021·Cellular and Molecular Life Sciences : CMLS·Tatsuo KawaiSatoru Eguchi
Apr 2, 2021·Circulation Research·Stephanie M CicaleseRita C Tostes
May 19, 2021·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Yue DengJun Cai

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Methods Mentioned

BETA
protein folding
electrophoresis

Software Mentioned

UN
IT
SCAN
Prism
ImageJ
GraphPad

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