Matrine suppresses advanced glycation end products-induced human coronary smooth muscle cells phenotype conversion by regulating endoplasmic reticulum stress-dependent Notch signaling.

Matrine suppresses advanced glycation end products-induced human coronary smooth muscle cells phenotype conversion by regulating endoplasmic reticulum stress-dependent Notch signaling. Eur J Pharmacol. 2020 Jun 12;:173257 Authors: Zhao L, Cai H, Tang Z, Cui Q, Liu Z, Lu S Abstract Advanced glycation end products (AGEs) induce vascular smooth muscle cells (VSMCs) contractile-synthetic phenotypic conversion which plays roles in aggravated atherosclerosis in diabetes. Matrine has been proved to suppress AGEs-induced phenotypic conversion which is governed by Notch pathway. Endoplasmic reticulum stress was associated with Notch pathway. Cultured human coronary smooth muscle cells (HCSMCs) were incubated with AGE-BSA at 0, 5 and 10 μmol/l. Specific siRNA was used to silence Protein kinase RNA-like ER kinase (PERK). Matrine at 0, 0.5 and 1.0 mmol/l were used to pre-treat the cells. Immunofluorescent staining of Smooth muscle myosin heavy chain 11 (MYH11) and smooth muscle α-actin 2 (ACTA2) were used to identify the contractile phenotype of HCSMCs. Protein phosphorylation and expression levels were evaluated by Western Blotting. AGE-BSA exposure facilitated the contractile-synthetic phenotypic conversion of HCSMCs in a concentration-dependent manner. AGE-BSA exposure increased expression levels of glucose-regulated protein 78 (GRP78), Delta-like 4 (Dll4), Notch intracellular domain (NICD1), Hes family basic helix-loop-helix (bHLH) tra...
Source: European Journal of Pharmacology - Category: Drugs & Pharmacology Authors: Tags: Eur J Pharmacol Source Type: research