TY - JOUR
T1 - Angiotensin II downregulates ACE2-mediated enhancement of MMP-2 activity in human cardiofibroblasts
AU - Kuan, Tang Ching
AU - Chen, Mu Yuan
AU - Liao, Yan Chiou
AU - Ko, Li
AU - Hong, Yi Han
AU - Yen, Chun Yi
AU - Hsieh, Wen Yeh
AU - Cheng, Kun Shan
AU - Wu, Chien Liang
AU - Lin, Chih-Sheng
PY - 2013/12/1
Y1 - 2013/12/1
N2 - Angiotensin converting enzyme II (ACE2) is a component of the renin-angiotensin system (RAS) that negatively regulates angiotensin II (Ang II). Ang II, in turn, affects the expression of matrix metalloproteinases (MMPs) to induce heart remodeling. The specific mechanisms by which ACE2 regulates MMP-2, however, remain unclear. The aim of this study was to investigate the regulatory relationships between Ang II, ACE2, and MMP-2. ACE2 expression was upregulated and downregulated in human cardiofibroblasts (HCFs) by lentiviral infection. Effects on MMP-2 activity, shed ACE2 activity, extracellular signal-regulated kinase (ERK) signaling pathway, and ADAM metallopeptidase domain 17 (ADAM17) expression were assessed. ACE2 increased MMP-2 activity, and Ang II inhibited this effect through the Ang II type-1 receptor (AT1R) and ERK1/2 signaling pathway. Ang II also reduced the effect of ACE2 on ERK1/2 levels, the activity of shed ACE2, and adam17 expression in HCFs. Additionally, these Ang II-mediated reductions could be attenuated by AT1R antagonist valsartan. In conclusion, these data help to clarify how ACE2 and Ang II interact to regulate MMP-2 and control tissue remodeling in heart disease.
AB - Angiotensin converting enzyme II (ACE2) is a component of the renin-angiotensin system (RAS) that negatively regulates angiotensin II (Ang II). Ang II, in turn, affects the expression of matrix metalloproteinases (MMPs) to induce heart remodeling. The specific mechanisms by which ACE2 regulates MMP-2, however, remain unclear. The aim of this study was to investigate the regulatory relationships between Ang II, ACE2, and MMP-2. ACE2 expression was upregulated and downregulated in human cardiofibroblasts (HCFs) by lentiviral infection. Effects on MMP-2 activity, shed ACE2 activity, extracellular signal-regulated kinase (ERK) signaling pathway, and ADAM metallopeptidase domain 17 (ADAM17) expression were assessed. ACE2 increased MMP-2 activity, and Ang II inhibited this effect through the Ang II type-1 receptor (AT1R) and ERK1/2 signaling pathway. Ang II also reduced the effect of ACE2 on ERK1/2 levels, the activity of shed ACE2, and adam17 expression in HCFs. Additionally, these Ang II-mediated reductions could be attenuated by AT1R antagonist valsartan. In conclusion, these data help to clarify how ACE2 and Ang II interact to regulate MMP-2 and control tissue remodeling in heart disease.
KW - angiotensin II
KW - angiotensin-converting enzyme II
KW - human cardiofibroblasts
KW - matrix metalloproteinases- 2
UR - http://www.scopus.com/inward/record.url?scp=84894274108&partnerID=8YFLogxK
U2 - 10.1139/bcb-2013-0031
DO - 10.1139/bcb-2013-0031
M3 - Article
C2 - 24219285
AN - SCOPUS:84894274108
SN - 0829-8211
VL - 91
SP - 435
EP - 442
JO - Biochemistry and Cell Biology
JF - Biochemistry and Cell Biology
IS - 6
ER -