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Angiotensin-(1-7)-induced activation of ERK1/2 is cAMP/protein kinase A-dependent in glomerular mesangial cells.
Am J Physiol Renal Physiol. 2012 Mar 15; 302(6):F784-90.AJ

Abstract

The renin-angiotensin system (RAS) plays an important role in renal physiology and kidney injury. Although the cellular effects of the RAS activation are generally attributed to angiotensin II (ANG II), the recent identification of angiotensin-converting enzyme 2 has shifted the focus to other peptides including Ang-(1-7). The G protein-coupled receptor for Ang-(1-7), mas, is expressed by mesangial cells (MC) but the signal transduction pathways activated by Ang-(1-7) in MC have not been fully elucidated. Accordingly, we studied the effect of Ang-(1-7) on extracellular signal-related kinase (ERK)1/2 activation in rat MC. Ang-(1-7)-induced ERK1/2 phosphorylation in MC is time- and concentration-dependent. Pretreatment of MC with the mas receptor antagonist A-779 but not the AT(1) antagonist losartan or the AT(2) antagonist PD123319 abrogated ERK1/2 activation. Neither pretreatment with the NADPH oxidase inhibitors diphenyleneiodonium and apocynin nor pretreatment with the epidermal growth factor (EGF) receptor antagonists AG1478 and PD158780 attenuated Ang-(1-7)-induced activation of ERK1/2. Even though each of these compounds abolished ANG II-induced activation of ERK1/2. Ang-(1-7) increased intracellular cAMP levels and activated protein kinase A (PKA) and inhibition of either adenylyl cyclase or PKA activity attenuated Ang-(1-7)-induced ERK1/2 activation. In conclusion, Ang-(1-7)-induced activation of ERK1/2 is cAMP/PKA-dependent in MC, but independent of NADPH oxidase and the EGF receptor.

Authors+Show Affiliations

Department of Medicine and Institute of Medical Sciences, University of Toronto, Toronto, Ontario, Canada M5G 2A8.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22189944

Citation

Liu, George C., et al. "Angiotensin-(1-7)-induced Activation of ERK1/2 Is cAMP/protein Kinase A-dependent in Glomerular Mesangial Cells." American Journal of Physiology. Renal Physiology, vol. 302, no. 6, 2012, pp. F784-90.
Liu GC, Oudit GY, Fang F, et al. Angiotensin-(1-7)-induced activation of ERK1/2 is cAMP/protein kinase A-dependent in glomerular mesangial cells. Am J Physiol Renal Physiol. 2012;302(6):F784-90.
Liu, G. C., Oudit, G. Y., Fang, F., Zhou, J., & Scholey, J. W. (2012). Angiotensin-(1-7)-induced activation of ERK1/2 is cAMP/protein kinase A-dependent in glomerular mesangial cells. American Journal of Physiology. Renal Physiology, 302(6), F784-90. https://doi.org/10.1152/ajprenal.00455.2011
Liu GC, et al. Angiotensin-(1-7)-induced Activation of ERK1/2 Is cAMP/protein Kinase A-dependent in Glomerular Mesangial Cells. Am J Physiol Renal Physiol. 2012 Mar 15;302(6):F784-90. PubMed PMID: 22189944.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Angiotensin-(1-7)-induced activation of ERK1/2 is cAMP/protein kinase A-dependent in glomerular mesangial cells. AU - Liu,George C, AU - Oudit,Gavin Y, AU - Fang,Fei, AU - Zhou,Joyce, AU - Scholey,James W, Y1 - 2011/12/21/ PY - 2011/12/23/entrez PY - 2011/12/23/pubmed PY - 2012/5/10/medline SP - F784 EP - 90 JF - American journal of physiology. Renal physiology JO - Am J Physiol Renal Physiol VL - 302 IS - 6 N2 - The renin-angiotensin system (RAS) plays an important role in renal physiology and kidney injury. Although the cellular effects of the RAS activation are generally attributed to angiotensin II (ANG II), the recent identification of angiotensin-converting enzyme 2 has shifted the focus to other peptides including Ang-(1-7). The G protein-coupled receptor for Ang-(1-7), mas, is expressed by mesangial cells (MC) but the signal transduction pathways activated by Ang-(1-7) in MC have not been fully elucidated. Accordingly, we studied the effect of Ang-(1-7) on extracellular signal-related kinase (ERK)1/2 activation in rat MC. Ang-(1-7)-induced ERK1/2 phosphorylation in MC is time- and concentration-dependent. Pretreatment of MC with the mas receptor antagonist A-779 but not the AT(1) antagonist losartan or the AT(2) antagonist PD123319 abrogated ERK1/2 activation. Neither pretreatment with the NADPH oxidase inhibitors diphenyleneiodonium and apocynin nor pretreatment with the epidermal growth factor (EGF) receptor antagonists AG1478 and PD158780 attenuated Ang-(1-7)-induced activation of ERK1/2. Even though each of these compounds abolished ANG II-induced activation of ERK1/2. Ang-(1-7) increased intracellular cAMP levels and activated protein kinase A (PKA) and inhibition of either adenylyl cyclase or PKA activity attenuated Ang-(1-7)-induced ERK1/2 activation. In conclusion, Ang-(1-7)-induced activation of ERK1/2 is cAMP/PKA-dependent in MC, but independent of NADPH oxidase and the EGF receptor. SN - 1522-1466 UR - https://www.unboundmedicine.com/medline/citation/22189944/Angiotensin__1_7__induced_activation_of_ERK1/2_is_cAMP/protein_kinase_A_dependent_in_glomerular_mesangial_cells_ L2 - https://journals.physiology.org/doi/10.1152/ajprenal.00455.2011?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -