Angiotensin-(1-7) decreased mitogen-activated protein (MAP) kinase (Erks) activation in cultured Mardin-Darby bovine kidney (MDBK) epithelial cells. Also, saturable, high-affinity 125I-angiotensin-(1-7) binding was detected in MDBK cell membranes. Together, the data suggested the possible presence of an angiotensin-(1-7) receptor. However, ligand structure-binding studies revealed that angiotensin-(3-7) and AT4 receptor ligands competed with high-affinity for 125I-angiotensin-(1-7) binding. Furthermore, angiotensin-(3-7) and AT4 receptor ligands decreased MAP kinase activation in MDBK cells. These results demonstrate that NH2-terminal-deleted metabolites of angiotensin-(1-7) can bind with high affinity to the AT4 receptor and regulate the MAP kinase/Erk signaling pathway in renal epithelial cells. Copyright (C) 2000 Elsevier Science Inc.
- AT receptor
- Ang IV
- Angiotensin peptides
- Kidney epithelial cells
- Mitogen-activated protein kinases
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience