Phosphorylation-dependent regulation of the guanylyl cyclase-linked natriuretic peptide receptors |
| |
Authors: | Potthast Regine Potter Lincoln R |
| |
Institution: | Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Twin Cities, 6-155 Jackson Hall, 321 Church Street SE, Minneapolis, MN 55455, USA. |
| |
Abstract: | Natriuretic peptides are a family of hormones/paracrine factors that regulate blood pressure, cardiovascular homeostasis and bone growth. The mammalian family consists of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and C-type natriuretic peptide (CNP). A family of three cell surface receptors mediates their physiologic effects. Two are receptor guanylyl cyclases known as NPR-A/GC-A and NPR-B/GC-B. Peptide binding to these enzymes stimulates the synthesis of the intracellular second messenger, cGMP, whereas a third receptor, NPR-C, lacks enzymatic activity and functions primarily as a clearance receptor. Here, we provide a brief review of how various desensitizing agents and/or conditions inhibit NPR-A and NPR-B by decreasing their phosphorylation state. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|