Summary
We have previously shown that pretreatment of A10 smooth muscle cells (SMC) with angiotensin II (Ang II) attenuated atrial natriuretic peptide (ANP) receptor-C (ANPC) mediated-inhibition of adenylyl cyclase without altering [125I]-ANP binding. In the present studies, we have investigated the modulation of ANP-C receptor signaling by C-ANP4–23, an analog of ANP that interacts specifically with ANP-C receptor and endothelin-1 (ET-1). Pretreatment of A10 SMC with C-ANP 4–23 for 24hrs resulted in the reduction in ANP receptor binding activity, whereas ET-1 treatment of the cells attenuated the expression of ANP-C receptor by about 60% as determined by immunoblotting. This decrease in receptor binding and receptor expression was reflected in attenuation of ANP-C receptor mediated-inhibition of adenylyl cyclase. C-ANP4–23 [des(Gln18,Ser19,Gln20,Leu21,Gly22) ANP4–23 NH2] a ring deleted peptide of ANP inhibited adenylyl cyclase activity in a concentration dependent manner with an apparent Ki of about 1 nM in control cells. The maximal inhibition observed was by about 30% which was almost completely attenuated by C-ANP4–23 and ET-1 treatments. In addition, Ang II-mediated inhibition of adenylyl cyclase was also attenuated by such treatments. The expression of Giα-2 and Giα-3 protein was decreased by C-ANP4–23 treatment, whereas it was augmented by ET-1 treatment. On the other hand, the expression of Gsα was augmented by C-ANP4–23and not by ET-treatment, whereas the expression of Gβ protein was unaltered by such treatments. The Gsα-mediated effects of some agonists on adenylyl cyclase activity were significantly increased by C-ANP4–23 treatment and was decreased by ET-1 treatment. These results suggest that both the vasoactive peptides down regulate ANP-C receptor in A10 SMC. The C-ANP4–23-induced down-regulation of ANP-C receptor and decreased expression of Giα proteins may be responsible for the attenuation of C-ANP4–23-mediated inhibition of adenylyl cyclase activity, whereas ET-induced attenuation of C-ANP4–23-mediated inhibition of adenylyl cyclase may be attributed to the decreased expression of ANP-C receptor and not to the overexpression of Giα proteins. From these studies it may be suggested that the desensitization of ANP-C receptors by ANP and endothelin in vivo may be one of the possible mechanisms for the pathophysiology of hypertension.
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Anand-Srivastava, M.B., Boumati, M. (2003). Modulation of Atrial Natriuretic Peptide (ANP)-C Receptor and Associated Signaling by Vasoactive Peptides. In: Dhalla, N.S., Hryshko, L.V., Kardami, E., Singal, P.K. (eds) Signal Transduction and Cardiac Hypertrophy. Progress in Experimental Cardiology, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0347-7_12
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