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Intracellular signaling mechanisms mediating catecholamine release upon activation of NPY Y 1 receptors in mouse chromaffin cells
Author(s) -
RosmaninhoSalgado Joana,
Araújo Inês M.,
Álvaro Ana Rita,
Duarte Emília P.,
Cavadas Cláudia
Publication year - 2007
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2007.04899.x
Subject(s) - neuropeptide y receptor , catecholamine , endocrinology , medicine , protein kinase a , chromaffin cell , nitric oxide , chemistry , nitric oxide synthase , receptor , extracellular , intracellular , biology , kinase , adrenal medulla , microbiology and biotechnology , neuropeptide
The adrenal chromaffin cells synthesize and release catecholamine (mostly epinephrine and norepinephrine) and different peptides, such as the neuropeptide Y (NPY). NPY stimulates catecholamine release through NPY Y 1 receptor in mouse chromaffin cells. The aim of our study was to determine the intracellular signaling events coupled to NPY Y 1 receptor activation that lead to stimulation of catecholamine release from mouse chromaffin cells. The stimulatory effect of NPY mediated by NPY Y 1 receptor activation was lost in the absence of extracellular Ca 2+ . On the other hand, inhibition of nitric oxide synthase and guanylyl cyclase also decreased the stimulatory effect of NPY. Moreover, catecholamine release stimulated by NPY or by the nitric oxide donor (NOC‐18) was inhibited by mitogen‐activated protein kinase (MAPK) and protein kinase C inhibitors. In summary, in mouse chromaffin cells, NPY evokes catecholamine release by the activation the NPY Y 1 receptor, in a Ca 2+ ‐dependent manner, by activating mitogen‐activated protein kinase and promoting nitric oxide production, which in turn regulates protein kinase C and guanylyl cyclase activation.