Circulation, Vol 86, 1081-1088, Copyright © 1992 by American Heart Association
KJ Koller and DV Goeddel
After the description in the past 5 years of BNP and CNP, interest in the
natriuretic peptide family has dramatically increased. Molecular
characterization of the receptors for this hormone family has identified a
heterogeneity in the receptor subtypes not previously alluded to by
pharmacological or biochemical studies. Much has been published on the
physiology of ANP, but the major roles for BNP and CNP remain to be
elucidated. Some experiments indicate that ANP and BNP may act
synergistically, especially during cardiac stress; however, the high level
of structural diversity of BNP among species and the ability of porcine
BNP, but not human BNP, to activate human NPR-B suggest that an as yet
unidentified receptor may exist that specifically recognizes BNP.
Localization studies have implied that CNP is the most prominent
neuropeptide in the natriuretic peptide family, and the restriction of its
receptor, NPR-B, to the nervous system suggests that CNP and NPR-B may act
in the brain to coordinate the central aspects of body fluid homeostasis.
Of the three known NPRs, two, NPR-A and NPR-B, are capable of synthesizing
their own second messenger, cGMP. The domain within these receptors that
has high homology to protein kinases has been demonstrated to be essential
for regulating this activity. No kinase activity has been measured in these
proteins, but it is possible that this region is important for ATP
regulation of guanylyl cyclase activity. This possibility raises
interesting parallels with receptor- mediated cAMP signaling within cells.
Seven transmembrane receptors, once activated by ligand, associate with G
proteins to affect the activity of adenylyl cyclase.(ABSTRACT TRUNCATED AT
250 WORDS)
ARTICLES
Molecular biology of the natriuretic peptides and their receptors
Department of Molecular Biology, Genetech Inc., South San Francisco, Calif.
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