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      Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP).

      Science (New York, N.Y.)
      Animals, Atrial Natriuretic Factor, physiology, Cells, Cultured, Cercopithecus aethiops, Cloning, Molecular, Dose-Response Relationship, Drug, Guanylate Cyclase, metabolism, Humans, Natriuretic Peptide, Brain, Natriuretic Peptide, C-Type, Nerve Tissue Proteins, pharmacology, Receptors, Atrial Natriuretic Factor, Receptors, Cell Surface, Recombinant Proteins, Signal Transduction

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          Abstract

          The natriuretic peptides are hormones that can stimulate natriuretic, diuretic, and vasorelaxant activity in vivo, presumably through the activation of two known cell surface receptor guanylyl cyclases (ANPR-A and ANPR-B). Although atrial natriuretic peptide (ANP) and, to a lesser extent, brain natriuretic peptide (BNP) are efficient activators of the ANPR-A guanylyl cyclase, neither hormone can significantly stimulate ANPR-B. A member of this hormone family, C-type natriuretic peptide (CNP), potently and selectively activated the human ANPR-B guanylyl cyclase. CNP does not increase guanosine 3',5'-monophosphate accumulation in cells expressing human ANPR-A. The affinity of CNP for ANPR-B is 50- or 500-fold higher than ANP or BNP, respectively. This ligand-receptor pair may be involved in the regulation of fluid homeostasis by the central nervous system.

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