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Atrial natriuretic peptide receptors
Nomenclature
ANP A
ANP B
Other names
GC-A, NPR-A
GC-B, NPR-B
Potency order
ANP>BNP»CNP
CNP » ANP = BNP
Selective agonists
ANP(R3D,G9T,RllS,MI2L,RI4S,G16R)*
Selective antagonists
[Asu7,23]-I3-ANP-7-28 (75)
Radioligands
[125I]ANP
Gene/Chromosomal localization
NPRl /lq21-q22 1
NPR2/9pI2-p21 1
Structure - 1TM
hl061 P16066 ml057 P18293 rl057 P18910
hl047 P20594 rl047 P16067
"specific for the human receptor? "rnonoclonal antibody 3G12 is an antagonist'
Comment: ANP A and ANPn receptors are catalytic receptors with guanylate cyclase (and potential protein kinase) activity on the intracellular domain of the protein sequence. Other receptorslbinding sites: Cloning studies have defined a further binding site for natriuretic peptides (ANPc or NPR-C) with an extracellular binding domain homologous to that of the ANP A receptor, but with a truncated intracellular domain of unknown function. This binding site has broadly equal affinity for ANP, BNP and CNP; and has been proposed to function as a clearance receptor. It exists as a disulphide-linked dimer (h540, P17342, NPR3 5p13-p141; r535, P41740), and can be radiolabelled with [l25I]ANP. An alternatively spliced variant has been described. Endogenous Iigandls): a-atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and type C-natriuretic peptide; a-ANP may derive from 'Y-ANP; the physiological role and action of I3-ANP is unknown; species heterogeneity in the sequences of the natriuretic peptides is evident. References: 1. Lowe, D.
c. et al. (1990) Genomics 8, 304-312; 2. Cunningham, B. C. et al. (1994) EMBO J.
13,2608-2515; 3. Drewett, J. G. et al. (1995) J. Bioi. Chem. 270, 4668--4674
Reviews • Anand-Srivastava, M. B. and Trachte, G . J. (1993) Atrial natriuretic factor receptors and signal transduction mechanisms Pharmacal. Rev. 45,455--497 • Garbers, D. L. and Lowe, D. G. (1994) Guanylyl cyclase receptors J. BioI. Chem. 269,30741-30744 • Smyth, E. M. and Keenan, A. K. (1994) The vascular ANF-C receptor: role in atrial peptide signalling Cell. Signal. 6, 125-133
ANP A
ANP B
Other names
GC-A, NPR-A
GC-B, NPR-B
Potency order
ANP>BNP»CNP
CNP » ANP = BNP
Selective agonists
ANP(R3D,G9T,RllS,MI2L,RI4S,G16R)*
Selective antagonists
[Asu7,23]-I3-ANP-7-28 (75)
Radioligands
[125I]ANP
Gene/Chromosomal localization
NPRl /lq21-q22 1
NPR2/9pI2-p21 1
Structure - 1TM
hl061 P16066 ml057 P18293 rl057 P18910
hl047 P20594 rl047 P16067
"specific for the human receptor? "rnonoclonal antibody 3G12 is an antagonist'
Comment: ANP A and ANPn receptors are catalytic receptors with guanylate cyclase (and potential protein kinase) activity on the intracellular domain of the protein sequence. Other receptorslbinding sites: Cloning studies have defined a further binding site for natriuretic peptides (ANPc or NPR-C) with an extracellular binding domain homologous to that of the ANP A receptor, but with a truncated intracellular domain of unknown function. This binding site has broadly equal affinity for ANP, BNP and CNP; and has been proposed to function as a clearance receptor. It exists as a disulphide-linked dimer (h540, P17342, NPR3 5p13-p141; r535, P41740), and can be radiolabelled with [l25I]ANP. An alternatively spliced variant has been described. Endogenous Iigandls): a-atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and type C-natriuretic peptide; a-ANP may derive from 'Y-ANP; the physiological role and action of I3-ANP is unknown; species heterogeneity in the sequences of the natriuretic peptides is evident. References: 1. Lowe, D.
c. et al. (1990) Genomics 8, 304-312; 2. Cunningham, B. C. et al. (1994) EMBO J.
13,2608-2515; 3. Drewett, J. G. et al. (1995) J. Bioi. Chem. 270, 4668--4674
Reviews • Anand-Srivastava, M. B. and Trachte, G . J. (1993) Atrial natriuretic factor receptors and signal transduction mechanisms Pharmacal. Rev. 45,455--497 • Garbers, D. L. and Lowe, D. G. (1994) Guanylyl cyclase receptors J. BioI. Chem. 269,30741-30744 • Smyth, E. M. and Keenan, A. K. (1994) The vascular ANF-C receptor: role in atrial peptide signalling Cell. Signal. 6, 125-133