Natriuretic peptide receptors in the kidney and the ventral and dorsal aortae of the Atlantic hagfish Myxine glutinosa (Agnatha).

The character of natriuretic peptide receptors (NPRs) in the kidney and aortae of the Atlantic hagfish Myxine glutinosa was determined and compared with that of NPRs in hagfish gills. The relationship of hagfish kidney and aortic NPRs with NPRs from higher vertebrates was also examined. Iodinated atrial and C-type natriuretic peptides (NPs) (125I-ANP, 125I-CNP) were used in tissue section autoradiography, competition studies and guanylate cyclase (GC) assays. Rat atrial and porcine C-type NPs (rANP, pCNP) and rat des[Gln18, Ser19, Gly20, Leu21 Gly22]ANP-(4-23)-NH2 (C-ANF, which binds to the mammalian and teleost 'clearance' receptor, NPR-C), were used as competing ligands. 125I-ANP binding sites were observed on both aortae and on the glomeruli, neck segments and archinephric ducts of the kidney. 4.0 nmol l-1 rANP competed for 50% of 125I-ANP glomerular sites. 125I-CNP did not visibly bind to any of the tissues, but 300 nmol l-1 pCNP competed for 50% of 125I-ANP glomerular sites. C-ANF failed to compete for 125I-ANP sites. rANP and pCNP stimulated cyclic GMP production in kidney membrane preparations, but C-ANF did not, demonstrating that the hagfish kidney NPR is GC-linked. This study suggests that a predominant population of ANP-like receptors, similar to the mammalian NPR-A, exists in the myxinoid aortae and kidney tissue. However, no detectable population of a receptor that binds all NPs, such as is present in the hagfish gill, nor an NPR similar to the NPR-C of higher vertebrates was discovered.

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Localization and analysis of natriuretic peptide receptors in the gills of the toadfish, Opsanus beta (teleostei)

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1994.267.6.r1437 ◽

1994 ◽

Vol 267 (6) ◽

pp. R1437-R1444 ◽

Cited By ~ 1

Author(s):

J. A. Donald ◽

T. Toop ◽

D. H. Evans

Keyword(s):

Natriuretic Peptide ◽

Binding Sites ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Major Band ◽

Opsanus Beta ◽

Secondary Lamellae ◽

Membrane Bound ◽

Type C ◽

Specific Ligand

The distribution and nature of natriuretic peptide binding sites was determined in the gills of the toadfish, Opsanus beta. Specific 125I-labeled rat atrial natriuretic peptide (rANP) and 125I-labeled porcine C-type natriuretic peptide (pCNP) binding sites were observed on the afferent and efferent filamental arteries and lamellar arterioles, and on the marginal channels of the secondary lamellae. In both section autoradiography and competition assays, the binding of both ligands was completely displaced by 1 microM rANP and 1 microM pCNP, but residual binding was observed with 1 microM of the type C natriuretic peptide receptor (NPR-C)-specific ligand C-ANF. Electrophoresis of gill membranes cross-linked with 125I-rANP showed a major band at 75 kDa and a fainter band at 140 kDa. Both rANP and pCNP significantly stimulated the production of cGMP above basal levels; C-ANF had no stimulatory effect. These data show that the intrafilamental gill vasculature of toadfish contains a major population of natriuretic peptide receptors very similar to mammalian clearance receptors and a smaller population of receptors that are linked to a membrane-bound guanylate cyclase.

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C-type natriuretic peptide and atrial natriuretic peptide receptors of rat brain

AJP Regulatory Integrative and Comparative Physiology ◽

10.1152/ajpregu.1993.264.3.r513 ◽

1993 ◽

Vol 264 (3) ◽

pp. R513-R523 ◽

Cited By ~ 2

Author(s):

J. Brown ◽

Z. Zuo

Keyword(s):

Olfactory Bulb ◽

Atrial Natriuretic Peptide ◽

Rat Brain ◽

Choroid Plexus ◽

Natriuretic Peptide ◽

Binding Sites ◽

Specific Binding ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Atrial Natriuretic

Natriuretic peptide receptors in rat brain were mapped by in vitro autoradiography using 125I-labeled [Tyr0]CNP-(1-22) to bind atrial natriuretic peptide receptor (ANPR)-B and ANPR-C receptors selectively, and 125I-labeled alpha-ANP to select ANPR-A and ANPR-C receptors. Des-[Gln18,Ser19,Gly20,Leu21,Gly22]ANP-(4- 23)-amide (C-ANP) was used for its selectivity for ANPR-C over ANPR-A. Specific binding of 125I-[Tyr0]CNP-(1-22) with a dissociation constant (Kd) approximately 1 nM occurred in olfactory bulb, cerebral cortex, lateral septal nucleus, choroid plexus, and arachnoid mater. This binding was abolished by C-type natriuretic peptide [CNP-(1-22)], alpha-ANP and C-ANP, and conformed to ANPR-C. 125I-alpha-ANP bound to all structures that bound 125I-[Tyr0]CNP-(1-22). This binding was also inhibited by both CNP-(1-22) and C-ANP, confirming the presence of ANPR-C-like binding sites. However, ANPR-C-like binding sites were heterogenous because only some had high affinities for 125I-[Tyr0]CNP-(1-22) and CNP-(1-22). 125I-alpha-ANP also bound sites without affinities for C-ANP or CNP-(1-22). These sites were consistent with ANPR-A. They occurred mainly on the olfactory bulb, the choroid plexus, and the subfornical organ. Guanosine 3',5'-cyclic monophosphate production was strongly stimulated by alpha-ANP but not by CNP-(1-22) in olfactory bulb. Neither ligand stimulated it in cortical tissue. Thus the natriuretic peptide binding sites of rat brain conformed to ANPR-A and to heterogenous ANPR-C-like sites. No ANPR-B were detected.

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LOCALIZATION OF NATRIURETIC PEPTIDE RECEPTORS IN HUMAN KIDNEY TISSUE

Journal of Hypertension ◽

10.1097/01.hjh.0000747924.16362.86 ◽

2021 ◽

Vol 39 (Supplement 1) ◽

pp. e300

Author(s):

Mia Jensen ◽

Andreas Frees ◽

Kasper Bostlund Assersen ◽

Kirsten Madsen ◽

Lars Lund ◽

...

Keyword(s):

Natriuretic Peptide ◽

Kidney Tissue ◽

Human Kidney ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors

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Selective downregulation of rat renal clearance receptors for atrial natriuretic peptide by chronic high-salt intake: study on isolated membranes using 125I-labelled c-atrial natriuretic peptide-(4–23)

Clinical Science ◽

10.1042/cs0830139 ◽

1992 ◽

Vol 83 (2) ◽

pp. 139-142 ◽

Cited By ~ 7

Author(s):

Harald Michel ◽

Angela Bäcker ◽

Herbert J. Kramer

Keyword(s):

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Biologically Active ◽

Preparation Technique ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Salt Loading ◽

Receptor Number ◽

Clearance Receptor ◽

Atrial Natriuretic

1. 125I-labelled c-atrial natriuretic peptide-(4–23) was used as radioligand for the direct quantification of atrial natriuretic peptide clearance receptors, and 125I-labelled rat atrial natriuretic peptide-(1–28) was used for the determination of total and biologically active atrial natriuretic peptide receptors, in renal glomerular and papillary membrane preparations of chronically salt-loaded and control rats. 2. The membrane preparation technique included acid-washing (pH 5), and receptor binding was assessed by saturation studies at 4°C for 3 h. Chronic salt loading revealed a 35% decrease in clearance receptor number in the glomerular membrane and a 42% decrease in the papillary membranes. The absolute decrease in clearance receptor number was almost identical with the observed reduction in absolute number of total atrial natriuretic peptide receptors. Biologically active receptors were not affected by chronic salt loading. 3. Selective downregulation of clearance receptors for atrial natriuretic peptide may reflect an important role for the rat renal atrial natriuretic peptide system in long-term fluid and electrolyte regulation.

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Alteration of lung atrial natriuretic peptide receptors in genetic cardiomyopathy

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.1996.271.1.l38 ◽

1996 ◽

Vol 271 (1) ◽

pp. L38-L45 ◽

Cited By ~ 2

Author(s):

S. Mukaddam-Daher ◽

J. Tremblay ◽

N. Fujio ◽

C. Koch ◽

M. Jankowski ◽

...

Keyword(s):

Atrial Natriuretic Peptide ◽

Natriuretic Peptide ◽

Guanylyl Cyclase ◽

Binding Sites ◽

Quantitative Polymerase Chain Reaction ◽

Statistical Significance ◽

Receptor Subtypes ◽

Peptide Receptors ◽

Natriuretic Peptide Receptors ◽

Atrial Natriuretic

These studies were designed to characterize the atrial natriuretic peptide (ANF) receptor subtypes [guanylyl cyclase natriuretic peptide receptors (NPR-A, NPR-B) and NPR-C] in lungs of normal hamsters and to evaluate alterations in receptor kinetics in genetic cardiomyopathy (CMO), a model of human congestive heart failure. Lung membranes were obtained from normal and CMO 200-to 230-day-old hamsters. Cross-linking and competitive binding receptor assays using 125I-labeled human ANF showed that lung membranes exhibit NPR, mainly guanylyl cyclase NPR-A and clearance NPR-C receptors. Stimulation of guanylyl cyclase by ANF and C-type natriuretic peptide (CNP) confirmed the presence of NPR-A and NPR-B. The maximum binding capacity of total ANF binding sites (442 +/- 68 vs. 271 +/- 57 fmol/mg protein, P < 0.05) was reduced, but dissociation constant (0.26 +/- 0.04 vs. 0.41 +/- 0.08 nM) was not altered in CMO animals. Similar reductions were observed in the binding sites for brain natriuretic peptide (BNP; 438 +/- 83 vs. 236 +/- 53 fmol/mg protein) and CNP (321 +/- 80 vs. 165 +/- 56 fmol/mg protein, P < 0.05) which may reflect a decline in NPR-A and NPR-B and/or NPR-C. Acid wash improved binding of 125I-labeled rat ANF to lung membranes of both normal and CMO hamsters, but the tendency towards reduced binding in CMO hamsters did not reach statistical significance, implying that downregulation may not have been due only to prior occupancy of the receptors. Transcripts of NPR-A, NPR-B, and NPR-C receptors in hamster lungs were detected by quantitative polymerase chain reaction. Compared with normal controls, the CMO hamster lung NPR-A mRNA was reduced by 50%, but NPR-B mRNA and NPR-C mRNA were not altered. Moreover, CMO hamster lungs showed less activation of guanylyl cyclase by ANF. These studies demonstrate that lung NPR are downregulated in hamster CMO.

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