scholarly journals 0006 : Proliferation of the cardiac precursor cells expressing the stem cell antigen-1 is controlled by activation of the natriuretic peptide receptors

2016 ◽  
Vol 8 (3) ◽  
pp. 255
Author(s):  
Stéphanie Rignault ◽  
Christelle Bielmann ◽  
Lucas Liaudet ◽  
Bernard Waeber ◽  
François Feihl ◽  
...  
Keyword(s):  
Stem Cell ◽  
Natriuretic Peptide ◽  
Precursor Cells ◽  
Peptide Receptors ◽  
Natriuretic Peptide Receptors ◽  
Cell Antigen ◽  
Cardiac Precursor Cells

scholarly journals 0130 : Is the stem cell antigen 1 involved in the brain natriuretic peptide effect on cardiac precursor cells?

2015 ◽  
Vol 7 (2) ◽  
pp. 149
Author(s):  
Fabien Cusin ◽  
Stéphanie Rignault ◽  
Christelle Bielmann ◽  
Suzanne Badoux ◽  
Lucas Liaudet ◽  
...  
Keyword(s):  
Stem Cell ◽  
Brain Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Precursor Cells ◽  
Cell Antigen ◽  
Cardiac Precursor Cells ◽  
The Brain

scholarly journals ATP-independent activation of natriuretic peptide receptors

2005 ◽  
Vol 5 (Suppl 1) ◽  
pp. P3
Author(s):  
Laura K Antos ◽  
Sarah E Abbey-Hosch ◽  
Darcy R Flora ◽  
Lincoln R Potter
Keyword(s):  
Natriuretic Peptide ◽  
Peptide Receptors ◽  
Natriuretic Peptide Receptors

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

1995 ◽  
Vol 198 (9) ◽  
pp. 1875-1882 ◽  
Author(s):  
T Toop ◽  
J A Donald ◽  
D H Evans
Keyword(s):  
Natriuretic Peptide ◽  
Binding Sites ◽  
Kidney Tissue ◽  
Peptide Receptors ◽  
Natriuretic Peptide Receptors ◽  
Myxine Glutinosa ◽  
Clearance Receptor ◽  
Relationship Of ◽  
The Relationship ◽  
Gmp Production

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.

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

1994 ◽  
Vol 267 (6) ◽  
pp. R1437-R1444 ◽  
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.

scholarly journals Natriuretic peptides appeared after their receptors in vertebrates

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Anna Grandchamp ◽  
Shifa Tahir ◽  
Philippe Monget
Keyword(s):  
Natriuretic Peptide ◽  
Natriuretic Peptides ◽  
Binding Pocket ◽  
Vertebrate Species ◽  
Peptide Receptors ◽  
Natriuretic Peptide Receptors ◽  
Animal Evolution ◽  
Transmembrane Receptors ◽  
Docking Analysis ◽  
Function Change

Abstract Background In mammals, the natriuretic system contains three natriuretic peptides, NPPA, NPPB and NPPC, that bind to three transmembrane receptors, NPR1, NPR2 and NPR3. The natriuretic peptides are known only in vertebrates. In contrast, the receptors have orthologs in all the animal taxa and in plants. However, in non-vertebrates, these receptors do not have natriuretic properties, and most of their ligands are unknown. How was the interaction of the NP receptors and the NP established in vertebrates? Do natriuretic peptides have orthologs in non-vertebrates? If so, what was the function of the interaction? How did that function change? If not, are the NP homologous to ancestral NPR ligands? Or did the receptor’s binding pocket completely change during evolution? Methods In the present study, we tried to determine if the pairs of natriuretic receptors and their ligands come from an ancestral pair, or if the interaction only appeared in vertebrates. Alignments, modeling, docking, research of positive selection, and motif research were performed in order to answer this question. Results We discovered that the binding pocket of the natriuretic peptide receptors was completely remodeled in mammals. We found several peptides in non vertebrates that could be related to human natriuretic peptides, but a set of clues, as well as modeling and docking analysis, suggest that the natriuretic peptides undoubtedly appeared later than their receptors during animal evolution. We suggest here that natriuretic peptide receptors in non vertebrates bind to other ligands. Conclusions The present study further support that vertebrate natriuretic peptides appeared after their receptors in the tree of life. We suggest the existence of peptides that resemble natriuretic peptides in non-vertebrate species, that might be the result of convergent evolution.

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