Expression and function of natriuretic peptide receptor subtype A (NPR-A) in antrum and fundus of rat and human stomach

2001 ◽  
Vol 120 (5) ◽  
pp. A311-A311
Author(s):  
W GOWERJR ◽  
S PREMARATNE ◽  
R MCCUEN ◽  
M SCHUBERT
Keyword(s):  
Natriuretic Peptide ◽  
Human Stomach ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
And Function ◽  
Subtype A

Localization and expression of natriuretic peptide receptor subtype A and subtype C in rat parietal cells

2000 ◽  
Vol 118 (4) ◽  
pp. A1240
Author(s):  
William R. Gower ◽  
S. Premaratne ◽  
William R. Gower ◽  
Quentin W. McAfee ◽  
Peter J. Fabri ◽  
...  
Keyword(s):  
Natriuretic Peptide ◽  
Parietal Cells ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
Subtype C ◽  
Peptide Receptor ◽  
Subtype A

scholarly journals Characterization of natriuretic peptide receptor subtypes in the AtT-20 pituitary tumour cell line

1994 ◽  
Vol 299 (2) ◽  
pp. 481-487 ◽  
Author(s):  
A F Gilkes ◽  
P H Ogden ◽  
S B Guild ◽  
G Cramb
Keyword(s):  
Natriuretic Peptide ◽  
Guanylate Cyclase ◽  
Cyclic Gmp ◽  
Specific Binding ◽  
Pituitary Tumour ◽  
Tumour Cell Line ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
Gmp Production

Receptors for the natriuretic peptide family have been characterized in the adrenocorticotrophic hormone (ACTH)-secreting AtT-20 pituitary tumour cell line. Northern blot analysis detected mRNA transcripts for the guanylate cyclase-linked GC-B receptor subtype. There was no evidence for the expression of either guanylate cyclase-linked GC-A receptor or atrial natriuretic peptide (ANP)-C (clearance) receptor mRNAs. Cyclic GMP production in AtT-20 cells was stimulated up to 200-fold by C-type natriuretic peptide (CNP), which was 10- and 20 times as effective as equivalent concentrations of brain natriuretic peptide and ANP respectively. Cyclic GMP dose-response curves to CNP failed to show any signs of saturation even at concentrations up to 30 microM, indicating a relatively low affinity of CNP for the GC-B receptor. Although CNP induced large stimulations in cyclic GMP production, specific binding of [125I-Tyr0]CNP could not be demonstrated in AtT-20 cells. The absence of specific binding with this radiolabelled analogue is possibly due to a reduced affinity for the GC-B receptor, as CNP analogues with N-terminal modifications such as [Tyr0]CNP and [127I-Tyr0]CNP exhibited reduced abilities to stimulate cyclic GMP production in these cells. Despite elevating cyclic GMP levels, CNP had no effect on basal or corticotrophin-releasing factor-stimulating ACTH release from the cells. These results show that the guanylate cyclase-coupled GC-B receptor is the only natriuretic peptide receptor subtype expressed in AtT-20 cells. Although CNP can markedly stimulate cyclic GMP production in these cells, there is incomplete expression of the normal natriuretic peptide-induced inhibitory pathway of ACTH secretion at some point distal to the production of cyclic GMP.

Chronically elevated plasma C-type natriuretic peptide level stimulates skeletal growth in transgenic mice

2009 ◽  
Vol 297 (6) ◽  
pp. E1339-E1348 ◽  
Author(s):  
Takei Kake ◽  
Hidetomo Kitamura ◽  
Yuichiro Adachi ◽  
Tetsuro Yoshioka ◽  
Tomoyuki Watanabe ◽  
...  
Keyword(s):  
Natriuretic Peptide ◽  
Guanylyl Cyclase ◽  
Natriuretic Peptides ◽  
Critical Role ◽  
Skeletal Growth ◽  
Heart Weight ◽  
Receptor Subtype ◽  
Natriuretic Peptide Receptor ◽  
High Concentration ◽  
Peptide Receptor

C-type natriuretic peptide (CNP) plays a critical role in endochondral ossification through guanylyl cyclase-B (GC-B), a natriuretic peptide receptor subtype. Cartilage-specific overexpression of CNP enhances skeletal growth and rescues the dwarfism in a transgenic achondroplasia model with constitutive active mutation of fibroblast growth factor receptor-3. For future clinical application, the efficacy of CNP administration on skeletal growth must be evaluated. Due to the high clearance of CNP, maintaining a high concentration is technically difficult. However, to model high blood CNP concentration, we established a liver-targeted CNP-overexpressing transgenic mouse (SAP-CNP tgm). SAP-CNP tgm exhibited skeletal overgrowth in proportion to the blood CNP concentration and revealed phenotypes of systemic stimulation of cartilage bones, including limbs, paws, costal bones, spine, and skull. Furthermore, in SAP-CNP tgm, the size of the foramen magnum, the insufficient formation of which results in cervico-medullary compression in achondroplasia, also showed significant increase. CNP primarily activates GC-B, but under high concentrations it cross-reacts with guanylyl cyclase-A (GC-A), a natriuretic peptide receptor subtype of atrial natriuretic peptides (ANP) and brain natriuretic peptides (BNP). Although activation of GC-A could alter cardiovascular homeostasis, leading to hypotension and heart weight reduction, the skeletal overgrowth phenotype in the line of SAP-CNP tgm with mild overexpression of CNP did not accompany decrease of systolic blood pressure or heart weight. These results suggest that CNP administration stimulates skeletal growth without adverse cardiovascular effect, and thus CNP could be a promising remedy targeting achondroplasia.

scholarly journals Immunolocalization of natriuretic peptide receptor B in the rat kidney.

1998 ◽  
Vol 9 (10) ◽  
pp. 1777-1786
Author(s):  
M C Bonhomme ◽  
K L Grove ◽  
S Caron ◽  
C T Crilley ◽  
G Thibault ◽  
...  
Keyword(s):  
Natriuretic Peptide ◽  
Western Blotting ◽  
Polyclonal Antibodies ◽  
Rat Kidney ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Natriuretic Peptide Receptor ◽  
Binding Studies ◽  
Peptide Receptor ◽  
Renal Vascular

The natriuretic peptide receptor (NPR) family consists of three receptor subtypes: two transmembrane forms that contain a guanylyl cyclase intracellular domain (NPR-A and NPR-B), and one truncated form (NPR-C). Because of the lack of specific agonists and antagonists for each receptor subtype and to the difficulty to detect the presence of small quantities of NPR-B by ligand binding studies, polyclonal antibodies against a peptide whose sequence was chosen from a region of the extracellular domain of rat NPR-B that is not homologous to sequences in NPR-A and NPR-C were developed. Western blotting with affinity-purified anti-NPR-B (413-426)-Tyr revealed a polypeptide of approximately 120 kD on COS-1 cell membranes transfected with rat NPR-B cDNA. The antibody recognized a second polypeptide, approximately 5 to 10 kD smaller, which probably represents the unglycosylated receptor. Anti-NPR-B (413-426)-Tyr did not show crossreactivity to any other NPR. Western blotting analysis with anti-NPR-B (413-426)-Tyr also identified a protein of appropriate size in renal vascular membranes. These results were supported by immunohistochemistry findings that demonstrated staining for NPR-B on papillary and medullary capillaries, glomeruli, and renal arteries. This study concludes that NPR-B is present in the rat kidney, although it was only detected in vascular structures.

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