Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera.

Bennett, Brian D.; Bennett, Gregory L.; Vitangcol, R. V.; Jewett, J. R. S.; Burnier, John; Henzel, William J.; Lowe, David

doi:10.1016/s0021-9258(18)54463-x

Cited by 132 publications

(29 citation statements)

References 41 publications

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“…Such antibodies might function as specific agonists or antagonists of the receptor. Using purified chimeric human B-IgG fusion protein (Bennett et al, 1991), mice were immunized using a complex of B-IgG and mouse anti-human Fe. A total of six clones, 2A8, 3G12, 4D2, 4E6, 6D8, and 6E5, that secrete mAbs recognizing the extracelluar domain of native hNPR-B were identified by flow cytometry.…”

Section: Resultsmentioning

confidence: 99%

“…Monoclonal and Polyclonal Antibodies-10 BALB/c mice were immunized with 4 j.Lg ofhB-IgG (Bennett et al, 1991) complexed with 40 /Lg of mouse anti-human IgG (Rockland, Gilbertsville, PA or Jackson Immunoresearch Labs, Inc. West Grove, PAl on days 0, 7, and 21. 5 j.Lg of hB-IgG complexed with 5 /Lg of mouse anti-human IgG was used for immunization on days 35 and 80.…”

Section: Methodsmentioning

confidence: 99%

“…Ultimately, six parental lineages (2A8, 3G12, 4D2, 4E6, 6D8, and 6E5) were chosen for limiting dilution cloning, ascites production, purification, and further characterization. Antibody purification from ascites was achieved by affinity chromatography on protein A (Bennett et al, 1991), and Fab preparation by papain cleavage was performed using an ImmunoPure® Fab purification kit (Pierce).…”

Section: Methodsmentioning

confidence: 99%

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Natriuretic Peptide Receptor-B (Guanylyl Cyclase-B) Mediates C-type Natriuretic Peptide Relaxation of Precontracted Rat Aorta

Drewett

Fendly²,

Garbers

et al. 1995

Journal of Biological Chemistry

100

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The most potent known agonist for the natriuretic peptide receptor-B (NPR-B)/guanylyl cyclase-B is C-type natriuretic peptide (CNP). A homologous ligand-receptor system consists of atrial natriuretic peptide (ANP) and NPR-A/guanylyl cyclase-A. A third member of this family is NPR-C, a non-guanylyl cyclase receptor. Monoclonal antibodies were raised against NPR-B by immunizing mice with a purified receptor-IgG fusion protein consisting of the extracellular domain of NPR-B and the Fc portion of human IgG-gamma 1. One monoclonal antibody, 3G12, did not recognize NPR-A or NPR-C and bound to human and rat NPR-B. CNP binding to NPR-B and stimulation of cGMP synthesis were inhibited by 3G12. With cells isolated from either the media or adventitia layers of rat thoracic aorta, 3G12 did not interfere with ANP-stimulated cGMP synthesis, but it inhibited CNP-stimulated cGMP levels in cells from both layers. CNP (IC50 = 10 nM) and ANP (IC50 = 1 nM) caused relaxation of phenylephrine-contracted rat aortic rings. 3G12 caused a marked increase in the IC50 for CNP, from 10 nM to 140 nM, but failed to affect ANP-mediated relaxation. Therefore, our results for the first time demonstrate that CNP relaxes vascular smooth muscle by virtue of its binding to NPR-B.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Natriuretic Peptide Receptor-B (Guanylyl Cyclase-B) Mediates C-type Natriuretic Peptide Relaxation of Precontracted Rat Aorta

Drewett

Fendly²,

Garbers

et al. 1995

Journal of Biological Chemistry

100

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“…GFRα-IgG-tagged receptors were made by transfecting 293 human embryonic kidney cells by the calcium phosphate method with an expression construct consisting of a cDNA encoding the respective GFRα receptor without its GPI-linked consensus sequence fused inframe with a cDNA encoding the Fc region of human IgG1 [29]. The recombinant GFRα-IgG fusion proteins were purified on a protein A-sepharose column (Pharmacia) and quantified by a human Fc-specific ELISA.…”

Section: Binding Of Persephin To Gfrα-igg-linked Receptorsmentioning

confidence: 99%

GFRα-4 and the tyrosine kinase Ret form a functional receptor complex for persephin

et al. 1998

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Glial-cell-line-derived neurotrophic factor (GDNF), neurturin and persephin are structurally related, secreted proteins that are widely expressed in the nervous system and other tissues and promote the survival of a variety of neurons during development. GDNF and neurturin signal through multicomponent receptors that consist of the Ret receptor tyrosine kinase and one of two structurally related glycosyl-phosphatidylinositol (GPI)-linked ligand-binding subunits: GFR alpha-1 is the preferred ligand-binding subunit for GDNF, and GFR alpha-2 is the preferred ligand-binding subunit for neurturin. Two additional members of the GFR alpha family of GPI-linked proteins have recently been cloned: GFR alpha-3 and GFR alpha-4. We have shown that persephin binds efficiently only to GFR alpha-4, and labelled persephin is effectively displaced from cells expressing GFR alpha-4 by persephin but not by GDNF or neurturin. Using microinjection to introduce expression plasmids into cultured neurons, we have also shown that coexpression of Ret with GFR alpha-4, confers a marked survival response to persephin but not to GDNF or neurturin. These results demonstrate that GFR alpha-4 is the ligand-binding subunit for persephin and that persephin, like GDNF and neurturin, also requires Ret for signalling.

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“…ANP, BNP, and CNP are degraded by binding to NPR-C through internalization followed by lysosomal degradation. The affinity of NPR-C for NPs is ANP > CNP > BNP in both humans and rats 9 , 10 , which may be related to the much shorter half-life of plasma ANP than that of BNP. Inactivation of NPR-C has been reported to increase the half-life of ANP in circulation by two-thirds in mice, and to show lower blood pressure 11 .…”

Section: Introductionmentioning

confidence: 99%

Osteocrin ameliorates adriamycin nephropathy via p38 mitogen-activated protein kinase inhibition

Handa

Mori

Ishii

et al. 2021

Sci Rep

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Natriuretic peptides exert multiple effects by binding to natriuretic peptide receptors (NPRs). Osteocrin (OSTN) binds with high affinity to NPR-C, a clearance receptor for natriuretic peptides, and inhibits degradation of natriuretic peptides and consequently enhances guanylyl cyclase-A (GC-A/NPR1) signaling. However, the roles of OSTN in the kidney have not been well clarified. Adriamycin (ADR) nephropathy in wild-type mice showed albuminuria, glomerular basement membrane changes, increased podocyte injuries, infiltration of macrophages, and p38 mitogen-activated protein kinase (MAPK) activation. All these phenotypes were improved in OSTN- transgenic (Tg) mice and NPR3 knockout (KO) mice, with no further improvement in OSTN-Tg/NPR3 KO double mutant mice, indicating that OSTN works through NPR3. On the contrary, OSTN KO mice increased urinary albumin levels, and pharmacological blockade of p38 MAPK in OSTN KO mice ameliorated ADR nephropathy. In vitro, combination treatment with ANP and OSTN, or FR167653, p38 MAPK inhibitor, reduced Ccl2 and Des mRNA expression in murine podocytes (MPC5). OSTN increased intracellular cyclic guanosine monophosphate (cGMP) in MPC5 through GC-A. We have elucidated that circulating OSTN improves ADR nephropathy by enhancing GC-A signaling and consequently suppressing p38 MAPK activation. These results suggest that OSTN could be a promising therapeutic agent for podocyte injury.

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Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera.

Cited by 132 publications

References 41 publications

Natriuretic Peptide Receptor-B (Guanylyl Cyclase-B) Mediates C-type Natriuretic Peptide Relaxation of Precontracted Rat Aorta

Natriuretic Peptide Receptor-B (Guanylyl Cyclase-B) Mediates C-type Natriuretic Peptide Relaxation of Precontracted Rat Aorta

GFRα-4 and the tyrosine kinase Ret form a functional receptor complex for persephin

Osteocrin ameliorates adriamycin nephropathy via p38 mitogen-activated protein kinase inhibition

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