Solubilization and molecular weight estimation of atrial natriuretic factor receptor from bovine adrenal cortex

Hirose, Shigehisa; Akiyama, Fumiaki; Shinjo, Masashi; Ohno, Hideto; Murakami, Kazuo

doi:10.1016/0006-291x(85)90455-3

Cited by 58 publications

(13 citation statements)

References 15 publications

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“…In all tissues examined, 1251I-ANP crosslinking or photoaffinity-labeling studies have identified proteins of Mr 60,000-70,000 and/or 120,000-180,000 (9)(10)(11)(12)(13)(14)(15)(16)(17)(18). Data presented in this report identify the Mr 60,000-70,000 species as the ANP receptor.…”

Section: Discussionmentioning

confidence: 99%

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Purification and subunit composition of atrial natriuretic peptide receptor.

Schenk¹,

Phelps²,

Porter³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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A receptor for atrial natriuretic peptide (ANP) was purified 2700-fold, to apparent homogeneity, from cultured bovine aortic smooth muscle cells by affinity chromatography. The native ANP receptor has a molecular weight of 125,000 as determined by both metrizamide gradient centrifugation and nonreducing NaDodSO4/polysicrylamide gel electrophoresis. With 125I-labeled ANP as ligand, the purified receptor bound a maximum of 5.70 nmol of ligand per mg of protein and the dissociation constant was 4.0 x 10-1o M. Upon treatment with 10 mM dithiothreitol, the purified receptor migrated as a single band at Mr 60,500 in NaDodSO4/ polyacrylamide gel electrophoresis. These fmdings show that the holoreceptor for ANP in vascular tissue is composed of two subunits of identical apparent molecular weight, presumably linked by a disulfide bridge(s).

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Section: Discussionmentioning

confidence: 99%

“…Binding sites for 125I-labeled ANP (125I-ANP) have been identified in all these target organs by binding studies (5)(6)(7)(8)(9)(10) and, more recently, by crosslinking and photoaffinity-labeling studies (11)(12)(13)(14)(15)(16)(17). These studies have tentatively identified two classes of ANP receptor proteins of Mr 60,000-70,000 and 120,000-180,000.…”

mentioning

confidence: 99%

Purification and subunit composition of atrial natriuretic peptide receptor.

Schenk¹,

Phelps²,

Porter³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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“…In rat kidney cortex, the molecular mass of the ANP receptor was 140 kDa in the absence or presence of dithiothreitol (DTT) (Yip et al, 1985). In bovine adrenal cortex, however, the apparent molecular mass of the ANP receptor was decreased from 130 to 70 kDa under reducing conditions (Hirose et al, 1985). Another study identified 2 bands in bovine adrenal cortex, displaying molecular masses of 68 and 114 kDa, which were labeled by 1251-ANP in the absence or presence of 2-mercaptoethanol (Meloche et al, 1986).…”

Section: Molecular Mass Of Anp Binding Sitesmentioning

confidence: 99%

“…Previous studies have identified the putative ANP receptor in several peripheral tissues. Using either photoactive derivatives of ANP or chemical cross-linking agents, only a single band was labeled in bovine and rat adrenal cortical membranes (Hirose et al, 1985;Misono et al, 1985) and in rat kidney cortical membranes (Yip et al, 1985). There is disagreement in these studies, however, over the effect of reducing agents on the apparent size of peripheral ANP receptors.…”

Section: Molecular Mass Of Anp Binding Sitesmentioning

confidence: 99%

“…protein band displaying an apparent molecular mass of 120-140 kDa as the putative ANP binding site in bovine and rat adrenal cortical membranes (Hirose et al, 1985;Misono et al, 1985) and in rat kidney cortical membranes (Yip et al, 1985). However, in rabbit aorta (Vandlen et al, 1985) and bovine adrenal cortical (Meloche et al, 1986) membranes, and in cultured bovine endothelial and smooth muscle cells (Schenk et al, 1985), a protein band with an approximate molecular mass of 60-70 kDa was prominently labeled using both photoaffinity ligands and chemical cross-linking agents.…”

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confidence: 99%

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Cross-linking of atrial natriuretic peptide to binding sites in rat olfactory bulb membranes

Wildey¹,

Glembotski²

1986

J. Neurosci.

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Binding sites for 125I-atrial natriuretic peptide (ANP)2 in rat olfactory bulb membranes have been studied using pharmacological and biochemical methods. Various unlabeled ANP-related peptides were tested for the ability to inhibit the binding of the radioligand in membrane binding assays. ANP(92-126) and ANP(99-126) were the most potent inhibitors tested, both exhibiting an IC50 value of 0.40 nM. ANP(103-126) and ANP(103-123) were 3 and 70 times less potent, respectively. ANP(111-126) was unable to inhibit the binding of the radioligand at a concentration of 1 microM. Several peptides unrelated to ANP were unable to inhibit the binding of the radioligand to rat olfactory bulb membranes. Membranes labeled with 125I-ANP were incubated with cross-linking agents and subjected to SDS-PAGE followed by autoradiography. A band possessing an apparent molecular mass of 116 kDa was identified. The labeling of this band was progressively decreased by increasing concentrations of unlabeled ANP(99-126) (IC50 = 0.6 nM) and by several other ANP-related peptides at nanomolar concentrations. For comparison purposes, ANP binding sites in rat aorta membranes were labeled with 125I-ANP and cross-linked using identical techniques. Three bands possessing molecular masses of 120, 72, and 62 kDa were identified. These results indicate that the ANP binding site in rat olfactory bulb membranes displays pharmacological and biochemical properties similar to peripheral ANP receptors.

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Natriuretic Peptides

Bold¹,

Bruneau²

2000

Comprehensive Physiology

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The sections in this article are: Historical Perspectives Primary Structure Assay Methods The Endocrine Heart Functional Morphology Biological Properties of Natriuretic Peptides and Their Receptors Natriuretic Peptide Gene Structure Mechanical and Neuroendocrine Control of Natriuretic Peptide Gene Expression and Release Contribution of Natriuretic Peptides to Cardiovascular Homeostasis

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Solubilization and molecular weight estimation of atrial natriuretic factor receptor from bovine adrenal cortex

Cited by 58 publications

References 15 publications

Purification and subunit composition of atrial natriuretic peptide receptor.

Purification and subunit composition of atrial natriuretic peptide receptor.

Cross-linking of atrial natriuretic peptide to binding sites in rat olfactory bulb membranes

Natriuretic Peptides

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