Photoaffinity labeling of atrial natriuretic factor receptor in bovine and rat adrenal cortical membranes

Misono, Kunio S.; Grammer, Robert T.; Rigby, J.; Inagami, Tadashi

doi:10.1016/0006-291x(85)91713-9

Cited by 79 publications

(35 citation statements)

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“…This finding suggests that the low-molecular-mass receptor species previously observed in the aortic membrane preparations may have been generated by proteolytic degradation of the 130-kDa receptor in v i m during the membrane preparation or affinity-labeling procedure. Similarly, it is possible that Creceptor-like low-molecular-mass receptors previously observed in the adrenal cortex (Meloche at al., 1986a;Shinjo et al, 1986;Takayanagi et al, 1987) and the kidney membranes (Koseki et al, 1986;Hamada et al, 1987) may also have been derived through artificial proteolysis of high-molecular-mass ANF receptors which have been reported by others (Yip et al, 1985;Misono et al, 1985;Meloche et al, 1986b) to be predominant in these organs. Indeed, it was found that the 130-kDa ANF receptor in bovine adrenal cortex membranes was readily cleaved by an endogenous proteasc (Misono, 1988;Abe and Misono, 1992), or by exogenously added trypsin (Liu et al, 1989) to generate an ANFbinding fragment with a molecular mass around 60 kDa.…”

Section: Discussionmentioning

confidence: 95%

“…This observation is consistent with the fact that both the guanylate-cyclase-active ANF receptor (Kuno et al, 1986) and the guanylate-cyclase-inactive 60-kDa C-receptor (Shimonaka et al, 1987) have been purified from the lung. Other major target organs of ANF, including the aorta, the adrenal cortex (Misono et al, 1985;Meloche et al. 198613) and the kidney (Yip et al, 1985), all contain high-molecular-mass guanylatecyclase-coupled receptor as the major species.…”

Section: Discussionmentioning

confidence: 99%

“…["'I)NaI was obtained From Amersham. No5-(4-azidobenzoyl)-ANF-(5-28)-peptide labeled with '*'I [N,PhCO-'251-ANF(5-28)] was prepared as described previously (Misono et a]., 1985;Pandey et al, 1986). Human ANF A-type receptor cDNA and bovine C-receptor cDNA were kindly provided by Dr. David Garbers (University of Texas at Dallas) and Dr. Gordon Porter (Scios Nova Inc., Mountain View CA), respectively.…”

Section: Methodsmentioning

confidence: 99%

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Aortic smooth muscle contains guanylate‐cyclase‐coupled 130‐kDa atrial natriuretic factor receptor as predominant receptor form

Abe

Nishiyama

Snajdar

et al. 1993

European Journal of Biochemistry

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Photoaffinity labeling of atrial natriuretic factor (ANF) receptor in the plasma membranes from bovine aortic smooth muscle tissue using Na5-(4-azidobenzoy1)-ANF-(5-28)-peptide labeled with yielded a 130-kDa band. However, when smooth muscle cells from the same bovine aorta were placed in culture, the 130-kDa receptor quickly disappeared and a 60-kDa band began to appear at high density. After three passages, essentially no 130-kDa band was found and only the 60-kDa band was strongly labeled. The primary structures of the two receptor forms were compared by radiochemical peptide mapping after endoproteinase Glu-C digestion of photoaffinity-labeled and detergent-solubilized 130-kDa receptor from the aorta or the 60-kDa receptor from the cultured cells. The peptide mapping showed courses of digestion that were significantly different from each other, suggesting difference in their primary structures. The basal guanylate cyclase activity in the aortic membranes was 1.0 pmol cGMP produced . min-' . mg protein ' at 37 "C using Mn2+-GTP as substrate. The corresponding activity in the membranes from the cultured cells was 20fmol cGMP . min-' . mg protein-'. Binding studies gave a density of binding sites (BmJ of 82 fmol/mg protcin for the aortic membranes and 850 fmol/mg protein for the cultured cell membranes. These data suggest that the major form of ANF receptor in the cultured cells, namely the 60-kDa receptor, lacked guanylate cyclase activity. Northern blot analysis of poly(A)-RNA extracted form bovine thoracic aorta or adrenal cortex gave a single 3.6-kb band when 32P-labeled human A-type ANF receptor cDNA was used as a hybridization probe. However, no band was detected when C-receptor cDNA was used as a probe. In addition to the major 130-kDa band, extended SDS/PAGE revealed two additional faint bands with estimalcd molecular masses of 126 kDa and 135 kDa. Treatment with endoglycosidase H resulted in disappearance of the 126-kDa band and appearance of a 100-kDa band. The 130-kDa and 135-kDa bands were unchanged. Treatment by endoglycosidase F or glycopeptidase F reduced all three bands to a single 100-kDa band. These results suggest that the slight difference in mobility is due to different states of glycosylation. Competitive protection experiments showed binding specificity in the order of ANF > BNP S-CNP, AP-I for all three bands, indicating that the state of glycosylation had no effect on the ligand specificity. Photoaffinity labeling of bovine adrenal cortex membranes gave a single 130-kDa band. The same experiment with lung membranes yielded a 130-kDa band and a 60-kDa band at about 1 : 1 ratio. The data presented in this report indicate that the vascular smooth muscle contains predominantly the 130-kDa guanylate-cyclase-coupled ANF receptor in vivo, and that C-receptors found in culturcd vascular smooth muscle cells have been induced artificially from cell culturing.Atrial natriuretic factor (ANF) is a potent natriuretic (deBold et a]., 1981) and vasorelaxant peptide (Currie et al., 1983;Grammer et al., ...

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Aortic smooth muscle contains guanylate‐cyclase‐coupled 130‐kDa atrial natriuretic factor receptor as predominant receptor form

Abe

Nishiyama

Snajdar

et al. 1993

European Journal of Biochemistry

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“…8 Bovine adrenocortical plasma membranes were isolated by differential centrifugation and partially purified by sucrose density-gradient centrifugation, as described. 9 BSA was obtained from Boehringer Mannheim Biochemicals and bacitracin from United States Biochemical. All other reagents were of analytical grade or highest available grades.…”

Section: Methodsmentioning

confidence: 99%

“…10 The hormone-binding domain (2.5 ng) was incubated with increasing concentrations of ANF-binding assays with the bovine adrenocortical membranes were carried out according to the method described previously. 9 Before the assay, the membranes were freed from chloride by dialyzing against 20 mmol/L sodium phosphate buffer, pH 7.5, containing a suspension of an anion exchange resin AG 1X8 in formate form (Bio-Rad) at 4°C overnight. The membranes (5 g membrane protein) were incubated in the assay medium containing 0.1 mol/L NaCl or sodium acetate.…”

Section: Methodsmentioning

confidence: 99%

Atrial Natriuretic Factor Binding to Its Receptor Is Dependent on Chloride Concentration

Misono

2000

Circulation Research

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Abstract-Although considerable evidence indicates a role for atrial natriuretic factor (ANF) in renal salt regulation, other studies have found a lack of natriuretic response to high-plasma ANF under certain physiological and pathophysiological conditions. The mechanism for this apparent insensitivity to ANF is unknown. In the present study, it was found that ANF binding to its receptor requires the presence of chloride and occurs in a chloride concentration-dependent manner. ANF binding was measured using the purified recombinant hormone-binding domain of the ANF receptor in the presence of 0.1 mol/L NaCl or other selected salt. High specific binding was detected in the presence of NaCl, KCl, or NH 4 Cl. However, binding was undetectable when the salt was replaced with NaHCO 3 , CH 3 COONa, or CH 3 COONH 4 , indicating that binding requires the presence of chloride. Chloride dependence was also found with the native receptor in bovine adrenocortical membrane preparations. ANF binding to the recombinant protein was chloride concentration-dependent over a range from 0.05 to 10 mmol/L, and a half-maximum binding was attained at Ϸ0.6 mmol/L equivalent chloride concentration.Competitive-binding assays at several fixed concentrations of NaCl showed that lowering chloride concentration caused a decrease in maximum binding but did not alter K d values, suggesting that a loss of chloride turns off ANF binding rather than reducing affinity for ANF. Saturation-binding studies showed that excess ANF cannot overcome loss of binding caused by low chloride. Chloride-dependent ANF-receptor binding may function as a feedback-control mechanism regulating the ANF-receptor action and, hence, renal sodium excretion.

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Atrial Natriuretic Factor

Atlas

Maack

1992

Comprehensive Physiology

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Photoaffinity labeling of atrial natriuretic factor receptor in bovine and rat adrenal cortical membranes

Cited by 79 publications

References 24 publications

Aortic smooth muscle contains guanylate‐cyclase‐coupled 130‐kDa atrial natriuretic factor receptor as predominant receptor form

Aortic smooth muscle contains guanylate‐cyclase‐coupled 130‐kDa atrial natriuretic factor receptor as predominant receptor form

Atrial Natriuretic Factor Binding to Its Receptor Is Dependent on Chloride Concentration

Atrial Natriuretic Factor

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