Idioma:

PROTEOLYTIC CLEAVAGE OF ATRIAL-NATRIURETIC-FACTOR RECEPTOR IN BOVINE ADRENAL MEMBRANES BY ENDOGENOUS METALLOENDOPEPTIDASE - EFFECTS ON GUANYLATE-CYCLASE ACTIVITY AND LIGAND-BINDING SPECIFICITY

ABE, T ; MISONO, KS

European journal of biochemistry, 1992-10, Vol.209 (2), p.717-724 [Periódico revisado por pares]

NEW YORK: Springer Nature

Texto completo disponível

Citações Citado por

Enviar para

Título:
PROTEOLYTIC CLEAVAGE OF ATRIAL-NATRIURETIC-FACTOR RECEPTOR IN BOVINE ADRENAL MEMBRANES BY ENDOGENOUS METALLOENDOPEPTIDASE - EFFECTS ON GUANYLATE-CYCLASE ACTIVITY AND LIGAND-BINDING SPECIFICITY
Autor: ABE, T ; MISONO, KS
Assuntos: Adrenal Cortex - metabolism ; adrenal glands ; Animals ; Aorta - metabolism ; Atrial Natriuretic Factor - metabolism ; Atrial Natriuretic Factor - pharmacology ; atrial natriuretic hormone ; Binding, Competitive ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Cattle ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; Cells, Cultured ; cleavage ; effects on ; Fundamental and applied biological sciences. Psychology ; guanylate cyclase ; Guanylate Cyclase - metabolism ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Hydrogen-Ion Concentration ; Kinetics ; Life Sciences & Biomedicine ; Ligands ; metalloendopeptidase ; Metalloendopeptidases - metabolism ; Molecular and cellular biology ; Muscle, Smooth, Vascular - metabolism ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; receptors ; Receptors, Atrial Natriuretic Factor - metabolism ; Science & Technology ; Substrate Specificity
É parte de: European journal of biochemistry, 1992-10, Vol.209 (2), p.717-724
Notas: Medline
NIH RePORTER
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
Descrição: Atrial natriuretic factor (ANF) is a peptide hormone from the heart atrium with potent natriuretic and vasorelaxant activities. The natriuretic activity of ANF is, in part, mediated through the adrenal gland, where binding of ANF to the 130-kDa ANF receptor causes suppression of aldosterone secretion. Incubation of bovine adrenal membranes at pH < 5.6 caused a rapid and spontaneous cleavage of the 130-kDa ANF receptor, yielding a 65-kDa polypeptide that could be detected by photoaffinity labeling by I-125-labeled N(alpha4)-azidobenzoyl-ANF(4 - 28) followed by SDS/PAGE under reducing conditions. Within 20 min of incubation at pH 4.0, essentially all the 130-kDa receptor was converted to a 65-kDa ANF binding protein. This cleavage reaction was completely inhibited by inclusion of 5 mM EDTA. When SDS/PAGE was carried out under non-reducing conditions, the apparent size of the ANF receptor remained unchanged at 130 kDa, indicating that the 65-kDa ANF-binding fragment was still linked to the remaining part(s) of the receptor polypeptide through a disulfide bond(s). The disappearance of the 130-kDa receptor was accompanied by a parallel decrease in guanylate cyclase activity in the membranes. Inclusion of EDTA in the incubation not only prevented cleavage of the 130-kDa receptor, but also protected guanylate cyclase activity, indicating that proteolysis, but not the physical effects of the acidic pH, causes inactivation of guanylate cyclase. The 130-kDa ANF receptor in adrenal membranes was competitively protected from photoaffinity labeling by ANF(1 - 28) or ANF(4 - 28), but not by atriopeptin I [ANF(5 - 25)] or C-ANF [des(18 -22)-ANF(4 - 23)-NH2]. On the contrary, the 65-kDa ANF-binding fragment generated after incubation at pH 4.0 was protected from labeling by any of the above peptides, indicating broader binding specificity. After incubation in the presence of EDTA, the 130-kDa ANF receptor, which was protected from proteolysis, retained binding specificity identical to that of the 130-kDa receptor in untreated membranes. The results indicate that the broadening of selectivity is caused by cleavage, but not by the physical effect of acidic pH. Spontaneous proteolysis of ANF receptor by an endogenous metalloendopeptidase, occurring with concomitant inactivation of guanylate cyclase activity and broadening of ligand-binding selectivity, may be responsible for the generation of low-molecular-mass receptors found in the adrenal gland and other target organs of ANF. The proteolytic process may play a role in desensitization or down-regulation of the ANF receptor.
Editor: NEW YORK: Springer Nature
Idioma: Inglês

Links

Voltar para lista de resultados

Anterior Resultado 8 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

PROTEOLYTIC CLEAVAGE OF ATRIAL-NATRIURETIC-FACTOR RECEPTOR IN BOVINE ADRENAL MEMBRANES BY ENDOGENOUS METALLOENDOPEPTIDASE - EFFECTS ON GUANYLATE-CYCLASE ACTIVITY AND LIGAND-BINDING SPECIFICITY

ABE, T ; MISONO, KS

NEW YORK: Springer Nature

Buscando em bases de dados remotas. Favor aguardar.