Atrial Natriuretic Factor Stimulates Phosphorylation of a 52-kDa Calmodulin-Binding Protein in Vascular Smooth Muscle Cells
Autor: | Tadashi Inagami, S. Nakajo |
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Rok vydání: | 1993 |
Předmět: |
Male
inorganic chemicals medicine.medical_specialty Vascular smooth muscle Calmodulin Biophysics Stimulation macromolecular substances environment and public health Biochemistry Muscle Smooth Vascular Phosphoserine Cytosol Atrial natriuretic peptide Internal medicine medicine Animals Protein phosphorylation Phosphorylation Rats Wistar Phosphotyrosine Cyclic GMP Molecular Biology Aorta Cells Cultured Dose-Response Relationship Drug biology Endothelins Binding protein Rats Inbred Strains Rats enzymes and coenzymes (carbohydrates) Phosphothreonine Endocrinology biology.protein Tyrosine bacteria Calmodulin-Binding Proteins Endothelin receptor Protein Kinases Atrial Natriuretic Factor |
Zdroj: | Archives of Biochemistry and Biophysics. 301:320-324 |
ISSN: | 0003-9861 |
DOI: | 10.1006/abbi.1993.1150 |
Popis: | The effect of atrial natriuretic factor (ANF) on the phosphorylation of the calmodulin-binding protein in vascular smooth muscle cells was investigated. Several phosphorylated calmodulin-binding proteins ranging in molecular weight from 205,000 to 50,000 were detected. Among them, we have found that the phosphorylation of a 52-kDa protein present mainly in the cytosolic fraction is stimulated by ANF and that the elevation of the phosphorylation is both time- and dose-dependent. Furthermore, the stimulation was mimicked by 8-bromo-cyclic GMP but not by 8-bromo-cyclic AMP. Endothelin induced significant inhibition of the phosphorylation. These results indicate that 52-kDa protein phosphorylation may be responsible for the regulation of vascular smooth muscle tone. |
Databáze: | OpenAIRE |
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