Isoproterenol-stimulated labelling of particulate proteins by using [adenylate-32P]NAD+ independent on a cAMP-dependent protein kinase in parotid acinar cells.
When saponin-permeabilized rat parotid acinar cells were incubated with [adenylate-32P]NAD+, labelling of proteins (33, 27 and 23 kDa) in particulate fractions of the cells was stimulated by isoproterenol. The effect of isoproterenol was completely blocked by a beta-antagonist. Both forskolin or cAMP mimicked the effect of isoproterenol on the labelling. However, an inhibitor of cAMPdPK failed to induce complete inhibition of the effects of isoproterenol, forskolin and cAMP. When the labelled proteins were treated with snake venom phosphodiesterase, neither [32P]5'-AMP nor [32P]phosphoribosyladenosine was released. These results suggest that covalent modification of proteins with NAD+, which is distinct from ADP-ribosylation and cAMPdPK-dependent phosphorylation, is coupled to beta-receptor-cAMP signalling system in rat parotid acinar cells.
Department of Physiology, Nihon University School of Dentistry at Matsudo, Chiba, Japan.
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Sugiya
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Hara-Yokoyama
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Furuyama
D000681:Amylases / Q000378:metabolism; D002463:Cell Membrane Permeability / Q000187:drug effects; D005576:Colforsin / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology; D007545:Isoproterenol / Q000494:pharmacology*; D009243:NAD / Q000378:metabolism*; D010306:Parotid Gland / Q000187:drug effects / Q000378:metabolism*; D043264:Phosphodiesterase I; D010727:Phosphoric Diester Hydrolases; D010761:Phosphorus Radioisotopes; D011433:Propranolol / Q000494:pharmacology; D012503:Saponins / Q000494:pharmacology
D010761:Phosphorus Radioisotopes; D012503:Saponins; D009243:NAD; D005576:Colforsin; D011433:Propranolol; D000242:Cyclic AMP; D010727:Phosphoric Diester Hydrolases; D043264:Phosphodiesterase I; C470790:phosphodiesterase I, snake venom; D000681:Amylases; D007545:Isoproterenol