Isoproterenol‐stimulated labelling of particulate proteins by using [adenylate‐32P]NAD+ independent on a cAMP‐dependent protein kinase in parotid acinar ells

FEBS Letters

Sugiya, Hiroshi¹  Furuyama, Shunsuke¹  Hara-okoyama, Miki¹ 

[1] Department of Physiology, Nihon University School of Dentistry at Matsudo, atsudo, Chiba 271, Japan

关键词: Isoproterenol;    NAD+;    Cyclic AMP;    Phosphorylation;    ADP-ribosylation;    Parotid;    cAMP;    cyclic AMP;    cAMPdPK;    cyclic AMP-dependent protein kinase;    IBMX;    3-isobutyl-1-methylxanthine;    H-8;    N-[2-(methylamino)ethyl]-5-isoquinolinesulfonamide;    HEPES;    4-(2-hydroxyethyl)-1-piperazincethanesulfonic acid;   

DOI  :  10.1016/0014-5793(92)80189-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β-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 β-receptor-cAMP signalling system in rat parotid acinar cells.

【 授权许可】

Unknown