Presence of three pertussis toxin substrates and Goα immunoreactivity in both plasma and granule membranes of chromaffin cells

FEBS Letters

Homburger, Vincent¹  Bockaert, Joël¹  Toutant, Madeleine¹  Aunis, Dominique²  Rouot, Bruno¹ 

[1] Centre CNRS-INSERM de Pharmacologie-Endocrinologie, Rue de la Cardonille, 34094 Montpellier Cédex France;Unité INSERM U-44, Centre de Neurochimie du CNRS, 5 Rue Blaise Pascal, 67084 Strasbourg, Cédex, France

关键词: Chromaffin granule;    G-protein;    Pertussis toxin;    Exocytosis;    Secretory granule;    NAD;    nicotinamide adenine;    GTP;    guanosine triphosphate;    GTP-γ-S;    guanosine 5′-(3-O-thio)triphosphate;    Gpp(NH)p;    guanosine 5′-(β;    γ-imido) triphosphate;    NEM;    N-ethylmaleimide;    DTT;    dithiothreitol;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(87)80174-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

GTP-binding proteins have been proposed to be involved in some secretory processes. Bordetella pertussis toxin is known to catalyze ADP-ribosylation of several GTP-binding proteins. In this paper, the subcellular localization of B. pertussis toxin substrates has been explored in chromaffin cells of bovine adrenal medulla. With appropriate gel electrophoresis conditions, three ADP-ribosylated substrates of 39, 40 and 41 kDa were detectable in both plasma and granule membranes. The more intense labelling occurred on the 40 kDa component, while the 41 kDa species exhibited electrophoretic mobility similar to that of G_iα. Significant immunoreactivity with anti-G_oα antibodies was detected at the level of the 39 kDa faster component. The association of G-proteins with granule and plasma membranes suggests the involvement of these proteins in the exocytotic process or in its regulation.

【 授权许可】

Unknown