Regulation of Clostridium perfringens alpha-toxin-activated phospholipase C in rabbit erythrocyte membranes.
The rapid phosphatidic acid (PA) formation induced by Clostridium perfringens alpha-toxin was stimulated by AlF4- in rabbit erythrocyte membranes. GTP[gamma S] [guanosine 5'-O-(3-thiotriphosphate)] stimulated the rapid 1,2-diacylglycerol formation and inositol 1,4,5-trisphosphate release induced by the toxin. On the other hand, treatment of erythrocyte lysates with phorbol 12-myristate 13-acetate (PMA) resulted in inhibition of toxin-induced PA production, and long-term PMA or 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7) treatment of the lysates led to stimulation of PA formation. Furthermore, treatment of erythrocytes with the toxin caused an increase of protein kinase C activity in membrane fractions. The results suggest that toxin-induced PA formation is mediated by endogenous phospholipase C regulated through GTP-binding protein and protein kinase C in rabbit erythrocytes.
Sakurai
J
J
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Japan.
Ochi
S
S
Tanaka
H
H
D000818:Animals; D001427:Bacterial Toxins / Q000633:toxicity*; D002135:Calcium-Binding Proteins; D003016:Clostridium perfringens / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000201:enzymology*; D019204:GTP-Binding Proteins / Q000378:metabolism; D066298:In Vitro Techniques; D008954:Models, Biological; D010712:Phosphatidic Acids / Q000096:biosynthesis; D011493:Protein Kinase C / Q000378:metabolism; D011817:Rabbits; D010738:Type C Phospholipases / Q000378:metabolism*
D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D010712:Phosphatidic Acids; D011493:Protein Kinase C; D010738:Type C Phospholipases; C040649:alpha toxin, Clostridium perfringens; D019204:GTP-Binding Proteins