Enhancement of adenylate cyclase activity in S49 lymphoma cell membranes by the toxin thionin from Pyrularia pubera.
We investigated the mode of action of Pyrularia thionin on adenylate cyclase in S49 lymphoma cell membranes. Thionin increased the forskolin-induced cAMP production in both wild-type and cyc- variant cell membranes. Thionin increased the apparent efficacy, but not potency, of the stimulation of adenylate cyclase by forskolin. Our results also indicated that the stimulatory G protein (Gs) was not involved in the action of thionin on adenylate cyclase; however, thionin appeared to reduce the effect of Gi on adenylate cyclase. We examined the effect of thionin on the temperature dependence of adenylate cyclase activity. The effect of thionin was not quantitatively the same at all temperatures. The effect was greatest in the range of about 30 degrees C to 50 degrees C. In addition, cardiotoxin, a structurally distinct peptide that alters the properties of biological membranes similarly to thionin, also enhanced the activity of adenylate cyclase. It seems reasonable to suspect that thionin influences the activity of adenylate cyclase indirectly by acting on the membrane.
Huang
W
W
Department of Zoology, Brigham Young University, Provo, UT 84602.
Vernon
L P
LP
Bell
J D
JD
D000262:Adenylyl Cyclases / Q000187:drug effects*; D023181:Antimicrobial Cationic Peptides; D002462:Cell Membrane / Q000201:enzymology*; D005576:Colforsin / Q000494:pharmacology; D004347:Drug Interactions; D019204:GTP-Binding Proteins / Q000187:drug effects; D008223:Lymphoma; D010940:Plant Proteins / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
D023181:Antimicrobial Cationic Peptides; D010940:Plant Proteins; C044942:THI1 protein, Pyrularia pubera; D005576:Colforsin; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases