Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts |
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| Authors: | R Porta A De Santis C Esposito G F Draetta A Di Donato G Illiano |
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| Affiliation: | 1. From the Division of BioMedical Sciences (H.P., S.W., G.Z., R.L.G., R.T.), Faculty of Medicine, Memorial University, St. John''s, Newfoundland, Canada;2. Smith Kettlewell Eye Research Institute (M.M., W.V.G.), San Francisco, California, USA;3. West Coast Retina (J.M.J.), San Francisco, California, USA;4. East Bay Retina Consultants, Inc. (D.B.), Oakland, California, USA |
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| Abstract: | ![]()
We report the occurrence in pigeon erythrocytes of a soluble Ca2+-dependent transglutaminase (TGase) activity. The effect of the erythrocyte ghost protein modifications, determined by TGase-catalyzed reactions, on adenylate cyclase, phospholipid methyltransferase I and II activities and on the lipidic matrix fluidity of the membrane was investigated by using a purified guinea pig liver TGase preparation. The results showed a significant inhibitory effect of such modifications both on the basal and on the variously stimulated (by NaF, Gpp(NH)p alone or in the presence of 1-isoproterenol) adenylate cyclase activity. By contrast, both the phospholipid methylation and the fluidity of the lipidic matrix of the membrane were unaffected by TGase-mediated reactions. These data suggest a new possible inhibitory mechanism of the cyclic AMP synthesis which might be triggered by the enhancement of the cytosolic Ca2+ concentration. |
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