Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts

R. Porta; A. De Santis; C. Esposito; G. F. Draetta; A. Di Donato; G. Illiano

doi:10.1016/S0006-291X(86)80538-1

Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts

R. Porta, A. De Santis, C. Esposito, G. F. Draetta, A. Di Donato, G. Illiano

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

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 l-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.

Original language	English (US)
Pages (from-to)	596-603
Number of pages	8
Journal	Biochemical and biophysical research communications
Volume	138
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(86)80538-1
State	Published - Jul 31 1986
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts",

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 l-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.",

author = "R. Porta and {De Santis}, A. and C. Esposito and Draetta, {G. F.} and {Di Donato}, A. and G. Illiano",

note = "Funding Information: We thank Prof. H.G. Williams-Ashman for a critical reading of the manuscript. This research was supported by grants From the Italian Ministry of Public Education (M.P.I. 40% - 1982) and C.N.R. (n°8400852.44) Progetto Finalizzato Oncologia.",

year = "1986",

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doi = "10.1016/S0006-291X(86)80538-1",

language = "English (US)",

volume = "138",

pages = "596--603",

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T1 - Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts

AU - Porta, R.

AU - De Santis, A.

AU - Esposito, C.

AU - Draetta, G. F.

AU - Di Donato, A.

AU - Illiano, G.

N1 - Funding Information: We thank Prof. H.G. Williams-Ashman for a critical reading of the manuscript. This research was supported by grants From the Italian Ministry of Public Education (M.P.I. 40% - 1982) and C.N.R. (n°8400852.44) Progetto Finalizzato Oncologia.

PY - 1986/7/31

Y1 - 1986/7/31

N2 - 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 l-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.

AB - 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 l-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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Inhibition of adenylate cyclase by transglutaminase-catalyzed reactions in pigeon erythrocyte ghosts

Abstract

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