Effect of corticotropin on the dehydrogenase activity of cells and tissues
Korkach, V.I.; Gudz', O.V.
Biulleten' Eksperimental'noi Biologii i Meditsiny 99(1): 45-48
1985
ISSN/ISBN: 0365-9615 PMID: 2981579 Document Number: 244777
The authors studied the effect of native ACTH on dehydrogenase activity of isolated strips of rat diaphragm and suspension of E. coli cells, serotype O III:B4, grown on beef extract agar in a medium with different dehydrogenation substrates. ACTH activated dehydrogenase of rat diaphragm in a medium containing pyruvate, alpha-ketoglutarate, malate, beta-hydroxybutyrate, D-aspartic acid and did not alter it in a medium containing succinate. In contradistinction to rat diaphragm, ACTH activated dehydrogenase of E. coli cells whatever the substrates used (oxaloacetate, isocitrate, alpha-ketoglutarate, succinate, fumarate, malate, pyruvate, lactate, beta-hydroxybutyrate, glucose, D-aspartic acid. Synacthen (ACTH1-24) exerted a similar effect. It is suggested that the effects of ACTH are mediated via its influence on adenylate cyclase in the absence of receptors.