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Epinephrine and serotonin activation of adenyl cyclase from Tetrahymena pyriformis
Author(s) -
Rozensweig Z.,
Kindler S.H.
Publication year - 1972
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(72)80489-7
Subject(s) - tel aviv , tetrahymena pyriformis , chemistry , citation , tetrahymena , physics , library science , computer science , biochemistry
Adenyl cyclase has been found in several bacterial species and many higher organisms [I]. The enzyme from Metazoa is activated by sodium fluoride and a wide variety of hormones, whilst the adenyl cyclase of Brevibacterium liquifaciens requires pyruvate as a cofactor [2] and that of Escherichia coli is inhibited by sodium fluoride [3]. To our knowledge the formation of 3’,5’ cyclic AMP has not previously been shown in protozoa. The findings of Blum [4] that aminophylline increased the glycogen synthetase activity of Tetrahymena can be explained by assuming that this drug elevated the level of 3’,5’ cyclic AMP in the cells. It was thus of interest to examine the adenyl cyclase activity in the ciliate Tetrahymena pyriformis. We report here the activation of this enzyme by epinephrine, serotonin and NaF. The abolition of the epinephrine stimulation by propranolol but not phentolamine indicates strongly that the activity of this neurohormone is mediated through a fl type adrenergic receptor.