In the ciliate Euplotes raikovi, two specific isoforms of cAMP- dependent phosphodiesterases were identified, one in the soluble and the other in the particulate fraction of the cell. Their activity was shown to be stimulated by Mg2+, insensitive to Ca2+ and cGMP, and scarcely inhibited by theophylline and 3-isobutyl-1-methyl-xanthine. They appear to be related to some phosphodiesterases of class II of other unicellular organisms in their biochemical features, and their enzymatic activity is up-regulated by elevation of intracellular cAMP level similarly to PDE-4 isoforms of mammals.
Identification and partial characterization of cAMP-phosphodiesterases in the ciliate Euplotes raikovi.
VALLESI, Adriana
2004-01-01
Abstract
In the ciliate Euplotes raikovi, two specific isoforms of cAMP- dependent phosphodiesterases were identified, one in the soluble and the other in the particulate fraction of the cell. Their activity was shown to be stimulated by Mg2+, insensitive to Ca2+ and cGMP, and scarcely inhibited by theophylline and 3-isobutyl-1-methyl-xanthine. They appear to be related to some phosphodiesterases of class II of other unicellular organisms in their biochemical features, and their enzymatic activity is up-regulated by elevation of intracellular cAMP level similarly to PDE-4 isoforms of mammals.File in questo prodotto:
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