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Inhibition of protein phosphatases activates glucose‐6‐phosphatase in isolated rat hepatocytes
Author(s) -
Claeyssens S.,
Chedeville A.,
Lavoinne A.
Publication year - 1993
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(93)81121-f
Subject(s) - okadaic acid , phosphatase , protein phosphatase 2 , puromycin , biochemistry , glucose 6 phosphatase , microsome , phosphorylation , protein phosphatase 1 , chemistry , acid phosphatase , incubation , enzyme , biology , protein biosynthesis
Incubation of hepatocytes in the presence of microcystin‐LR, okadaic acid, calyculin A (inhibitors of protein phosphatases PP1 and PP2A) or microcystin‐RR (a specific inhibitor of PP2A) activated glucose‐6‐phosphatase both in the supernatant and in intact or disrupted microsomes. Puromycin, an inhibitor of protein synthesis, totally suppressed this activating effect, suggesting the involvement of protein phosphatases in the regulation of glucose‐6‐phosphatase synthesis.