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Adenylate cyclase stimulating agents and mitogens raise fructose 2,6‐bisphosphate levels in human fibroblasts Evidence for a dual control of the metabolite
Author(s) -
Bruni Paola,
Vasta Valeria,
Farnararo Marta
Publication year - 1987
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(87)80185-0
Subject(s) - adenylate kinase , fructose 2,6 bisphosphate , phosphofructokinase 2 , protein kinase c , activator (genetics) , glycolysis , chemistry , protein kinase a , cyclase , forskolin , biochemistry , fructose 1,6 bisphosphatase , fructose , biology , endocrinology , kinase , medicine , phosphofructokinase , enzyme , receptor
Fructose 2,6‐bisphosphate, the most potent activator of 6‐phosphofructo‐1‐kinase, has been demonstrated to mediate the increase of glycolytic flux induced by mitogens human fibroblasts. In the present work the molecular basis of transmembrane control of fructose 2,6‐bisphosphate has been investigated. Prostacyclin and isoprenaline, known to activate adenylate cyclase, are able to increase fructose 2,6‐bisphosphate levels, indicating that in human fibroblasts cyclic AMP plays a positive role in the control of the metabolite concentration, opposite to that exerted in hepatocytes. Substances known to activate protein kinase C such as phorbol 12‐myristate 13‐acetate, or to stimulate phosphoinositide turnover such as thrombin and bradykinin are also effective in raising fructose 2,6‐bisphosphate. Therefore, we conclude that cyclic AMP and protein kinase C are likely involved in the control of fructose 2,6‐bisphosphate levels in human fibroblasts.