Bruni P, Vasta V, Farnararo M
Institute of Biochemistry, University of Florence, Italy.
FEBS Lett. 1987 Sep 28;222(1):27-31. doi: 10.1016/0014-5793(87)80185-0.
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.
果糖2,6 - 二磷酸是6 - 磷酸果糖 -1 - 激酶最有效的激活剂，已被证明可介导有丝分裂原诱导的人成纤维细胞糖酵解通量的增加。在本研究中，对果糖2,6 - 二磷酸跨膜调控的分子基础进行了研究。已知能激活腺苷酸环化酶的前列环素和异丙肾上腺素能够提高果糖2,6 - 二磷酸水平，这表明在人成纤维细胞中，环磷酸腺苷在代谢物浓度的调控中起积极作用，这与在肝细胞中的作用相反。已知能激活蛋白激酶C的物质，如佛波醇12 - 肉豆蔻酸酯13 - 乙酸酯，或能刺激磷酸肌醇周转的物质，如凝血酶和缓激肽，也能有效提高果糖2,6 - 二磷酸水平。因此，我们得出结论，环磷酸腺苷和蛋白激酶C可能参与了人成纤维细胞中果糖2,6 - 二磷酸水平的调控。
