期刊
BIOCHIMIE
卷 85, 期 7, 页码 647-650出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/S0300-9084(03)00135-4
关键词
phycotoxins; okadaic acid; alkaline phosphatase; non-competitive inhibition
This paper reports on a potential physiological target of okadaic acid (OA), the toxin metabolite responsible for shellfish poisoning and, consequently, human intoxication. OA is a potent promoter of tumor activity, most likely by inhibiting protein phosphatase 1 and 2A (Adv. Cancer. Res. 61 (1993) 143). However, all of its cellular targets have not yet been characterized. The interaction of OA with alkaline phosphatase (ALP) has been investigated in view of its protein phosphatase inhibition activity. Kinetic analysis of ALP from Escherichia coli, human placental and calf intestinal ALP has shown that OA acts as a non-competitive inhibitor of ALP. The bacterial enzyme displays a higher affinity for OA (K-i 360 nM) than the eukaryotic proteins (human placental ALP, K-i 2.05 muM; calf intestinal ALP, K-i 3.15 muM). The inhibition by OA suggests a putative role of ALP in the phosphorylation status, through regulation of the phosphorylation/dephosphorylation equilibrium of proteins with phosphoseryl or phosphothreonyl residues. (C) 2003 Editions scientifiques et medicales Elsevier SAS. All rights reserved.
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