Inhibition of alkaline phosphatase activity by okadaic acid, a protein phosphatase inhibitor.

@article{citeulike:100105, abstract = {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 microM; calf intestinal ALP, K(i) 3.15 microM). 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.}, address = {Department of Chemistry, Faculty of Natural Sciences, Mathematics and Education, University of Split, N. Tesle 12, 21000, Split, Croatia.}, author = {Mestrovi\'{c}, V. and Pavela-Vrancic, M. }, citeulike-article-id = {100105}, issn = {0300-9084}, journal = {Biochimie}, month = {July}, number = {7}, pages = {647--650}, posted-at = {2005-02-21 16:58:42}, priority = {2}, title = {Inhibition of alkaline phosphatase activity by okadaic acid, a protein phosphatase inhibitor.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/14505819}, volume = {85}, year = {2003} }

TY - JOUR ID - citeulike:100105 L3 - citeulike-article-id:100105 TI - Inhibition of alkaline phosphatase activity by okadaic acid, a protein phosphatase inhibitor. JF - Biochimie VL - 85 IS - 7 SP - 647 EP - 650 AD - Department of Chemistry, Faculty of Natural Sciences, Mathematics and Education, University of Split, N. Tesle 12, 21000, Split, Croatia. SN - 0300-9084 N2 - 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 microM; calf intestinal ALP, K(i) 3.15 microM). 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. AU - Mestrović, V AU - Pavela-Vrancic, M PY - 2003/07// UR - http://view.ncbi.nlm.nih.gov/pubmed/14505819 ER -