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Comparative study on in vitro inhibition of grass carp ( Ctenopharyngodon idellus ) and mouse protein phosphatases by microcystins
Author(s) -
Xu L.,
Lam P. K. S.,
Chen J.,
Zhang Y.,
Harada K.
Publication year - 2000
Publication title -
environmental toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.813
H-Index - 77
eISSN - 1522-7278
pISSN - 1520-4081
DOI - 10.1002/(sici)1522-7278(2000)15:2<71::aid-tox1>3.0.co;2-e
Subject(s) - microcystin , phosphatase , grass carp , microcystin lr , biology , protein phosphatase 2 , cyanobacteria , biochemistry , protein phosphatase 1 , in vitro , carp , phosphorylation , fish <actinopterygii> , bacteria , fishery , genetics
Microcystins isolated from toxic cyanobacteria are potent inhibitors of protein phosphatases 1 and 2A (PP1 and PP2A). The inhibitory effects of three structural variants of microcystins (microcystin‐LR, ‐YR, and ‐RR) on protein phosphatases isolated and purified from the liver and kidney of grass carp ( Ctenopharyngodon idellus ) were investigated using the 32 P radiometric assay. The relationships between percentage inhibition of protein phosphatase activity and microcystin levels followed a typical dose‐dependent sigmoid curve. These results were compared to those obtained from mouse PP2A. The degree and pattern of inhibition of both fish and mouse protein phosphatases by microcystins were similar. Protein phosphatases in crude fish tissue homogenates showed similar inhibition patterns as purified fish PP2A toward microcystins. © 2000 John Wiley & Sons, Inc. Environ Toxicol 15: 71–75, 2000