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P Cohen et al.
FEBS letters, 250(2), 596-600 (1989-07-03)
The type 2A protein phosphatases in mammalian tissue extracts are inhibited completely and specifically by 1-2 nM okadaic acid. In contrast, type 1 protein phosphatases are hardly affected at these concentrations, complete inhibition requiring 1 microM okadaic acid. These observations
R Nishiwaki et al.
Cancer letters, 83(1-2), 283-289 (1994-08-15)
Microcystin-LR is a unique and potent liver tumor promoter, belonging to the okadaic acid class compounds. Although microcystin-LR is a potent inhibitor of protein phosphatases 1 and 2A, as is okadaic acid, microcystin-LR has liver specificity dominance. Two significant aspects
C MacKintosh et al.
FEBS letters, 264(2), 187-192 (1990-05-21)
The cyclic heptapeptide, microcystin-LR, inhibits protein phosphatases 1 (PP1) and 2A (PP2A) with Ki values below 0.1 nM. Protein phosphatase 2B is inhibited 1000-fold less potently, while six other phosphatases and eight protein kinases tested are unaffected. These results are
R Nishiwaki-Matsushima et al.
Journal of cancer research and clinical oncology, 118(6), 420-424 (1992-01-01)
Certain waterblooms of toxic cyanobacteria (blue-green algae) are a health threat because of their production of toxic peptides, termed microcystins, which cause liver damage in wild and domesticated animals. The most widely studied microcystin is microcystin-LR, a heptapeptide containing the
M Craig et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 74(4), 569-578 (1996-01-01)
Heptapeptide microcystin and pentapeptide motuporin (nodularin-V) are equipotent inhibitors of type-1 and type-2A protein phosphatase catalytic subunits (PP-1c and PP-2Ac). Herein we describe elucidation of the molecular mechanisms involved in the interaction of these structurally similar hepatotoxins with PP-1c/PP-2Ac and
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