In:
FEBS Letters, Wiley, Vol. 307, No. 2 ( 1992-07-28), p. 206-210
Abstract:
Okadaic acid (OA), a potent inhibitor of protein phosphatases type 1 and type 2A, inhibited thrombin‐induced platelet aggregation (IC 50 = 0.8 μM), [ 14 C]serotonin release and increase in intracellular Ca 2+ ([Ca 2+ ] i ) in the same dose dependence. In the absence of thrombin OA increased the phosphorylation of 50‐kDa protein and 20‐kDa myosin light chain (MLC20). The 50‐kDa protein phosphorylation was accomplished within a shorter time period and at a lower concentration than was the MLC20, OA decreased the thrombin‐induced phosphorylation of 47‐kDa protein and MLC20, although phosphorylation of MLC20 reincreased at higher concentrations of OA (5−10 μM). Since type 2A phosphatase is more sensitive to OA than type 1, these results suggest that type 2A phosphatases are involved in the regulation of Ca 2+ signaling in thrombin‐induced platelet activation.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(92)80768-C
Language:
English
Publisher:
Wiley
Publication Date:
1992
detail.hit.zdb_id:
1460391-3
SSG:
12
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