The β isoform of the catalytic subunit of protein phosphatase 2B restrains platelet function by suppressing outside-in αII b β3 integrin signaling.

ABSTRACT:

Background

Calcium-dependent signaling mechanisms play a critical role in platelet activation. Unlike calcium-activated protease and kinase, the contribution of calcium-activated protein serine/threonine phosphatase in platelet activation is poorly understood.

Objective

To assess the role of catalytic subunit of protein phosphatase 2B (PP2B) or calcineurin in platelet function.

Results

Here, we showed that an increase in PP2B activity was associated with agonist-induced activation of human and murine platelets. Pharmacological inhibitors of the catalytic subunit of protein phosphatase 2B (PP2B-A) such as cyclosporine A or tacrolimus (FK506) potentiated aggregation of human platelets. Murine platelets lacking the β isoform of PP2B-A (PP2B-Aβ(-/-) ) displayed increased

SUBMITTER: Khatlani T 

PROVIDER: S-EPMC4268338 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature