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Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3.

Publication ,  Journal Article
Wang, H; Yan, B; Satterwhite, LL; Ma, Q; Goldschmidt-Clermont, PJ
Published in: Biochemical and biophysical research communications
February 2008

Polymorphisms in alphaIIbbeta3 are important genetic factors that alter platelet biology and have been associated with susceptibility to thromboembolic disorders. To define the molecular mechanisms that lead to variance in thrombotic diathesis dictated by the beta3 polymorphism, we examined regulation of intracellular signaling by alphaIIbbeta3, and studied the effects of a common beta subunit PlA2 polymorphism. We found that PP2A regulates alphaIIbbeta3 control of the ERK signaling in a polymorphism specific fashion. In CHO cells, exogenous expression of alphaIIbbeta3 reduced ATP-stimulated ERK phosphorylation and more so for PlA2 than PlA1. Interestingly, reduced level of ERK phosphorylation correlated with an increase in PP2A activity, with higher activity associated with PlA2 than PlA1. We tested the effect of PP2A on alphaIIbbeta3-dependent adhesion, and found that PP2A overexpression increased cell adhesion, while phosphatase inhibitors decreased cell adhesion. We propose that PlA2 alters cell signaling at least in part by increasing beta3-associated PP2A activity.

Duke Scholars

Published In

Biochemical and biophysical research communications

DOI

EISSN

1090-2104

ISSN

0006-291X

Publication Date

February 2008

Volume

367

Issue

1

Start / End Page

72 / 77

Related Subject Headings

  • Polymorphism, Genetic
  • Platelet Glycoprotein GPIIb-IIIa Complex
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Phospholipases A2
  • Phospholipases A1
  • Group II Phospholipases A2
  • Extracellular Signal-Regulated MAP Kinases
  • Enzyme Inhibitors
  • Cricetulus
 

Citation

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ICMJE
MLA
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Wang, H., Yan, B., Satterwhite, L. L., Ma, Q., & Goldschmidt-Clermont, P. J. (2008). Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3. Biochemical and Biophysical Research Communications, 367(1), 72–77. https://doi.org/10.1016/j.bbrc.2007.12.094
Wang, Huili, Bin Yan, Lisa L. Satterwhite, Qi Ma, and Pascal J. Goldschmidt-Clermont. “Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3.Biochemical and Biophysical Research Communications 367, no. 1 (February 2008): 72–77. https://doi.org/10.1016/j.bbrc.2007.12.094.
Wang H, Yan B, Satterwhite LL, Ma Q, Goldschmidt-Clermont PJ. Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3. Biochemical and biophysical research communications. 2008 Feb;367(1):72–7.
Wang, Huili, et al. “Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3.Biochemical and Biophysical Research Communications, vol. 367, no. 1, Feb. 2008, pp. 72–77. Epmc, doi:10.1016/j.bbrc.2007.12.094.
Wang H, Yan B, Satterwhite LL, Ma Q, Goldschmidt-Clermont PJ. Increased activity of phosphatase PP2A in the presence of the PlA2 polymorphism of alphaIIbbeta3. Biochemical and biophysical research communications. 2008 Feb;367(1):72–77.
Journal cover image

Published In

Biochemical and biophysical research communications

DOI

EISSN

1090-2104

ISSN

0006-291X

Publication Date

February 2008

Volume

367

Issue

1

Start / End Page

72 / 77

Related Subject Headings

  • Polymorphism, Genetic
  • Platelet Glycoprotein GPIIb-IIIa Complex
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Phospholipases A2
  • Phospholipases A1
  • Group II Phospholipases A2
  • Extracellular Signal-Regulated MAP Kinases
  • Enzyme Inhibitors
  • Cricetulus