Dystrophin-related protein in the platelet membrane skeleton. Integrin-induced change in detergent-insolubility and cleavage by calpain in aggregating platelets.

@article{Earnest1995DystrophinrelatedPI,
  title={Dystrophin-related protein in the platelet membrane skeleton. Integrin-induced change in detergent-insolubility and cleavage by calpain in aggregating platelets.},
  author={J. P. Earnest and Gilberto de Figueiredo Santos and S Zuerbig and Jennifer E. Fox},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 45},
  pages={
          27259-65
        }
}
The platelet membrane is lined with a membrane skeleton that associates with transmembrane adhesion receptors and is thought to play a role in regulating the stability of the membrane, distribution and function of adhesive receptors, and adhesive receptor-induced transmembrane signaling. When platelets are lysed with Triton X-100, cytoplasmic actin filaments can be sedimented by centrifugation at low g-forces (15,600 x g) but the membrane skeleton requires 100,000 x g. The present study shows… CONTINUE READING
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