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Identification of a membrane skeleton in platelets.

J E Fox¹, J K Boyles, M C Berndt

¹Department of Pathology, Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.

The Journal of Cell Biology

|May 1, 1988

Summary

Platelets possess a distinct membrane skeleton composed of actin and actin-binding protein, separate from cytoplasmic filaments. This submembranous layer likely stabilizes platelet shape and plasma membrane integrity.

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Area of Science:

Cell Biology
Hematology
Biochemistry

Background:

Platelets contain actin filaments linked to plasma membrane glycoproteins.
Previous methods disrupted platelet cytoskeleton organization.

Purpose of the Study:

To morphologically examine the distribution of membrane-bound filaments in platelets.
To establish conditions minimizing post-lysis changes to platelet cytoskeletons.

Main Methods:

Utilized a morphological approach with optimized lysis buffers.
Employed immunocytochemistry and SDS-polyacrylamide gel electrophoresis.
Investigated actin filament presence using DNase I and phalloidin.

Main Results:

Established platelet-shaped cytoskeletons with a peripheral amorphous layer.

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Identified the amorphous layer as containing actin, actin-binding protein, and glycoprotein Ib-IX.

Demonstrated the amorphous layer's association with the plasma membrane.

Conclusions:

Platelets contain a distinct membrane skeleton, separate from cytoplasmic actin filaments.
This membrane skeleton may stabilize the platelet plasma membrane and influence cell shape.
The findings provide insights into platelet structural organization.