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Dematin and its interaction with platelet cytoskeleton (833.8)
Author(s) -
Azim Anser,
Murungi Terry,
Giragandi Abdelrahim
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.833.8
Subject(s) - microbiology and biotechnology , cytoskeleton , spectrin , myosin , actin , filopodia , platelet , lamellipodium , actin cytoskeleton , microfilament , biology , chemistry , biochemistry , immunology , cell
Background: Human platelets have spectrin based cytoskeleton that supports the plasma membrane of platelets and plays an important role in its activated and resting stages. The platelet cytoskeleton is also composed of peripheral microtubules. Human platelets have many actin binding proteins like spectrin, α□actinin, vinculin, talin, trpomyosin, adducin, dematin, myosin etc. In platelets monomeric actin is rapidly polymerized into F‐actin upon stimulation with the formation of surface filopodia and lamellipodia and acquires dendritic shape. Myosin forms stress like fibers with actin molecules. Dematin plays a role in activated platelets in the regulation of cytoskeleton. In this study we hypothesize the role of dematin, an ATP binding protein, in the regulation of cytoskeleton and its interaction with actin binding proteins. Method: We isolated human platelets from anti‐coagulated blood as described earlier (Azim AC et al Blood. 2000, 95(3):959‐64.). Platelets were used after incubating them at 37 0C for half an hour before the experiment. Results: The present study serially analyzed dematin’s coimmunoprecipitation with platelet myosin. And we believe that this interaction serves as a possible mechanism of ATP loading on the myosin molecule that subsequently plays a role in spreading and shape change. Discussion: In an attempt to understand the physiological role of dematin in hemostasis its worth knowing the role of this actin bundling protein, dematin, in human platelets. We show for the first time that platelet myosin interacts with dematin. Further studies are needed to know the precise role of this interaction in regulating actin cytoskeleton, shape change and platelet expansion.