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Cytochalasin B binding by human platelets

C R Zobel, C Y Jung

    Journal of Cellular Physiology
    |November 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Human platelets bind cytochalasin B (CB), with most binding occurring in the cytosol and sensitive to cytochalasin E (CE). Glucose-sensitive binding, associated with membranes, represents a small fraction of total CB binding.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Pharmacology

    Background:

    • Platelets play crucial roles in hemostasis and thrombosis.
    • Cytochalasin B (CB) is a known inhibitor of actin polymerization, affecting cell shape and function.
    • Understanding CB binding in platelets provides insights into cytoskeletal dynamics and drug interactions.

    Purpose of the Study:

    • To characterize the binding kinetics and localization of cytochalasin B (CB) in human platelets.
    • To differentiate between cytochalasin E (CE)-sensitive and CE-insensitive CB binding.
    • To investigate the role of glucose-sensitive binding in membrane-associated components.

    Main Methods:

    • Saturation binding assays using radiolabeled cytochalasin B (CB) on intact human platelets.

    Related Experiment Videos

  • Displacement assays utilizing cytochalasin E (CE) and D-glucose to identify binding components.
  • Analysis of CB binding to sedimentable constituents from washed platelets.

    • Main Results:

    • Intact platelets exhibit saturable CB binding (100-120 pmol/mg protein) with dissociation constants (KD) between 2 x 10(-8) and 10(-6) M.
    • Approximately 85% of saturable binding is sensitive to cytochalasin E (CE), indicating cytosolic association, likely with actin.
    • A minor fraction (3%) of binding is D-glucose sensitive and membrane-associated, with a KD of 1.5 x 10(-6) M.

    Conclusions:

    • The majority (95%) of saturable CB binding in human platelets is cytosolic and CE-sensitive.
    • CE-insensitive binding represents a smaller, distinct component.
    • Glucose-sensitive, membrane-associated binding is minimal, suggesting limited interaction with membrane proteins.