Mediation of the physiological response of platelets by interactions of spectrin and protein 4.1 with the cytoskeleton.
Spectrin and protein 4.1 became associated with the Triton-insoluble cytoskeletons during platelet activation. Inhibition of platelet activation by a PGI2 analogue resulted in release of the proteins from the cytoskeletons. Changes in subcellular distributions of the proteins preceded changes in the state of platelet aggregation. These results suggest that interactions of spectrin and protein 4.1 with the cytoskeletons are involved in mediating the physiological response of the platelet.
Matsuoka
Y
Y
Department of Pathology, Mie University School of Medicine, Japan.
Nishikawa
M
M
Toyoda
H
H
Hirokawa
Y
Y
Ando
S
S
Yano
T
T
Tanabe
K
K
Yatani
R
R
D000199:Actins / Q000097:blood; D001792:Blood Platelets / Q000187:drug effects / Q000502:physiology*; D002846:Chromatography, Affinity; D003598:Cytoskeletal Proteins; D003599:Cytoskeleton / Q000502:physiology*; D004910:Erythrocyte Membrane / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D009479:Neuropeptides; D015539:Platelet Activation / Q000187:drug effects / Q000502:physiology*; D013049:Spectrin / Q000302:isolation & purification / Q000378:metabolism*; D013917:Thrombin / Q000494:pharmacology
D000199:Actins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009479:Neuropeptides; C028841:erythrocyte membrane band 4.1 protein; C120557:erythrocyte membrane protein band 4.1-like 1; D013049:Spectrin; D013917:Thrombin