Thrombin induces the association of cyclic ADP‐ribose‐synthesizing CD38 with the platelet cytoskeleton

FEBS Letters

Torti, Mauro²  Bertoni, Alessandra²  Festetics, Enrico Tolnai²  Balduini, Cesare²  Sinigaglia, Fabiola¹ 

[1] Institute of Biological Chemistry, University of Genoa, viale Benedetto XV 1, 16132 Genoa, Italy;Department of Biochemistry, University of Pavia, via Bassi 21, 27100 Pavia, Italy

关键词: ADP-ribosyl cyclase;    CD38;    Cytoskeleton;    Platelet;    Integrin αIIbβ3;    NGD+;    nicotinamide guanine dinucleotide;    cGDPR;    cyclic GDP-ribose;    cADPR;    cyclic ADP-ribose;    ADPR;    ADP-ribose;   

DOI  :  10.1016/S0014-5793(98)00516-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of platelet stimulation on the subcellular localization of CD38, a membrane glycoprotein that catalyses the synthesis of cyclic ADP-ribose from β-NAD⁺ was investigated. Treatment of human platelets with thrombin caused the association of about 40% of the total ADP-ribosyl cyclase activity with the cytoskeleton, through the translocation of the CD38 molecule from the Triton X-100-soluble to the insoluble fraction. The interaction of CD38 with the cytoskeleton was a specific and reversible process, mediated by the binding to the actin-rich filaments and was inhibited by treatment of platelets with cytochalasin D. This event was regulated by integrin α_IIbβ₃ and platelet aggregation as it was prevented by the inhibition of fibrinogen binding and was not observed in platelets from a patient affected by Glanzmann thrombasthenia. These results demonstrate that the subcellular localization of CD38 can be influenced by platelet stimulation with physiological agonists, and that membrane CD38 can interact with intracellular proteins.

【 授权许可】

Unknown