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Thrombin induces the association of cyclic ADP‐ribose‐synthesizing CD38 with the platelet cytoskeleton
Author(s) -
Torti Mauro,
Festetics Enrico Tolnai,
Bertoni Alessandra,
Sinigaglia Fabiola,
Balduini Cesare
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00516-x
Subject(s) - cyclic adp ribose , thrombin , cd38 , cytoskeleton , platelet , chemistry , biochemistry , platelet activation , microbiology and biotechnology , biophysics , medicine , biology , cell , stem cell , cd34
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 IIb β 3 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.