Cibone online dating

Activation of alpha IIbbeta3 is believed to occur in part via engagement of the beta3 cytoplasmic tail with talin; however, the role of the alpha IIb tail and its potential binding partners in regulating alpha IIbbeta3 activation is less clear.We report that calcium and integrin binding protein 1 (CIB1), which interacts directly with the alpha IIb tail, is an endogenous inhibitor of alpha IIbbeta3 activation; overexpression of CIB1 in megakaryocytes blocks agonist-induced alpha IIbbeta3 activation, whereas reduction of endogenous CIB1 via RNA interference enhances activation.Because CIB1 is one of a few proteins known to bind directly to the αIIb cytoplasmic tail, we hypothesized that CIB1 may modulate platelet αIIbβ3 activation.To determine whether CIB1 affects αIIbβ3 activation, we used differentiated megakaryocytes from murine bone marrow because megakaryocytes, unlike platelets, are amenable to direct genetic manipulation.However, like platelets but unlike many cell lines, mature megakaryocytes express αIIbβ3 and activate this integrin in response to agonists (Shiraga et al., 1999; Shattil and Leavitt, 2001; Bertoni et al., 2002), making them a suitable model system for studying platelet integrin regulation.We provide evidence that CIB1 is an inhibitor of agonist-induced αIIbβ3 activation, most likely via competition with talin binding to αIIbβ3.

This process contributes to both normal hemostasis and thrombosis.Integrin αIIbβ3, when in a resting state, does not bind plasma fibrinogen.However, upon platelet stimulation by agonists such as thrombin, intracellular signals are generated that change the conformation of αIIbβ3 to an active state via “inside-out” signaling (for review see Parise et al., 2001).S1 C), which directly activates αIIbβ3 independent of agonist-induced, inside-out signaling.These data suggest that CIB1 negatively regulates agonist-induced αIIbβ3 activation.

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