A dual role for integrin-linked kinase in platelets: regulating integrin function and alpha-granule secretion

K.L. Tucker, T. Sage, J.M. Stevens, P.A. Jordan, S. Jones, N.E. Barrett, R. St-Arnaud, J. Frampton, S. Dedhar, J.M. Gibbins

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Integrin-linked kinase (ILK) has been implicated in the regulation of a range of fundamental biological processes such as cell survival, growth, differentiation, and adhesion. In platelets ILK associates with beta 1- and beta 3-containing integrins, which are of paramount importance for the function of platelets. Upon stimulation of platelets this association with the integrins is increased and ILK kinase activity is up-regulated, suggesting that ILK may be important for the coordination of platelet responses. In this study a conditional knockout mouse model was developed to examine the role of ILK in platelets. The ILK-deficient mice showed an increased bleeding time and volume, and despite normal ultrastructure the function of ILK-deficient platelets was decreased significantly. This included reduced aggregation, fibrinogen binding, and thrombus formation under arterial flow conditions. Furthermore, although early collagen stimulated signaling such as PLC gamma 2 phosphorylation and calcium mobilization were unaffected in ILK-deficient platelets, a selective defect in alpha-granule, but not dense-granule, secretion was observed. These results indicate that as well as involvement in the control of integrin affinity, ILK is required for alpha-granule secretion and therefore may play a central role in the regulation of platelet function. (Blood. 2008; 112: 4523-4531)
Original languageEnglish
Pages (from-to)4523-4531
Number of pages9
Issue number12
Publication statusPublished - 2008


  • protein-kinase cell-adhesion actin cytoskeleton ilk activation matrix pinch sites complex phosphorylation


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