A dual role for integrin-linked kinase in platelets: regulating integrin function and alpha-granule secretion. by Tucker, K, Sage, T, Stevens, J, Jordan, P, Jones, S, Barrett, N, St-Arnaud, R, Frampton, J, Dedhar, S, Gibbins, J

“…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. …”

Integrin linked kinase is important in platelet signalling and function by Tucker, K, Stevens, J, Jordan, P, Sage, T, Jones, S, Barrett, N, St-Arnaud, R, Frampton, J, Dedhar, S, Gibbins, J

Integrin‐linked kinase regulates the rate of platelet activation and is essential for the formation of stable thrombi by Jones, C, Tucker, K, Sasikumar, P, Sage, T, Kaiser, W, Moore, C, Emerson, M, Gibbins, J

“… <p style="text-align:justify;"> <b>Background:</b> Integrin‐linked kinase (ILK) and its associated complex of proteins are involved in many cellular activation processes, including cell adhesion and integrin signaling. …”

Integrin-linked kinase regulates the rate of platelet activation and is essential for the formation of stable thrombi. by Jones, C, Tucker, K, Sasikumar, P, Sage, T, Kaiser, W, Moore, C, Emerson, M, Gibbins, J

“…BACKGROUND: Integrin-linked kinase (ILK) and its associated complex of proteins are involved in many cellular activation processes, including cell adhesion and integrin signaling. …”

Mass spectrometry of platelet lipid raft fractions reveals a substantial pool of active integrin aIIb beta 3 by Jones, C, Tucker, K, Barrett, E, Wen, Y, Leake, D, Gibbins, J

Platelet endothelial cell adhesion molecule-1 inhibits platelet response to thrombin and von Willebrand factor by regulating the internalization of glycoprotein ib via AKT/glycogen synthase kinase-3/dynamin and integrin αiibβ3 by Jones, C, Sage, T, Moraes, L, Vaiyapuri, S, Hussain, U, Tucker, K, Barrett, N, Gibbins, J

“…<br/> <b>Approach and Results—</b> Here, we show that the activation of PECAM-1 inhibits fibrinogen binding to integrin αIIbβ3 and P-selectin surface expression in response to thrombin (0.1–3 U/mL) but not thrombin receptor–activating peptides SFLLRN (3×10−7–1×10−5 mol/L) and GYPGQV (3×10−6–1×10−4 mol/L). …”

Platelet endothelial cell adhesion molecule-1 inhibits platelet response to thrombin and von Willebrand factor by regulating the internalization of glycoprotein Ib via AKT/glycogen synthase kinase-3/dynamin and integrin αIIbβ3. by Jones, C, Sage, T, Moraes, L, Vaiyapuri, S, Hussain, U, Tucker, K, Barrett, N, Gibbins, J

“…APPROACH AND RESULTS: Here, we show that the activation of PECAM-1 inhibits fibrinogen binding to integrin αIIbβ3 and P-selectin surface expression in response to thrombin (0.1-3 U/mL) but not thrombin receptor-activating peptides SFLLRN (3×10(-7)-1×10(-5) mol/L) and GYPGQV (3×10(-6)-1×10(-4) mol/L). …”

Clot retraction. by Tucker, K, Sage, T, Gibbins, J

“…Plasma clots should retract away from the sides of a glass tube within a few hours allowing the rapid characterization of outside-in signaling through platelet integrin α(IIb)β(3). In this chapter, we describe the role of platelets in fibrin clot retraction and provide a detailed description of the methods used to assess this process.…”

Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets. by Tucker, K, Kaiser, W, Bergeron, A, Hu, H, Dong, J, Tan, T, Gibbins, J

“…Further analysis of HIP-55 revealed that this adaptor protein becomes increasingly associated with both Syk and integrin beta3 upon platelet activation. Analysis of HIP-55 deficient platelets revealed reduced fibrinogen binding upon thrombin stimulation, suggesting HIP-55 to be an important regulator of platelet function.…”