scholarly journals Vascular growth responses to chronic arterial occlusion are unaffected by myeloid specific focal adhesion kinase (FAK) deletion

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Joshua L. Heuslein ◽  
Kelsey P. Murrell ◽  
Ryan J. Leiphart ◽  
Ryan A. Llewellyn ◽  
Joshua K. Meisner ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Arterial Occlusion ◽  
Growth Responses ◽  
Vascular Growth ◽  
Chronic Arterial Occlusion

scholarly journals Impaired thrombin-induced platelet activation and thrombus formation in mice lacking the Ca2+-dependent tyrosine kinase Pyk2

Blood ◽  
2013 ◽  
Vol 121 (4) ◽  
pp. 648-657 ◽  
Author(s):  
Ilaria Canobbio ◽  
Lina Cipolla ◽  
Alessandra Consonni ◽  
Stefania Momi ◽  
Gianni Guidetti ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Focal Adhesion Kinase ◽  
Platelet Activation ◽  
Focal Adhesion ◽  
Ex Vivo ◽  
Thrombus Formation ◽  
Arterial Occlusion ◽  
In Vivo Model ◽  
Glycoprotein Vi

Abstract In the present study, we used a knockout murine model to analyze the contribution of the Ca2+-dependent focal adhesion kinase Pyk2 in platelet activation and thrombus formation in vivo. We found that Pyk2-knockout mice had a tail bleeding time that was slightly increased compared with their wild-type littermates. Moreover, in an in vivo model of femoral artery thrombosis, the time to arterial occlusion was significantly prolonged in mice lacking Pyk2. Pyk2-deficient mice were also significantly protected from collagen plus epinephrine-induced pulmonary thromboembolism. Ex vivo aggregation of Pyk2-deficient platelets was normal on stimulation of glycoprotein VI, but was significantly reduced in response to PAR4-activating peptide, low doses of thrombin, or U46619. Defective platelet aggregation was accompanied by impaired inside-out activation of integrin αIIbβ3 and fibrinogen binding. Granule secretion was only slightly reduced in the absence of Pyk2, whereas a marked inhibition of thrombin-induced thromboxane A2 production was observed, which was found to be responsible for the defective aggregation. Moreover, we have demonstrated that Pyk2 is implicated in the signaling pathway for cPLA2 phosphorylation through p38 MAPK. The results of the present study show the importance of the focal adhesion kinase Pyk2 downstream of G-protein–coupled receptors in supporting platelet aggregation and thrombus formation.

scholarly journals A role for FRNK, a selectively expressed inhibitor of focal adhesion kinase (FAK), in vascular growth and development

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Rebecca Lynn Sayers ◽  
Mauricio Rojas ◽  
Jackie E. Kylander ◽  
J. Thomas Parsons ◽  
Christopher P. Mack ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Growth And Development ◽  
Vascular Growth

Early signalling events of autophagy

2013 ◽  
Vol 55 ◽  
pp. 1-15 ◽  
Author(s):  
Laura E. Gallagher ◽  
Edmond Y.W. Chan
Keyword(s):  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Mammalian Cells ◽  
Mammalian Target Of Rapamycin ◽  
Interacting Protein ◽  
The Core ◽  
Autophagy Gene ◽  
Autophagy Induction ◽  
Cellular Pathways

Autophagy is a conserved cellular degradative process important for cellular homoeostasis and survival. An early committal step during the initiation of autophagy requires the actions of a protein kinase called ATG1 (autophagy gene 1). In mammalian cells, ATG1 is represented by ULK1 (uncoordinated-51-like kinase 1), which relies on its essential regulatory cofactors mATG13, FIP200 (focal adhesion kinase family-interacting protein 200 kDa) and ATG101. Much evidence indicates that mTORC1 [mechanistic (also known as mammalian) target of rapamycin complex 1] signals downstream to the ULK1 complex to negatively regulate autophagy. In this chapter, we discuss our understanding on how the mTORC1–ULK1 signalling axis drives the initial steps of autophagy induction. We conclude with a summary of our growing appreciation of the additional cellular pathways that interconnect with the core mTORC1–ULK1 signalling module.

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