Focal adhesion kinase as well as p130Cas and paxillin is crucially involved in the enhanced malignant properties under expression of ganglioside GD3 in melanoma cells

2008 ◽  
Vol 1780 (3) ◽  
pp. 513-519 ◽  
Author(s):  
Kazunori Hamamura ◽  
Momoko Tsuji ◽  
Yuki Ohkawa ◽  
Hideyuki Nakashima ◽  
Sayaka Miyazaki ◽  
...  
2008 ◽  
Vol 52 (6) ◽  
pp. 655-663 ◽  
Author(s):  
Jang-Chang Lee ◽  
Chih-Yen Tsai ◽  
Jung-Yie Kao ◽  
Ming-Ching Kao ◽  
Shih-Chang Tsai ◽  
...  

2013 ◽  
Vol 2013 ◽  
pp. 1-10
Author(s):  
Haw-Young Kwon ◽  
Kyoung-Sook Kim ◽  
Ji-Sue Baik ◽  
Hyung-In Moon ◽  
Ji-Won Lee ◽  
...  

Triptolide (TPL) has been shown to inhibit cell proliferation and induce apoptosis in various human cancer cells; however, the precise mechanism of apoptosis induced by TPL in human melanoma cells has not yet been elucidated. In this study, we investigated the precise mechanism underlying cytocidal effects of TPL on human melanoma cells. Treatment of human melanoma cells with TPL significantly inhibited cell growth and induced apoptosis, as evidenced by flow cytometry and annexin V-fluorescein isothiocyanate analyses. TPL increased the levels of Fas and Fas-associated death domain (FADD) and induced cleavage of Bid by activation of caspase-8 and cytochrome c release from mitochondria to the cytosol, which resulted in activation of caspase-9 and caspase-3. Moreover, TPL-induced apoptosis in SK-MEL-2 cells was mediated through dephosphorylation of focal adhesion kinase (FAK) and its cleavage by caspase-8-mediated caspase-3 activation via upregulation of Fas expression. We also found that TPL mediated the dissociation of receptor-interacting protein (RIP) from FAK and enhanced the formation of RIP/Fas complex formation initiating cell death. In conclusion, our data firstly demonstrated that TPL induces apoptosis by both extrinsic and intrinsic apoptosis pathways in human melanoma cells and identified that RIP shuttles between Fas and FAK to mediate apoptosis.


2011 ◽  
Vol 3 (1) ◽  
pp. 19-24 ◽  
Author(s):  
HIROKI OZAWA ◽  
YOSHIKO SONODA ◽  
TAKAHARU SUZUKI ◽  
NAOMI YOSHIDA-HOSHINA ◽  
MEGUMI FUNAKOSHI-TAGO ◽  
...  

2009 ◽  
Vol 285 (2) ◽  
pp. 141-150 ◽  
Author(s):  
Tao Sun ◽  
Nan Zhao ◽  
Chun-sheng Ni ◽  
Xiu-lan Zhao ◽  
Wen-zhi Zhang ◽  
...  

2013 ◽  
Vol 55 ◽  
pp. 1-15 ◽  
Author(s):  
Laura E. Gallagher ◽  
Edmond Y.W. Chan

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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