Glucosidase II beta subunit (GluIIβ) plays a role in autophagy and apoptosis regulation in lung carcinoma cells in a p53-dependent manner

2017 ◽  
Vol 40 (6) ◽  
pp. 579-591 ◽  
Author(s):  
Worapong Khaodee ◽  
Nichanan Inboot ◽  
Suruk Udomsom ◽  
Warunee Kumsaiyai ◽  
Ratchada Cressey
2000 ◽  
Vol 113 (5) ◽  
pp. 869-876 ◽  
Author(s):  
Y. Kikkawa ◽  
N. Sanzen ◽  
H. Fujiwara ◽  
A. Sonnenberg ◽  
K. Sekiguchi

Laminin-10/11, the laminin isoforms containing the alpha 5 chain, are major components of basement membranes of many fetal and adult tissues. Laminin-10/11 purified from the conditioned medium of human lung carcinoma cells were potent in mediating adhesion of the carcinoma cells in an integrin alpha 3 beta 1-dependent manner. To further define the type(s) of integrins involved in cell adhesion to laminin-10/11, we examined the effects of a panel of function-blocking anti-integrin antibodies on the adhesion of different cell types to laminin-10/11. Although anti-integrin beta 1 antibody inhibited the adhesion of all cell types tested, anti-alpha 3 antibody inhibited the adhesion of carcinoma and glioma cells but not fibroblastic cells. Adhesion of fibroblastic cells was inhibited, however, by a combination of anti-alpha 3 and anti-alpha 6 antibodies, suggesting that both alpha 3 beta 1 and alpha 6 beta 1 integrins function as laminin-10/11 receptors in these cells. To explore this possibility, we examined the adhesion of K562 leukemic cells transfected with integrin alpha 3 or alpha 6 subunit to laminin-10/11 or other laminin isoforms. Laminin-10/11 were potent adhesive ligands for both the alpha 3 beta 11 and alpha 6 beta 1 transfectants, whereas laminin-5 was the preferred ligand for the alpha 3 beta 1 transfectants. Upon stimulation with the activating anti-integrin beta 1 antibody, both transfectants became more adherent to the substratum regardless of the type of laminins coated, although their preference for laminin isoforms remained unaltered. K562 cells transfected with alpha 6 and beta 4 subunits were also capable of adhering to laminin-10/11, indicating that integrin alpha 6 beta 4 is another receptor for laminin-10/11. Even with lung carcinoma cells, the alpha 6-containing integrins partly contributed to adhesion to laminin-10/11 at higher coating concentrations, although non-integrin receptor(s) might also be involved under such conditions. These results indicated that laminin-10/11 are potent and versatile adhesive ligands in basement membranes capable of binding to both alpha 3 beta 1 and alpha 6 beta 1 integrins with high avidity and also to alpha 6 beta 4 integrin.


1991 ◽  
Vol 266 (28) ◽  
pp. 18771-18779
Author(s):  
M.H. Corjay ◽  
D.J. Dobrzanski ◽  
J.M. Way ◽  
J. Viallet ◽  
H. Shapira ◽  
...  

2011 ◽  
Vol 25 (7) ◽  
pp. 1082-1086 ◽  
Author(s):  
Hye-Jin Boo ◽  
Jae-Hee Hyun ◽  
Sang-Cheol Kim ◽  
Jung-Il Kang ◽  
Min-Kyoung Kim ◽  
...  

2009 ◽  
Vol 182 (5) ◽  
pp. 2795-2807 ◽  
Author(s):  
Ingrid E. Dumitriu ◽  
Donald R. Dunbar ◽  
Sarah E. Howie ◽  
Tariq Sethi ◽  
Christopher D. Gregory

2015 ◽  
Vol 117 (17) ◽  
pp. 17D123 ◽  
Author(s):  
J. Devkota ◽  
M. Howell ◽  
P. Mukherjee ◽  
H. Srikanth ◽  
S. Mohapatra ◽  
...  

2015 ◽  
Vol 27 (3) ◽  
pp. 568-577 ◽  
Author(s):  
Daisuke Iitaka ◽  
Serisha Moodley ◽  
Hiroki Shimizu ◽  
Xiao-Hui Bai ◽  
Mingyao Liu

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