Role of Insulin in Regulation of Na+-/K+-Dependent ATPase Activity and Pump Function in Corneal Endothelial Cells

2010 ◽  
Vol 51 (8) ◽  
pp. 3935 ◽  
Author(s):  
Shin Hatou ◽  
Masakazu Yamada ◽  
Yoko Akune ◽  
Hiroshi Mochizuki ◽  
Atsushi Shiraishi ◽  
...  
2009 ◽  
Vol 34 (5) ◽  
pp. 347-354 ◽  
Author(s):  
Shin Hatou ◽  
Masakazu Yamada ◽  
Hiroshi Mochizuki ◽  
Atsushi Shiraishi ◽  
Takeshi Joko ◽  
...  

2016 ◽  
Vol 42 (3) ◽  
pp. 380-385 ◽  
Author(s):  
Takatoshi Uchida ◽  
Osamu Sakai ◽  
Hirotaka Imai ◽  
Takashi Ueta

1984 ◽  
Vol 99 (2) ◽  
pp. 734-741 ◽  
Author(s):  
W A Braell ◽  
D M Schlossman ◽  
S L Schmid ◽  
J E Rothman

ATP hydrolysis was used to power the enzymatic release of clathrin from coated vesicles. The 70,000-mol-wt protein, purified on the basis of its ATP-dependent ability to disassemble clathrin cages, was found to possess a clathrin-dependent ATPase activity. Hydrolysis was specific for ATP; neither dATP nor other ribonucleotide triphosphates would either substitute for ATP or inhibit the hydrolysis of ATP in the presence of clathrin cages. The ATPase activity is elicited by clathrin in the form of assembled cages, but not by clathrin trimers, the product of cage disassembly. The 70,000-mol-wt polypeptide, but not clathrin, was labeled by ATP in photochemical cross-linking, indicating that the hydrolytic site for ATP resides on the uncoating protein. Conditions of low pH or high magnesium concentration uncouple ATP hydrolysis from clathrin release, as ATP is hydrolyzed although essentially no clathrin is released. This suggests that the recognition event triggering clathrin-dependent ATP hydrolysis occurs in the absence of clathrin release, and presumably precedes such release.


2014 ◽  
Vol 55 (3) ◽  
pp. 1213 ◽  
Author(s):  
Imad Lahdou ◽  
Christoph Engler ◽  
Stefan Mehrle ◽  
Volker Daniel ◽  
Mahmoud Sadeghi ◽  
...  

2006 ◽  
Vol 14 (4) ◽  
pp. 215-223 ◽  
Author(s):  
Wei-Li Chen ◽  
Chung-Tien Lin ◽  
Chung-Chen Yao ◽  
Yu-Hua Huang ◽  
Yu-Bin Chou ◽  
...  

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