Immunological identification and characterization of the desmosomal cadherin Dsg2 in coupled and uncoupled epithelial cells and in human tissues

1996 ◽  
Vol 60 (2) ◽  
pp. 99 ◽  
Author(s):  
Stephan Schäfer ◽  
Sabine Stumpp ◽  
W. W. Franke
2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Dongmei Lai ◽  
Minhua Xu ◽  
Qiuwan Zhang ◽  
Yifei Chen ◽  
Ting Li ◽  
...  

2008 ◽  
Vol 283 (39) ◽  
pp. 26428-26435 ◽  
Author(s):  
Takeshi Uemura ◽  
Hagit F. Yerushalmi ◽  
George Tsaprailis ◽  
David E. Stringer ◽  
Kirk E. Pastorian ◽  
...  

2020 ◽  
Vol 249 ◽  
pp. 108848
Author(s):  
Jianing Chen ◽  
Yaru Cui ◽  
Zemei Wang ◽  
Guangliang Liu

2012 ◽  
Vol 443 (1) ◽  
pp. 241-247 ◽  
Author(s):  
Gennaro Agrimi ◽  
Annamaria Russo ◽  
Pasquale Scarcia ◽  
Ferdinando Palmieri

The essential cofactors CoA, FAD and NAD+ are synthesized outside the peroxisomes and therefore must be transported into the peroxisomal matrix where they are required for important processes. In the present study we have functionally identified and characterized SLC25A17 (solute carrier family 25 member 17), which is the only member of the mitochondrial carrier family that has previously been shown to be localized in the peroxisomal membrane. Recombinant and purified SLC25A17 was reconstituted into liposomes. Its transport properties and kinetic parameters demonstrate that SLC25A17 is a transporter of CoA, FAD, FMN and AMP, and to a lesser extent of NAD+, PAP (adenosine 3′,5′-diphosphate) and ADP. SLC25A17 functioned almost exclusively by a counter-exchange mechanism, was saturable and was inhibited by pyridoxal 5′-phosphate and other mitochondrial carrier inhibitors. It was expressed to various degrees in all of the human tissues examined. Its main function is probably to transport free CoA, FAD and NAD+ into peroxisomes in exchange for intraperoxisomally generated PAP, FMN and AMP. The present paper is the first report describing the identification and characterization of a transporter for multiple free cofactors in peroxisomes.


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