TY  - JOUR
A1  - Piontek, J.
A1  - Winkler, Lars
A1  - Bal, M. S.
A1  - Lassowski, Birgit
A1  - Mueller, Sandra L.
A1  - Gast, Klaus
A1  - Blasig, Ingolf E.
T1  - Investigating of homophilic interactions of the tight junction proteins occludin and claudin-5
Y1  - 2004
ER  - 
TY  - JOUR
A1  - Walter, Juliane K.
A1  - Castro, Victor Manuel
A1  - Voss, M.
A1  - Gast, Klaus
A1  - Rueckert, C.
A1  - Piontek, J.
A1  - Blasig, Ingolf E.
T1  - Redox sensitivity of the dimerization of occludin
N2  - Occludin is a self-associating transmembrane tight junction protein affected in oxidative stress. However, its function is unknown. The cytosolic C-terminal tail contains a coiled coil-domain forming dimers contributing to the self- association. Studying the hypothesis that the self-association is redox-sensitive, we found that the dimerization of the domain depended on the sulfhydryl concentration of the environment in low-millimolar range. Under physiological conditions, monomers and dimers were detected. Masking the sulfhydryl residues in the domain prevented the dimerization but affected neither its helical structure nor cylindric shape. Incubation of cell extracts containing full-length occludin with sulfhydryl reagents prevented the dimerization; a cysteine/alanine exchange mutant also did not show dimer formation. This demonstrates, for the first time, that disulfide bridge formation of the domain is involved in the occludin dimerization. It is concluded that the redox-dependent dimerization of occludin may play a regulatory role in the tight junction assembly under physiological and pathological conditions.
Y1  - 2009
UR  - http://www.springerlink.com/content/a0w10t7jgn01lk6h/
SN  - 1420-682X
ER  -