cdb3Cytoplasmic Domain of Band 3 Protein
Copyright 1988-2018, All rights reserved.
References in periodicals archive ?
Caspase 3 catalyzes the specific cleavage of cdB3, NHE1, and PMCA4.
In particular, as cdB3 serves as a docking station for multiple GE, its cleavage operated by caspase 3 deprives RBCs of the fundamental and primary regulation of metabolic G6P pathways.
Caspase 3 action, once primed, mediates cleavage of the cdb3 and the [Na.sup.+]/[H.sup.+] antiporter, supporting two vicious circles, one that induces oxidative stress (for loss of cdb3, control site for the metabolic fluxes of G6P) and the other one that further increases the intracellular acidity (for loss of activity of the [Na.sup.+]/[H.sup.+] antiporter).