Erythrocyte ankyrin binds to β spectrin [21], protein 4.2 [22] and the cytoplasmic domain of band 3 (cdb3) [23] and has three domains: the N-terminal membrane-binding domain, the spectrin-binding domain, and the C-terminal regulatory domain [24]. The membrane-binding domain, which includes a fragment of D34 that binds to protein 4.2 and cdb3, is comprised of 24 tandem repeats of 33
Tedizolid that form a superhelical spiral [25]. These repeats exhibit tertiary-structure-based elasticity and behave as a linear and fully reversible spring as revealed by atomic force microscopy (Fig. 1E) [26]. Having a calpain cleavage site within the C-terminal regulatory domain may render ankyrin sensitive to enzymatic degradation, conformational changes, and lowering binding affinity after cleavage [27]. Since
erythrocytes lack intracellular calcium stores, the elevation of intracellular calcium levels must stem from a calcium influx [28]. It has been reported that removal of extracellular glucose may deplete cellular ATP and incubation with Ca2+in vitro may increase the intracellular Ca2+, resulting in programmed cell death [29].
