Abstract
The calcium-activated neutral protease calpain is activated in several pathological conditions. Calpain usually hydrolyses one or only a few peptide bonds in its substrate. One prominent substrate for calpain is spectrin and it has been shown that α-spectrin is the preferred substrate. We now show that the β-chain of spectrin is also a substrate for calpain proteolysis, and that the cleavage site in each β-subunit is located at the very C-terminal part of the molecule. Surprisingly, βIΣ1-spectrin is cleaved at a different site than βIΣ2- and βIIΣ1-spectrins despite their high degree of sequence identity.
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