Calpain‐induced proteolysis of β‐spectrins

FEBS Letters

Backman, Lars¹  Löfvenberg, Lars¹ 

[1] Department of Biochemistry, Umeå University, S-901 87 Umeå, Sweden

关键词: Spectrin;    Calpain;    Proteolysis;    Neuron;   

DOI  :  10.1016/S0014-5793(98)01697-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown