Properties of calpastatin forms in rat brain

FEBS Letters

Pontremoli, Sandro¹  Tedesco, Ilaria¹  De Tullio, Roberta¹  Salamino, Franca¹  Sparatore, Bianca¹  Averna, Monica¹  Melloni, Edon¹ 

[1] Institute of Biological Chemistry, University of Genoa, Viale Benedetto XV, 1, 16132 Genoa, Italy

关键词: Calpastatin;    Calpain;    Rat brain;    GST;    glutathione S-transferase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    RT-PCR;    reverse transcription-polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(98)00724-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Four recombinant calpastatin forms, deduced from rat brain mRNAs and differing in the number of inhibitory repetitive domains from zero to four, were expressed and characterized for their inhibitory efficiency on μ- and m-calpain. Although the most effective one is a truncated calpastatin form composed of the N-terminal region (domain L) and a single inhibitory domain, all inhibitors are more active against μ-calpain, but are preferentially degraded and inactivated by m-calpain. The protein form composed exclusively of a domain L is deprived of any inhibitory activity but prevents inhibition of calpain by the other calpastatin forms, indicating that this calpastatin region could be relevant in the recognition of the proteinase. A calpastatin form having molecular properties similar to those of the recombinant truncated calpastatin, has also been found in rat brain. It does not derive from proteolysis of a higher molecular mass precursor. The expression of multiple calpastatin forms may be relevant for the specific modulation of the different calpain isozymes normally present in a single cell type.

【 授权许可】

Unknown