Calpain Inhibitor-like Fraction in Rabbit Cerebrospinal Fluid is probably an Oligopeptide

We have proved before that μ-calpain can be a promising autogenous agent to replace chymopapain in chemonucleolysis treatment. Even in the case of accidental intrathecal injection, the undesirable neural damage of calpain can be neutralized by normal cerebrospinal fluid (CSF). The aim of this study...

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Bibliographic Details
Published in:Biomedical Research 2003/12/01, Vol.24(6), pp.317-324
Main Authors: LIU, Naxin, KODAMA, Hirotaka, BANNO, Yoshiko, MORITA, Masaji, SHIMIZU, Katsuji
Format: Article
Language:English
Subjects:
Amino acid sequence
Calpain
Cerebrospinal fluid
Chloroform
Chromatography
Chymopapain
Digestion
Gel filtration
Inhibitors
Membrane proteins
Membrane structure
Molecular weight
Paper chromatography
Pheochromocytoma cells
Platelets
Proteins
Proteolysis
Rabbits
Thermal stability
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Summary:We have proved before that μ-calpain can be a promising autogenous agent to replace chymopapain in chemonucleolysis treatment. Even in the case of accidental intrathecal injection, the undesirable neural damage of calpain can be neutralized by normal cerebrospinal fluid (CSF). The aim of this study was to characterize this unknown calpain inhibitor-like component in the CSF of normal rabbits. A heat-stable low molecular weight fraction in the CSF was identified. It was not extracted by chloroform solution, but labile to protease digestion. It inhibited the calpain proteolysis of microtubule-associating protein-2 (MAP-2) and membrane structure proteins of platelets and PC12 cells. It can block the autolytic activation of native human erytluocyte μ-calpain, where the conversion of the large subunit of μ-calpain from the 80-kDa form to the 76-kDa form was obstructed, with accumulation of the intermediate 78-kDa form. A possible calpain inhibition mechanism was discussed. After purification by paper chromatography, gel filtration and reverse phase chromatography, the composition of the calpain inhibitor was investigated. An oligopeptide with molecular weight about 800 Da was identified as a novel calpain inhibitor by partial amino acid sequence.
ISSN:0388-6107
1880-313X
DOI:10.2220/biomedres.24.317