Truncated cystatin C in cerebrospiral fluid: Technical artefact or biological process?

被引：68

作者：

Carrette, O

Burkhard, PR

Hughes, S

Hochstrasser, DF

Sanchez, JC

机构：

[1] Univ Hosp Geneva, Biomed Proteom Res Grp, Geneva, Switzerland

[2] Sch Med, Geneva, Switzerland

[3] Univ Hosp Geneva, Dept Neurol, Geneva, Switzerland

[4] Univ Hosp Geneva, Cent Clin Chem Lab, Geneva, Switzerland

来源：

PROTEOMICS | 2005年 / 5卷 / 12期

关键词：

cystatin C; protein stability; protein storage;

D O I：

10.1002/pmic.200402039

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Cystatin C, a low molecular weight cysteine proteinase inhibitor present in human body fluids at physiological concentrations, is more expressed in cerebrospinal fluid (CSF) than in plasma. Mass spectrometric characterization showed that after 3 months of storage of human CS F at 20 degrees C, cystatin C was cleaved in the peptide bond between R8 and L9 and lost its eight N-termini amino acids, whereas this cleavage did not occur when stored at -80 degrees C. This truncation occurred in all CSF samples studied irrespective of the underlying neurological status, indicating a storage-related artefact rather than a physiological or pathological processing of the protein. These results stress the importance of optimal preanalytical storage conditions of any sample prior to proteomics studies.

引用

收藏

页码：3060 / 3065

页数：6

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