Comprehensive analysis of the N and C terminus of endogenous serum peptides reveals a highly conserved cleavage site pattern derived from proteolytic enzymes.
10.1007/s13238-012-2934-4
- Author:
Fangjun WANG
1
;
Jun ZHU
;
Lianghai HU
;
Hongqiang QIN
;
Mingliang YE
;
Hanfa ZOU
Author Information
1. CAS Key Lab of Separation Sciences for Analytical Chemistry, National Chromatographic Research and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
- Publication Type:Journal Article
- MeSH:
Carcinoma, Hepatocellular;
blood;
diagnosis;
Chromatography, High Pressure Liquid;
Chromatography, Reverse-Phase;
Humans;
Liver Neoplasms;
blood;
diagnosis;
Mass Spectrometry;
Nanotechnology;
Peptide Hydrolases;
metabolism;
Peptides;
blood;
Protein Structure, Tertiary;
Proteome;
analysis;
Proteomics;
Silicon Dioxide;
chemistry;
Time Factors
- From:
Protein & Cell
2012;3(9):669-674
- CountryChina
- Language:English
-
Abstract:
The human serum proteome is closely associated with the state of the body. Endogenous peptides derived from proteolytic enzymes cleaving on serum proteins are widely studied due to their potential application in disease-specific marker discovery. However, the reproducibility of peptidome analysis of endogenous peptides is significantly influenced by the proteolytic enzymes within body fluids, thereby limiting the clinical use of the endogenous peptides. We comprehensively investigated the N and C terminus of endogenous peptides using peptidomics. The cleavage site patterns of the N and C terminus and adjacent sites from all the identified endogenous peptides were highly conserved under different sample preparation conditions, including long-term incubation at 37°C and pretreatment with repeated freeze-thaw cycles. Furthermore, a distinguishable cleavage site pattern was obtained when a different disease serum was analyzed. The conserved cleavage site pattern derived from proteolytic enzymes holds potential in highly specific disease diagnosis.
