Comprehensive analysis of the N and C terminus of endogenous serum peptides reveals a highly conserved cleavage site pattern derived from proteolytic enzymes
Protein & Cell
; (12): 669-674, 2012.
Artigo
em Inglês
| WPRIM (Pacífico Ocidental)
| ID: wpr-757236
Biblioteca responsável:
WPRO
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.
Texto completo:
Disponível
Base de dados:
WPRIM (Pacífico Ocidental)
Assunto principal:
Peptídeo Hidrolases
/
Peptídeos
/
Espectrometria de Massas
/
Fatores de Tempo
/
Sangue
/
Química
/
Cromatografia Líquida de Alta Pressão
/
Estrutura Terciária de Proteína
/
Carcinoma Hepatocelular
/
Dióxido de Silício
Tipo de estudo:
Estudo diagnóstico
/
Estudo prognóstico
Limite:
Humanos
Idioma:
Inglês
Revista:
Protein & Cell
Ano de publicação:
2012
Tipo de documento:
Artigo