Subjects: Biology >> Biochemistry submitted time 2020-02-11
Abstract： The chemical modifications of proteins refer to the covalent group reaction involved in its amino acid residues or chain ends, which in turn change the molecular structure and function. There are many types of molecular modifications in the human plasma proteome, such as phosphorylation, methylation, acetylation, etc. In this study, two groups of human plasma proteome at different age groups were used to compare the global chemical modifications by LC-MS/MS combined with non-limiting modification identification algorithms. A total of 4 molecular modifications were found to have statistical differences, the succinylation and phosphorylation modification of cysteine (Cys, C) and the modification of lysine (Lys, K) modification of lysine with threonine (Thr, T) were significantly higher in the old group than in the young group, while the carbamylation of lysine was lower in the young group. The sulfhydryl in the cysteine residue is an important group to form disulfide bonds and maintain the structure of the protein. All differential cysteine-related modifications may cause structural and functional changes. Lysine is a basic amino acid, and the modification of its amino group will change the charge state of the protein, which may affect the structure and function of the protein. In summary, four types of protein chemical modifications and substitutes were found to be differential in the plasma proteome in different age groups. We speculate that there is an increase in certain modified proteins in the blood of the elderly people which in turn changes the function of those proteins. This may be one of the reasons why elderly people are more likely than young people to be at risk for age-related diseases such as metabolic disease, cerebral and cardiovascular diseases, and cancer. "
Peer Review Status:
Awaiting Review
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