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Selenocysteine-Specific Mass Spectrometry Reveals Tissue-Distinct Selenoproteomes and Candidate Selenoproteins.

Authors :
Guo L
Yang W
Huang Q
Qiang J
Hart JR
Wang W
Hu J
Zhu J
Liu N
Zhang Y
Source :
Cell chemical biology [Cell Chem Biol] 2018 Nov 15; Vol. 25 (11), pp. 1380-1388.e4. Date of Electronic Publication: 2018 Aug 30.
Publication Year :
2018

Abstract

Selenoproteins, defined by the presence of selenocysteines (Sec), play important roles in a wide range of biological processes. All known selenoproteins are marked by the presence of Sec insertion sequence (SECIS) at their mRNA. The lack of an effective analytical method has hindered our ability to explore the selenoproteome and new selenoproteins beyond SECIS. Here, we develop a Sec-specific mass spectrometry-based technique, termed "SecMS," which allows the systematic profiling of selenoproteomes by selective alkylation of Sec. Using SecMS, we quantitatively characterized the age- and stress-regulated selenoproteomes for nine tissues from mice of different ages and mammalian cells, demonstrating tissue-specific selenoproteomes and an age-dependent decline in specific selenoproteins in brains and hearts. We established an integrated platform using SecMS and SECIS-independent selenoprotein (SIS) database and further identified five candidate selenoproteins. The application of this integrated platform provides an effective strategy to explore the selenoproteome independent of SECIS.<br /> (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Details

Language :
English
ISSN :
2451-9448
Volume :
25
Issue :
11
Database :
MEDLINE
Journal :
Cell chemical biology
Publication Type :
Academic Journal
Accession number :
30174312
Full Text :
https://doi.org/10.1016/j.chembiol.2018.08.006