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Capillary electrophoresis electrospray ionization-mass spectrometry for peptidomics-based processing site determination.

Abstract：

:Proteolytic cleavage at specific sites is a key event that modulates protein functions in biological processes. These cleavage sites are identified through mass spectrometry-based peptidomics of overlapping peptide sequences. Here, we assessed to what extent a recent capillary electrophoresis (CE) system interfaced with electrospray ionization-mass spectrometry (ESI-MS) contributes to identifying endogenous peptides present in a biological sample. Peptides released by a human endocrine cell line stimulated for secretion was analyzed for uncovering potential processing sites created by proprotein convertases (PCs) that cleave precursors in the secretory pathway. CE-ESI-MS was conducted, in comparison to a standard liquid chromatography (LC)-ESI-MS platform. LC and CE complemented each other in elucidating processing sites that match PC consensus sequences from known substrates. We suggest that the precursors BIGH3, STC1, LFNG, QSOX1 and CYTC are potential substrates for PCs, and that a CE-ESI system would come in handy and garner greater recognition as a robust tool in peptidomics.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tsuchiya T,Nakayama A,Kawamura T,Sasaki K

doi

10.1016/j.bbrc.2020.09.056

subject

Has Abstract

pub_date

2020-12-17 00:00:00

pages

872-878

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(20)31797-6

journal_volume

533

pub_type

杂志文章

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