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Extensive Characterization of the Human Salivary Basic Proline-Rich Protein Family by Top-Down Mass Spectrometry

Authors :
Barbara Manconi
Tiziana Cabras
Claudia Desiderio
Alessandra Olianas
Alessandra Padiglia
Mozhgan Boroumand
Federica Iavarone
Irene Messana
Massimo Castagnola
Roberto Orru
Maria Teresa Sanna
Barbara Liori
Source :
Journal of proteome research, 17 (2018): 3292–3307. doi:10.1021/acs.jproteome.8b00444, info:cnr-pdr/source/autori:Padiglia, Alessandra; Orru, Roberto; Boroumand, Mozhgan; Olianas, Alessandra; Manconi, Barbara; Sanna, Maria Teresa; Desiderio, Claudia; Iavarone, Federica; Liori, Barbara; Messana, Irene; Castagnola, Massimo; Cabras, Tiziana/titolo:Extensive Characterization of the Human Salivary Basic Proline-Rich Protein Family by Top-Down Mass Spectrometry/doi:10.1021%2Facs.jproteome.8b00444/rivista:Journal of proteome research (Print)/anno:2018/pagina_da:3292/pagina_a:3307/intervallo_pagine:3292–3307/volume:17
Publication Year :
2018

Abstract

Human basic proline-rich proteins and basic glycosylated proline-rich proteins, encoded by the polymorphic PRB1-4 genes and expressed only in parotid glands, are the most complex family of adult salivary proteins. The family includes 11 parent peptides/proteins and more than 6 parent glycosylated proteins, but a high number of proteoforms with rather similar structures derive from polymorphisms and post-translational modifications. SS new components of the family were characterized by top-down liquid chromatography mass spectrometry and tandem-mass platforms, bringing the total number of proteoforms to 109. The new components comprise the three variants P-H S-1 -> A, P-Ko P-36 -> S, and P-Ko A(41) -> S and several of their naturally occurring proteolytic fragments. The paper represents an updated reference for the peptides included in the heterogeneous family of proteins encoded by PRB1/PRB4. MS data are available via ProteomeXchange with the identifier PXD009813.

Details

ISSN :
15353907
Volume :
17
Issue :
9
Database :
OpenAIRE
Journal :
Journal of proteome research
Accession number :
edsair.doi.dedup.....67541abd7910d7d8e25282174341512c
Full Text :
https://doi.org/10.1021/acs.jproteome.8b00444