| Literature DB >> 30064219 |
Alessandra Padiglia1, Roberto Orrù1, Mozhgan Boroumand1, Alessandra Olianas1, Barbara Manconi1, Maria Teresa Sanna1, Claudia Desiderio2, Federica Iavarone3,4, Barbara Liori1, Irene Messana2, Massimo Castagnola2,3,4, Tiziana Cabras1.
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. 55 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 S1 → A, P-Ko P36 → S, and P-Ko A41 → 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.Entities:
Keywords: basic proline-rich proteins; human saliva; mass spectrometry; top-down proteomics
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Year: 2018 PMID: 30064219 DOI: 10.1021/acs.jproteome.8b00444
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466