Extensive characterization of the human salivary basic proline-rich protein family by top-down mass spectrometry

Padiglia, Alessandra

First

;Orrù, Roberto;Boroumand, Mozhgan;Olianas, Alessandra;Manconi, Barbara;Sanna, Maria Teresa;Desiderio, Claudia;Iavarone, Federica;Liori, Barbara;Messana, Irene;Castagnola, Massimo;Cabras, Tiziana

Last

2018-01-01

---

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 A41â†' 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.