The Post-Translational Modifications of Human Salivary Peptides and Proteins Evidenced by Top-Down Platforms

Author:

Messana Irene1ORCID,Manconi Barbara2ORCID,Cabras Tiziana2ORCID,Boroumand Mozhgan3ORCID,Sanna Maria Teresa2,Iavarone Federica45ORCID,Olianas Alessandra2,Desiderio Claudia1ORCID,Rossetti Diana Valeria1,Vincenzoni Federica45ORCID,Contini Cristina2ORCID,Guadalupi Giulia2ORCID,Fiorita Antonella56,Faa Gavino78ORCID,Castagnola Massimo9ORCID

Affiliation:

1. Istituto di Scienze e Tecnologie Chimiche “Giulio Natta”, Consiglio Nazionale delle Ricerche, 00168 Rome, Italy

2. Department of Life and Environmental Sciences, University of Cagliari, 09124 Cagliari, Italy

3. National Institut on Aging, NIH, Baltimore, MD 21224, USA

4. Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie, Università Cattolica del Sacro Cuore, 00168 Rome, Italy

5. Fondazione Policlinico Universitario A. Gemelli Fondazione IRCCS, 00168 Rome, Italy

6. Dipartimento di Scienze dell’Invecchiamento, Neurologiche, Ortopediche e della Testa e del Collo, Università Cattolica del Sacro Cuore, 00168 Rome, Italy

7. Unit of Pathology, Department of Medical Sciences and Public Health, University of Cagliari, 09124 Cagliari, Italy

8. Department of Biology, College of Science and Technology, Temple University, Philadelphia, PA 19122, USA

9. Proteomics Laboratory, European Center for Brain Research, (IRCCS) Santa Lucia Foundation, 00168 Rome, Italy

Abstract

In this review, we extensively describe the main post-translational modifications that give rise to the multiple proteoforms characterized to date in the human salivary proteome and their potential role. Most of the data reported were obtained by our group in over twenty-five years of research carried out on human saliva mainly by applying a top-down strategy. In the beginning, we describe the products generated by proteolytic cleavages, which can occur before and after secretion. In this section, the most relevant families of salivary proteins are also described. Next, we report the current information concerning the human salivary phospho-proteome and the limited news available on sulfo-proteomes. Three sections are dedicated to the description of glycation and enzymatic glycosylation. Citrullination and N- and C-terminal post-translational modifications (PTMs) and miscellaneous other modifications are described in the last two sections. Results highlighting the variation in the level of some proteoforms in local or systemic pathologies are also reviewed throughout the sections of the manuscript to underline the impact and relevance of this information for the development of new diagnostic biomarkers useful in clinical practice.

Publisher

MDPI AG

Subject

Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis

Reference196 articles.

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