The surprising composition of the salivary proteome of preterm human newborn.

Federica Iavarone, Giovanni Vento, Massimo Castagnola, Rosanna Inzitari, Chiara Fanali, Claudia Desiderio, Chiara Tirone, Costantino Romagnoli, Tiziana Cabras, Barbara Manconi, Maria Teresa Sanna, Roberto Boi, Elisabetta Pisano, Alessandra Olianas, Irene Messana, Andrea Vitali, M. Pellegrini, S. Nemolato, Cw Heiznann, G. Faa

Research output: Contribution to journalArticle

Abstract

Saliva is a body fluid of a unique composition devoted to protect the mouth cavity and the digestive tract. Our high performance liquid chromatography (HPLC)-electrospray ionization-MS analysis of the acidic soluble fraction of saliva from preterm human newborn surprisingly revealed more than 40 protein masses often undetected in adult saliva. We were able to identify the following proteins: stefin A and stefin B, S100A7 (two isoforms), S100A8, S100A9 (four isoforms), S100A11, S100A12, small proline-rich protein 3 (two isoforms), lysozyme C, thymosins β(4) and β(10), antileukoproteinase, histone H1c, and α and γ globins. The average mass value reported in international data banks was often incongruent with our experimental results mostly because of post-translational modifications of the proteins, e.g. acetylation of the N-terminal residue. A quantitative label-free MS analysis showed protein levels altered in relation to the postconceptional age and suggested coordinate and hierarchical functions for these proteins during development. In summary, this study shows for the first time that analysis of these proteins in saliva of preterm newborns might represent a noninvasive way to obtain precious information of the molecular mechanisms of development of human fetal oral structures.
Original languageEnglish
Pages (from-to)N/A-N/A
JournalMOLECULAR & CELLULAR PROTEOMICS
Publication statusPublished - 2010

Keywords

  • proteome

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