HPLC-ESI-MS top-down analysis of salivary peptides of preterm newborns evidenced high activity of some exopeptidases and convertases during late fetal development

Mozhgan Boroumand, Federica Iavarone, Barbara Manconi, Luisa Pieroni, Viviana Greco, Giovanni Vento, Chiara Tirone, Claudia Desiderio, Antonella Fiorita, Gavino Faa, Irene Messana, Tiziana Cabras, Alessandra Olianas, Massimo Castagnola

Research output: Contribution to journalArticlepeer-review

Abstract

To have information on the proteolytic activity of convertases and exo-peptidases on human salivary proteins, this study investigated the relative amounts of the truncated proteoforms in the saliva of preterm newborns and compared them with the relative amounts measured in saliva of at-term newborns, of babies (0–10 years old) and of adults. Results indicated that convertase(s), acting on acidic proline-rich proteins and histatin 3, and carboxypeptidase(s) acting on acidic proline-rich proteins, P–C peptide, histatin 6 and statherin were many folds more active in preterm newborns than in the other groups. Conversely, the aminopeptidase responsible for the removal of the N-terminal Asp residue of statherin was not active in preterm newborns, becoming active only several months after the normal term of delivery. The high activity of convertases determined in preterm newborns suggests that it is required for the molecular events connected to the fetus development, and encourages further studies devoted to the characterization of their specific substrates.

Original languageEnglish
Article number121429
JournalTalanta
Volume222
DOIs
Publication statusPublished - Aug 2020

Keywords

  • Histatins
  • Newborns
  • Proline-rich proteins
  • Proteolysis
  • Salivary proteins
  • Statherin

ASJC Scopus subject areas

  • Analytical Chemistry

Fingerprint Dive into the research topics of 'HPLC-ESI-MS top-down analysis of salivary peptides of preterm newborns evidenced high activity of some exopeptidases and convertases during late fetal development'. Together they form a unique fingerprint.

Cite this