Mapping of Transglutaminase-2 Sites of Human Salivary Small Basic Proline-Rich Proteins by HPLC-High-Resolution ESI-MS/MS

Mozhgan Boroumand, Alessandra Olianas, Barbara Manconi, Simone Serrao, Federica Iavarone, Claudia Desiderio, Luisa Pieroni, Gavino Faa, Irene Messana, Massimo Castagnola, Tiziana Cabras

Research output: Contribution to journalArticlepeer-review

Abstract

Because of the distinctive features of the oral cavity, the determination of the proteins involved in the formation of the "oral protein pellicle" is demanding. The present study investigated the susceptibility of several human basic proline-rich peptides, named P-H, P-D, P-F, P-J, and II-2, as substrates of transglutaminase-2. The reactivity of the P-C peptide and statherin was also investigated. Peptides purified from human whole saliva were incubated with the enzyme in the presence or in the absence of monodansyl-cadaverine. Mass spectrometry analyses of the reaction products highlighted that P-H and P-D (P32 and A32 variants) were active substrates, II-2 was less reactive, and P-F and P-J showed very low reactivity. P-C and statherin were highly reactive. All of the peptides formed cyclo derivatives, and only specific glutamine residues were involved in the cycle formation and reacted with monodansyl-cadaverine: Q29 of P-H, Q37 of P-D, Q21 of II-2, Q41 of P-C, and Q37 of statherin were the principal reactive residues. One or two secondary glutamine residues of only P-H, P-D P32, P-C, and statherin were hierarchically susceptible to the reaction with monodansyl-cadaverine. MS and MS/MS data were deposited to the ProteomeXchange Consortium (http://www.ebi.ac.uk/pride) via the PRIDE partner repository with the data set identifier PXD014658.

Original languageEnglish
JournalJournal of Proteome Research
DOIs
Publication statusAccepted/In press - Jan 1 2019

Keywords

  • basic proline-rich peptides
  • human saliva
  • mass spectrometry
  • monodansyl-cadaverine
  • transglutaminase-2

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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