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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2003

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Identification of transglutaminase-mediated deamidation sites in a recombinant alpha-gliadin by advanced mass-spectrometric methodologies

Anno di pubblicazione: 2003

Autori: Mazzeo MF;De Giulio B; Senger S; Rossi M; Malorni A; Siciliano RA.

Affiliazioni autori: Istituto di Scienze dell'Alimentazione del CNR, Avellino

Autori CNR:

  • BEATRICE DE GIULIO
  • ANTONIO MALORNI
  • MARIA FIORELLA MAZZEO
  • MAURO ROSSI
  • ROSA ANNA SICILIANO

Lingua: inglese

Abstract: Celiac disease is a permanent immune-mediated food intolerance triggered by ingestion of wheat gliadins in genetically susceptible individuals. It has been reported that tissue transglutaminase plays an important role in the onset of celiac disease by converting specific glutamine residues within gliadin fragments into glutamic acid residues. This process increases binding affinity of gliadin peptides to HLA-DQ2/DQ8 molecules, thus enhancing the immune response. The aim of the present study was to achieve a detailed structural characterization of modifications induced by transglutaminase on gliadin peptides. Therefore, structural analyses were carried out on a recombinant alpha-gliadin and on a panel of 26 synthetic peptides, overlapping the complete protein sequence. Modified glutamine residues were identified by means of advanced mass-spectrometric methodologies on the basis of MALDI-TOF-MS and tandem mass spectrometry. Results led to the identification of 19 of 94 glutamine residues present in the recombinant alpha-gliadin, which were converted into glutamic acid residues by a transglutaminase-mediated reaction. This allowed us to achieve a global view of the modifications induced by the enzyme on this protein. Furthermore, results gathered could likely be utilized as relevant information for a better understanding of processes leading to T-cell recognition of gliadin peptides involved in celiac disease.

Lingua abstract: inglese

Pagine da: 2434

Pagine a: 2442

Rivista:

Protein science Cambridge University Press,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 0961-8368

Numero volume: 12

DOI: 10.1110/ps.03185903.

Referee: Sė: Internazionale

Indicizzato da:

  • ISI Web of Science (WOS) [000186333800005]
  • PubMed [14573857]

Parole chiave:

  • mass spectrometry
  • gliadin
  • trans-glutaminase
  • coeliac disease
  • post-translational modification

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