Expression and Enzymatic Activity of Small Intestinal Tissue Transglutaminase in Celiac Disease (Articolo in rivista)

Type
Label
  • Expression and Enzymatic Activity of Small Intestinal Tissue Transglutaminase in Celiac Disease (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0002-9270(03)00431-3 (literal)
Alternative label
  • Carla Esposito, Francesco Paparo, Ivana Caputo, Raffaele Porta,,Virginia M. Salvati., Giuseppe Mazzarella, Salvatore Auricchio, Riccardo Troncone, (2003)
    Expression and Enzymatic Activity of Small Intestinal Tissue Transglutaminase in Celiac Disease
    in The American journal of gastroenterology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Carla Esposito, Francesco Paparo, Ivana Caputo, Raffaele Porta,,Virginia M. Salvati., Giuseppe Mazzarella, Salvatore Auricchio, Riccardo Troncone, (literal)
Pagina inizio
  • 1813 (literal)
Pagina fine
  • 1820 (literal)
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  • 24 (literal)
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  • 98 (literal)
Rivista
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  • Le proprietà funzionali e molecolari della transglutaminasi (tTG) a livello del piccolo intestino sono in gran parte sconosciute nonostante il grosso interesse dato al suo ruolo nella malattia celiaca. In questo studio abbiamo valutato sia l’espressione della proteina, mediante tecniche immunoistochimiche, sia l’attività enzimatica in vitro ed in situ su biopsie intestinali ottenute da pazienti celiaci e da pazienti controlli. Nei pazienti celiaci non trattati a differenza dei pazienti controlli, si osservava che tTG non solo era più espressa ma era anche più attiva in aree ben definite della mucosa intestinale celiaca, soprattutto nella regione subepiteliale della lamina propria e nella matrice extracellulare. Questo dato risulta consistente con il ruolo importante della tTG nei casi di danneggiamento della mucosa intestinale, dove l’enzima va ad interagire con alcune proteine della matrice extracellulare per stabilizzare l’area lesionata. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • C Esposito,I Caputo,R Porta Department of Chemistry, University of Salerno, Salerno;G Mazzarella Institute for Food Science, CNR, Avellino, Italy; F Paparo, VM. Salvati, S Auricchio, R Troncone Department of Pediatrics and European Laboratory for the Investigation of Food-Induced Diseases, University Federico II, Naples; (literal)
Titolo
  • Expression and Enzymatic Activity of Small Intestinal Tissue Transglutaminase in Celiac Disease (literal)
Abstract
  • OBJECTIVES: The molecular and functional properties of small intestinal tissue transglutaminase are largely unknown despite growing interest because of its role in celiac disease (CD). In this study, we aimed to evaluate tissue transglutaminase expression and enzymatic activity in bioptic fragments obtained from the duodenum of untreated individuals with CD and from control subjects. METHODS: Analysis of tissue transglutaminase mRNA expression was performed by reverse transcription-polymerase chain reaction (RT-PCR). The presence of the enzyme in bioptic fragments as well as in homogenates from CD patients and controls was revealed by immunohistochemistry and Western blot, respectively, using the antitissue transglutaminase CUB 7402 clone. To evaluate in situ transglutaminase activity, sections of bioptic fragments were incubated in the presence of 5 mmol/L CaCl(2) with 5-(biotinamido)pentylamine or, alternatively, with a biotinylated glutamine-containing hexapeptide (TVQQEL) and the biotinylated 31-43 A-gliadin-derived peptide. RESULTS: Tissue transglutaminase mRNA levels were 1.0-fold higher (p < 0.05) in CD patients than in controls. Immunohistochemistry and in situ demonstration of enzymatic activity in celiac mucosa clearly showed an increased expression of active tissue transglutaminase in the extracellular matrix of the subepithelial region and in the enterocytes. Staining of the biotinylated 31-43 A-gliadin peptide in the same area of tissue transglutaminase suggested the presence of lysine-donor substrates in intestinal mucosa. CONCLUSIONS: Tissue transglutaminase is more expressed and active in defined areas of the small intestinal mucosa from patients with CD. The presence in the celiac mucosa of proteins able to act as amine-donor substrates suggests that tissue transglutaminase-mediated post-translational modification of proteins cross-linked with gliadin peptides may represent a pathogenic mechanism of CD. (literal)
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