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Virchows Archiv
Published in: Virchows Archiv 6/2005

01-06-2005 | Original Article

Localization of tissue transglutaminase and N (epsilon)-(gamma) -glutamyl lysine in duodenal cucosa during the development of mucosal atrophy in coeliac disease

Authors: Wahiba Sakly, Badreddine Sriha, Ibtissem Ghedira, Françoise Bienvenu, Abdelkarim Ayadi, Mohamed Tahar Sfar, Alain Lachaux, Sadok Korbi, Jacques Bienvenu, Nicole Fabien

Published in: Virchows Archiv | Issue 6/2005

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Abstract

Expression and transamidation activity of tissue transglutaminase (tTG) may be involved in the morphological modifications leading to the mucosal atrophy observed in coeliac disease (CD). We aimed to investigate the localization of tTG within the duodenal mucosa during the development of villous atrophy. The localization and level of expression of Nɛ-(γ-glutamyl) lysine isopeptides which could reflect the transamidation activity of tTG were also analyzed. tTG and Nɛ-(γ-glutamyl) lysine were localized using an immunohistochemical technique on duodenal biopsies obtained from 75 patients with CD and 51 subjects with normal mucosa (control group). The number of cases displaying tTG-expressing cells in the basement membrane and lamina propria was significantly higher in CD patients than in the control group. Moreover, the intensity of tTG staining in these areas was higher in CD. In contrast, the number of biopsies with tTG-expressing enterocytes was significantly lower in CD than in the control group. There was no difference in Nɛ-(γ-glutamyl) lysine between the two populations. Tissue transglutaminase was differently expressed in the various areas of the mucosa according to the stage of atrophy, whereas the localization and the intensity of the labelling of Nɛ-(γ-glutamyl) lysine isopeptides did not show any modification. The preferential localization in the basement membrane and lamina propria may reflect the involvement of tTG in the development of mucosal atrophy in CD.
Literature
1.
Aeschlimann D, Thomazy V (2000) Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases. Connect Tissue Res 41:1–27PubMed
2.
Birckbichler PJ, Dowben RM, Matacic S, Loewy AG (1973) Isopeptide bonds in membrane proteins from eukaryotic cells. Biochim Biophys Acta 291:149–155PubMed
3.
Bruce SE, Bjarnason I, Peters TJ (1985) Human jejunal transglutaminase: demonstration of activity enzyme kinetics and substrate specificity with special relation to gliadin and celiac disease. Clin Sci 68:573–579PubMed
4.
Brusco G, Muzi P, Ciccocioppo R, Biagi F, Cifone MG, Corazza GR (1999) Transglutaminase and coeliac disease: endomysial reactivity and small bowel expression. Clin Exp Immunol 118:371–375CrossRefPubMed
5.
Ciccocioppo R, Di Sabatino A, Ara C, Biagi F, Perilli M, Amicosante G, Cifone MG, Corazza GR (2003) Gliadin and tissue transglutaminase complexes in normal and coeliac duodenal mucosa. Clin Exp Immunol 134:516–524CrossRefPubMed
6.
Dieterich W, Ehnis T, Bauer M, Donner P, Volta I (1997) Identification of tissue transglutaminase as the auto-antigen of celiac disease. Nat Med 3:797–803CrossRefPubMed
7.
El Alaoui S, Legastelois S, Roch AM, Chantepie J, Quash G (1991) Transglutaminase activity and N epsilon (gamma glutamyl) lysine isopeptide levels during cell growth: an enzymatic and immunological study. Int J Cancer 48:221–226PubMed
8.
El Alaoui S, Mian S, Lawry J, Quash G, Griffin M (1992) Cell cycle kinetics, tissue transglutaminase and programmed cell death (apoptosis). FEBS Lett 311:174–178CrossRefPubMed
9.
Ehrmann J, Kolek A, Kod’ousek R, Zapletalova J, Lisova S, Murray PG, Drabek J, Kolar Z (2003) Immunohistochemical study of the apoptotic mechanisms in the intestinal mucosa during children’s coeliac disease. Virchows Arch 442:453–461PubMed
10.
Esposito C, Paparo F, Caputo I, Porta R, Salvati VM, Mazzarella G, Auricchio S, Troncone R (2003) Expression and enzymatic activity of small intestinal tissue transglutaminase in celiac disease. Am J Gastroenterol 98:1813–1820CrossRefPubMed
11.
Fesus L, Thomazy V, Falus A (1987) Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett 224:104–108PubMed
12.
Fleckenstein B, Molberg O, Qiao SW, Schmid DG, Von der Mulbe F, Elgstoen K, Jung G, Sollid LM (2002) Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation process. J Biol Chem 277:34109–34116CrossRefPubMed
13.
Folk JE, Finlayson JS (1977) The ɛ-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases. Adv Protein Chem 31:1–133PubMed
14.
Gaudry CA, Verderio E, Jones RA, Smith C, Griffin M (1999) Tissue transglutaminase is an important player at the surface of human endothelial cells: evidence for its externalization and its colocalization with the beta (1) integrin. Exp Cell Res 252:104–113CrossRefPubMed
15.
Hansson T, Ulfgren AK, Lindroos E, DannAEus A, Dahlbom I, Klareskog L (2002) Transforming growth factor-;β (TGF-β) and tissue transglutaminase expression in the small intestine in children with coeliac disease. Scand J Immunol 56:530–537PubMed
16.
Melino G, Piacentini M (1998) Tissue transglutaminase in cell death: a downstream or a multifunctional upstream effector? FEBS Lett 430:59–63PubMed
17.
Molberg O, McAdam S, Körner R, Quarsten H, Kristiansen C, Madsen L, Fugger L, Scott H, Noren O, Roepstorff P, Lundin KE, Sjöström H, Sollid LM (1998) Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat Med 4:713–717CrossRefPubMed
18.
Molberg O, McAdam, S, Lundin KE, Kristiansen C, Arentz-Hansen H, Kett K, Sollid LM (2001) T cells from coeliac disease lesions recognise gliadin epitopes deamidated in situ by endogenous tissue transglutaminase. Eur J Immunol 31:1317–1323CrossRefPubMed
19.
Nicholas B, Smethurst P, Verderio E, Jones R, Griffin M (2003) Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity. Biochem J 371:413–422PubMed
20.
Novak P, Man P, Tuckova L, Tlaskalova-Hogenova H, Bezouska K, Havlicek V (2002) Monitoring of in vitro deamidation of gliadin peptic fragment by mass spectrometry may reflect one of the molecular mechanisms taking place in coeliac disease development. J Mass Spectrom 37:507–511CrossRefPubMed
21.
Oliverio S, Amendela A, Rodolfo C, Spinedi A, Pacentini M (1999) Inhibition of tissue transglutaminase increases cell survival by preventing apoptosis. J Biol Chem 274:34123–34128PubMed
22.
Revised criteria for diagnosis of coeliac disease (1990) Report of Working Group of European Society of Pediatric Gastroenterology and Nutrition. Arch Dis Child 65:909–911PubMed
23.
Thomas V, Fournet G, Simonet F, Roch AM, Ceylan I, El Alaouia S, Quash G (2004) Definition of the fine specificity of the monoclonal antibody 81D4: its reactivity with lysine and polyamine isopeptide cross-links. J Immunol Methods 292:83–95CrossRefPubMed
24.
Thomazy V, Fesus L (1989) Differential expression of tissue transglutaminase in human cells. An immunohistochemical study. Cell Tissue Res 255:215–224PubMed
Metadata
Title
Localization of tissue transglutaminase and N (epsilon)-(gamma) -glutamyl lysine in duodenal cucosa during the development of mucosal atrophy in coeliac disease
Authors
Wahiba Sakly
Badreddine Sriha
Ibtissem Ghedira
Françoise Bienvenu
Abdelkarim Ayadi
Mohamed Tahar Sfar
Alain Lachaux
Sadok Korbi
Jacques Bienvenu
Nicole Fabien
Publication date
01-06-2005
Publisher
Springer-Verlag
Published in
Virchows Archiv / Issue 6/2005
Print ISSN: 0945-6317
Electronic ISSN: 1432-2307
DOI
https://doi.org/10.1007/s00428-005-1237-z

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