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001-es BibID:	BIBFORM002290
Első szerző:	Garcia-Horsman, J. Arturo
Cím:	Deficient activity of mammalian prolyl oligopeptidase on the immunoactive peptide digestion in coeliac disease / J. Arturo Garcia-Horsman, Jarkko I. Venäläinen, Olli Lohi, I. Seppo Auriola, Ilma R. Korponay-Szabó, Katri Kaukinen, Markku Mäki, Pekka T. Männistö
Dátum:	2007
Megjegyzések:	Objective. Gliadin digestion-resistant peptides are harmful in coeliac disease (CD), and initiate an autoimmune reaction that cause a cascade of symptoms. The role of the endogenous prolyl oligopeptidase (POP) is still not clear, and its activity over gliadin immunoactive peptides has not been fully established. Our objective was therefore to determine the endogenous POP protein level, tissue distribution and total activity in normal and CD epithelia, to evaluate tissue peptidase activity over gliadin peptides, and compare this with activities of mammalian POP and rat intestinal extracts. Material and methods. POP was assayed in biopsy preparations enzymatically and by Western blot analysis. Distribution was studied by immunohistochemistry using a specific POP antibody. Peptide cleavage was followed by mass spectroscopy-highperformance liquid chromatography (MS-HPLC). Results. There was no difference in POP activity between normal and CD samples, but those from active CD subjects had an even higher ability to degrade the 33-mer peptide than those from treated CD and healthy humans. POP locates intracellularly in epithelia, similarly to dipeptidyl peptidase IV (DPPIV), but the latter is clearly found in normal microvilli but less so in diseased microvilli. Mammalian POP is unable to digest 33-mer peptide, which, conversely, is a POP inhibitor. Rat intestine is more effective than human intestine in cleaving the 33-mer peptide. However, the products are still harmful epitopes. A surplus of POP eliminates 12-mer and 19-mer peptide products. Conclusions. The results rule out a causative role of POP in the pathogenesis of CD and strongly suggest that other peptidases are needed to eliminate gliadin-derived, immunoactive and toxic peptides larger than 33-mer, which is a POP inhibitor.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban coeliac disease digestion gliadin peptidase prolyl oligopeptidase
Megjelenés:	Scandinavian Journal of Gastroenterology 42 : 5 (2007), p. 562-571. -
További szerzők:	Venäläinen, Jarkko I. Lohi, Olli Auriola, I. Seppo Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Kaukinen, Katri Mäki, Markku Männistö, Pekka T.
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001-es BibID:	BIBFORM044272
Első szerző:	Rauhavirta, Tiina
Cím:	Epithelial transport and deamidation of gliadin peptides : a role for coeliac disease patient immunoglobulin A / Rauhavirta, T., Qiao, S.-W., Jiang, Z., Myrsky, E., Loponen, J., Korponay-Szabó, I. R., Salovaara, H., Garcia-Horsman, J. A., Venäläinen, J., Männistö, P. T., Collighan, R., Mongeot, A., Griffin, M., Mäki, M., Kaukinen, K., Lindfors, K.
Dátum:	2011
ISSN:	0009-9104
Megjegyzések:	In coeliac disease, the intake of dietary gluten induces small-bowel mucosal damage and the production of immunoglobulin (Ig)A class autoantibodies against transglutaminase 2 (TG2). We examined the effect of coeliac patient IgA on the apical-to-basal passage of gluten-derived gliadin peptides p31-43 and p57-68 in intestinal epithelial cells. We demonstrate that coeliac IgA enhances the passage of gliadin peptides, which could be abolished by inhibition of TG2 enzymatic activity. Moreover, we also found that both the apical and the basal cell culture media containing the immunogenic gliadin peptides were able to induce the proliferation of deamidation-dependent coeliac patient-derived T cells even in the absence of exogenous TG2. Our results suggest that coeliac patient IgA could play a role in the transepithelial passage of gliadin peptides, a process during which they might be deamidated.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Clinical And Experimental Immunology. - 164 : 1 (2011), p. 127-136. -
További szerzők:	Qiao, Shuo-Wang Jiang, Z. Myrsky, Essi Loponen, J. Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Salovaara, H. Garcia-Horsman, J. Arturo Venäläinen, Jarkko I. Männistö, Pekka T. Collighan, Russell Mongeot, Alexandre Griffin, Martin Mäki, Markku Kaukinen, Katri Lindfors, Katri
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