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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:BIBFORM044280
Első szerző:Stenman, Satumarja M.
Cím:Secretion of celiac disease autoantibodies after in vitro gliadin challenge is dependent on small-bowel mucosal transglutaminase 2-specific IgA deposits / Stenman Satumarja M., Lindfors Katri, Korponay-Szabo Ilma R., Lohi Olli, Saavalainen Paivi, Partanen Jukka, Haimila Katri, Wieser Herbert, Maki Markku, Kaukinen Katri
Dátum:2008
ISSN:1471-2172
Megjegyzések:BACKGROUND:In celiac disease gluten, the disease-inducing toxic component in wheat, induces the secretion of autoantibodies which are targeted against transglutaminase 2 (TG2). These autoantibodies are produced in the small-intestinal mucosa, where they can be found deposited extracellularly below the epithelial basement membrane and around mucosal blood vessels. In addition, during gluten consumption these autoantibodies can also be detected in patients' serum but disappear from the circulation on a gluten-free diet. Interestingly, after adoption of a gluten-free diet the serum autoantibodies disappear from the circulation more rapidly than the small-intestinal mucosal autoantibody deposits. The toxicity of gluten and the secretion of the disease-specific autoantibodies have been widely studied in organ culture of small-intestinal biopsy samples, but results hitherto have been contradictory. Since the mucosal autoantibodies disappear slowly after a gluten-free diet, our aim was to establish whether autoantibody secretion to organ culture supernatants in treated celiac disease patient biopsies is related to the duration of the diet and further to the pre-existence of mucosal TG2-specific IgA deposits in the cultured biopsy samples.RESULTS:In the organ culture system conducted with biopsies derived from treated celiac disease patients, gliadin induced secretion of autoantibodies to culture supernatants, reduced epithelial cell height and increased the density of lamina proprial CD25+ cells. However, these changes could be demonstrated only in biopsies from short-term treated celiac disease patients, where the small-intestinal mucosal TG2-specific IgA autoantibody deposits were still present. Furthermore, in these biopsies autoantibody secretion could be stimulated fully only after a 48-hour gliadin challenge.CONCLUSION:Our results show that studies focusing on the toxic effects of gliadin in the organ culture system should be carried out with biopsy samples from short-term treated celiac disease patients who are likely still to have mucosal IgA deposits present. In addition to providing an explanation for the discrepancies in previous publications, the present study also enables further validation of the organ culture method.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Bmc Immunology. - 9 : 1 (2008), p. [6]. -
További szerzők:Lindfors, Katri Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Lohi, Olli Saavalainen, Päivi Partanen, Jukka Haimila, Katri Wieser, Herbert Mäki, Markku Kaukinen, Katri
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DOI
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