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001-es BibID:BIBFORM044301
Első szerző:Kaukinen, Katri
Cím:Small-bowel mucosal transglutaminase 2-specific IgA deposits in coeliac disease without villous atrophy : a prospective and randomized clinical study / Kaukinen Katri, Peräaho Markku, Collin Pekka, Partanen Jukka, Woolley Nina, Kaartinen Tanja, Nuutinen Tuula, Halttunen Tuula, Mäki Markku, Korponay-Szabo Ilma
Dátum:2005
ISSN:0036-5521
Megjegyzések:OBJECTIVE:In coeliac disease, autoantibodies directed against transglutaminase 2 are produced in small-bowel mucosa, and they have been found to be deposited extracellularly. The aim of this study was to investigate whether such mucosal IgA deposits are important in the diagnostic work-up of early-stage coeliac disease without small-bowel mucosal villous atrophy.MATERIAL AND METHODS:Forty-one adults suspected of coeliac disease owing to increased density of mucosal gamma(delta)+ intraepithelial lymphocytes but normal villous morphology were randomized to gluten challenge or a gluten-free diet for 6 months. Clinically and histologically verified gluten dependency was compared with existence of small-bowel mucosal transglutaminase 2-specific extracellular IgA deposits and (coeliac disease-type) HLA DQ2 and DQ8; 34 non-coeliac subjects and 18 patients with classical coeliac disease served as controls.RESULTS:Of the 41 patients, 5 in the challenge group and 6 in the gluten-free diet group were clinically gluten sensitive; all 11 had HLA DQ2 or DQ8. Ten of these 11 patients showed transglutaminase 2-targeted mucosal IgA deposits, which were dependent on gluten consumption. Minimal IgA deposits were seen in only 3 out of 30 patients with suspected coeliac disease without any clinically detected gluten dependency. The deposits were found in all classical coeliac patients and in none of the non-coeliac control subjects.CONCLUSIONS:Clinically pertinent coeliac disease exists despite normal small-bowel mucosal villous architecture. Mucosal transglutaminase 2-specific IgA deposits can be utilized in detecting such patients with genetic gluten intolerance
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Scandinavian Journal Of Gastroenterology. - 40 : 5 (2005), p. 564-572. -
További szerzők:Peräaho, Markku Collin, Pekka Partanen, Jukka Woolley, Nina Kaartinen, Tanja Nuutinen, Tuula Halttunen, Tuula Mäki, Markku Korponay-Szabó Ilma (1959-) (gyermekgyógyász)
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2.

001-es BibID:BIBFORM044305
Első szerző:Korponay-Szabó Ilma (gyermekgyógyász)
Cím:Tissue Transglutaminase Is the Target in Both Rodent and Primate Tissues for Celiac Disease - Specific Autoantibodies / Korponay-Szabo Ilma R., Sulkanen Satu, Halttunen Tuula, Maurano Francesco, Rossi Mauro, Mazzarella Giuseppe, Laurila Kaija, Troncone Riccardo, Maki Markku
Dátum:2000
ISSN:0277-2116
Megjegyzések:BACKGROUND:Endomysial antibodies have recently been shown to react with tissue transglutaminase. This study was undertaken to investigate whether the tissue distribution of transglutaminase is also compatible with reticulin, jejunal, and fibroblast autoantibody binding patterns.METHODS:Sera from patients with and without celiac disease, monoclonal tissue transglutaminase antibodies, and sera from mice parenterally immunized against commercially available tissue transglutaminase, transglutaminase complexed with gliadin, or gliadin were used in indirect immunofluorescence and double-staining studies using both rodent and primate tissues as substrates. Also, antibody competition, affinity chromatography, and potassium thiocyanate extraction studies were undertaken.RESULTS:Tissue transglutaminase antibody binding patterns were identical with the extracellular binding patterns seen with celiac patient sera. Human umbilical cord-derived fibroblasts exhibited both cytoplasmic and extracellular matrix staining. Double staining with patients' sera and tissue transglutaminase antibodies showed complete overlapping. Tissue transglutaminase effectively absorbed reticulin-endomysial antibodies from celiac sera, and patients' sera blocked the staining of the monoclonal tissue transglutaminase antibodies. Potassium thiocyanate extraction abolished the staining patterns, but they were elicited again after readdition of tissue transglutaminase.CONCLUSIONS:Reticulin, endomysial, and jejunal antibodies detect transglutaminase in both rodent and primate tissues, indicating that these tissue autoantibodies are identical
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Pediatric Gastroenterology And Nutrition. - 31 : 5 (2000), p. 520-527. -
További szerzők:Sulkanen, Satu Halttunen, Tuula Maurano, Francesco Rossi, Mauro Mazzarella, Giuseppe Laurila, Kaija Troncone, Riccardo Mäki, Markku
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3.

001-es BibID:BIBFORM044330
Első szerző:Korponay-Szabó Ilma (gyermekgyógyász)
Cím:Tranglutaminase-alapú coeliakia diagnosztikus vizsgálatok hazai eredményei / Korponay-Szabo I., Halttunen T., Lőrincz M., Szalai Zs., B. Kovács J., Maki M.
Dátum:2001
ISSN:0017-5900
Tárgyszavak:Orvostudományok Klinikai orvostudományok magyar nyelvű folyóiratközlemény hazai lapban
coeliakia
Megjelenés:Gyermekgyógyászat 53 : 3 (2001), p. 254-259. -
További szerzők:Halttunen, Tuula Lőrincz Margit Szalai Zsuzsanna B. Kovács Judit Mäki, Markku
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4.

001-es BibID:BIBFORM042703
035-os BibID:PMID:15082580
Első szerző:Korponay-Szabó Ilma (gyermekgyógyász)
Cím:In vivo targeting of intestinal and extraintestinal transglutaminase 2 by coeliac autoantibodies / I. R. Korponay-Szabo, T. Halttunen, Z. Szalai, K. Laurila, R. Király, J. B. Kovács, L. Fésüs, M. Mäki
Dátum:2004
ISSN:0017-5749
Megjegyzések:BACKGROUND: IgA class serum autoantibodies against type 2 (tissue) transglutaminase (TG2) bind to both intestinal and extraintestinal normal tissue sections in vitro, eliciting endomysial, reticulin, and jejunal antibody reactions. It is not known whether similar binding also occurs in coeliac patients in vivo, and may thereby contribute to disease manifestations. AIMS: To investigate intestinal and extraintestinal coeliac tissues for the presence of in vivo bound TG2 specific IgA and its relation to small intestinal mucosal atrophy. PATIENTS: We investigated jejunal samples with normal villous morphology from 10 patients with developing coeliac disease who subsequently progressed to a flat lesion, from 11 patients with dermatitis herpetiformis, and from 12 non-coeliac controls. Six extrajejunal biopsy samples (liver, lymph node, muscle, appendix), obtained based on independent clinical indications from patients with active coeliac disease, were also studied. METHODS: Double colour immunofluorescent studies for in situ IgA, TG2, and laminin were performed. IgA was eluted from tissue sections and tested for TG2 specificity by enzyme linked immunosorbent assay and indirect immunofluorescence. RESULTS: IgA (in one IgA deficient case IgG) deposition on extracellularly located TG2 was detected in jejunal and extrajejunal specimens of all coeliac patients, and also in seven of 11 dermatitis herpetiformis patients, of whom two had no circulating endomysial antibodies. IgA eluted from extraintestinal coeliac tissues was targeted against TG2. CONCLUSIONS: Coeliac IgA targets jejunal TG2 early in disease development even when endomysial antibodies are not present in the circulation. Extraintestinal target sites of coeliac IgA further indicate that humoral immunity may have a pathogenetic role.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Gut. - 53 : 5 (2004), p. 641-648. -
További szerzők:Halttunen, Tuula Szalai Zoltán Laurila, Kaija Király Róbert (1975-) (biológus) Kovács J. Béla Fésüs László (1947-) (orvos biokémikus) Mäki, Markku
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5.

001-es BibID:BIBFORM028773
Első szerző:Korponay-Szabó Ilma (gyermekgyógyász)
Cím:Missing endomysial and reticulin binding of coeliac antibodies in transglutaminase 2 knockout tissues / I. R. Korponay-Szabó, K. Laurila, Zs. Szondy, T. Halttunen, Z. Szalai, I. Dahlbom, I. Rantala, J. B. Kovács, L. Fésüs, M. Mäki
Dátum:2003
ISSN:0017-5749
Megjegyzések:Autoantibodies against transglutaminase 2 (TG2) are thought to be responsible for the endomysial (EMA), reticulin (ARA), and jejunal antibody (JEA) tissue binding of serum samples from coeliac patients but the exclusive role of TG2 in these staining patterns has not yet been established. AIMS: To evaluate whether antigens other than TG2 contribute to EMA/ARA/JEA reactions. PATIENTS: Serum samples from 61 EMA/ARA/JEA positive untreated patients with coeliac disease, 40 dermatitis herpetiformis patients, and 34 EMA/ARA/JEA negative non-coeliac controls were tested. METHODS: TG2 knockout (TG2-/-) and wild-type mouse oesophagus, jejunum, liver, and kidney sections, and TG2-/- sections coated with human recombinant TG2 were used as substrates in single and double immunofluorescent studies for patient IgA binding and tissue localisation of TG2, fibronectin, actin, and calreticulin. RESULTS: None of the patient serum samples elicited EMA, ARA, or JEA binding in TG2-/- morphologically normal tissues. In contrast, 96 of 101 gluten sensitive patient samples (95%) reacted with wild-type mouse tissues and all 101 reacted in EMA/ARA/JEA patterns with TG2-/- mouse tissues coated with human TG2. Serum IgA binding to TG2-/- smooth muscle cells was observed in low titres in 31.1%, 27.5%, and 20.5%, and to TG2-/- epithelium in 26.3%, 5.0%, and 8.8% of coeliac, dermatitis herpetiformis, and control samples, respectively. These positivities partly colocalised with actin and calreticulin but not with TG2 or fibronectin. CONCLUSIONS: EMA/ARA/JEA antibody binding patterns are exclusively TG2 dependent both in coeliac and dermatitis herpetiformis patients. Actin antibodies are responsible for some positivities which are not part of the EMA/ARA/JEA reactions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Gut 52 : 2 (2003), p. 199-204. -
További szerzők:Laurila, Kaija Szondy Zsuzsanna (1959-) (molekuláris sejtbiológus, biokémikus) Halttunen, Tuula Szalai Zoltán Dahlbom, Ingrid Rantala, I. Kovács B. J. Fésüs László (1947-) (orvos biokémikus) Mäki, Markku
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6.

001-es BibID:BIBFORM044307
Első szerző:Sulkanen, Satu
Cím:Tissue transglutaminase autoantibody enzyme-linked immunosorbent assay in detecting celiac disease / Sulkanen Satu, Halttunen Tuula, Laurila Kaija, Kolho Kaija-Leena, Korponay-Szabó Ilma R., Sarnesto Annikki, Savilahti Erkki, Collin Pekka, Mäki Markku
Dátum:1998
ISSN:0016-5085
Megjegyzések:BACKGROUND & AIMS: Tissue transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue transglutaminase autoantibodies can be considered specific for celiac disease. METHODS:Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS:The calcium-activated tissue transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue transglutaminase antibodies showed complete overlap. CONCLUSIONS:Calcium-activated tissue transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue transglutaminase seems to be the target self-antigen for endomysial antibodies.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Gastroenterology. - 115 : 6 (1998), p. 1322-1328. -
További szerzők:Halttunen, Tuula Laurila, Kaija Kolho, Kaija-Leena Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Sarnesto, Annikki Savilahti, Erkki Collin, Pekka Mäki, Markku
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