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Titolo:
ACTIVATION OF CELIAC-DISEASE IMMUNE-SYSTEM BY SPECIFIC ALPHA-GLIADIN PEPTIDES
Autore:
LAHDEAHO ML; VAINIO E; LEHTINEN M; PARKKONEN P; PARTANEN J; KOSKIMIES S; MAKI M;
Indirizzi:
UNIV TAMPERE,SCH MED,POB 607 SF-33101 TAMPERE FINLAND UNIV TURKU,DEPT DERMATOL SF-20500 TURKU FINLAND NATL PUBL HLTH INST HELSINKI FINLAND FINNISH RED CROSS & BLOOD TRANSFUS SERV SF-00310 HELSINKI FINLAND UNIV TAMPERE,INST MED TECHNOL SF-33101 TAMPERE FINLAND TAMPERE UNIV HOSP,DEPT PEDIAT TAMPERE FINLAND
Titolo Testata:
Cereal chemistry
fascicolo: 5, volume: 72, anno: 1995,
pagine: 475 - 479
SICI:
0009-0352(1995)72:5<475:AOCIBS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
DERMATITIS-HERPETIFORMIS; E1B PROTEIN; ANTIGLIADIN ANTIBODIES; A-GLIADIN; GLUTEN; ADENOVIRUS-12; ASSOCIATION; SEQUENCES; INVITRO; SPRUE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
M.L. Lahdeaho et al., "ACTIVATION OF CELIAC-DISEASE IMMUNE-SYSTEM BY SPECIFIC ALPHA-GLIADIN PEPTIDES", Cereal chemistry, 72(5), 1995, pp. 475-479

Abstract

Two different gliadin molecules (designated alpha-gliadin and alpha/beta-gliadin) were synthesized as 52 and 58 ten amino acid (aa) long overlapping peptides for the determination of their B-cell epitopes. Monoclonal antibodies and human serum pools revealed two epitopes common for both gliadins (peptide 14 aa:s 66-75 and peptides 34 alpha aa:s 166-175, 36 alpha/beta aa:s 176-185) and two unique epitopes (alpha-gliadin peptides 48 aa:s 236-245 and alpha/beta-gliadin peptide 52 aa:s 256-275). In addition, peptide 9 (QPYPQPQPFP) aa:s 41-50 and peptide 42 (LGQGSFRPSQ) aa:s 206-215 were detectable by monoclonal antibodies andserum pools from patients with untreated celiac disease but not by serum pools from disease control patients who had antigliadin antibodies. Patients with celiac disease were also studied for their human leukocyte antigen (HLA) class II status (the presence of genetically determined proteins on antigen-presenting cells that are important for immunological recognition). Antigliadin antibody response to peptide QPYPQPQPFP was restricted by celiac disease (and HLA class II) because relative amounts of the antipeptide antibodies were significantly (P < 0.05) increased in celiac disease patients. The HLA alleles DQA10501 and DQB10201 are strongly associated with celiac disease. The difference between patients with celiac disease and healthy control subjects withregard to peptide QPYPQPQPFP suggest that this region in the gliadin molecule is of pathogenetic importance in celiac disease.

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Documento generato il 27/11/20 alle ore 22:04:45