The interaction of dietary fibres with disulphide bonds (S-S) and a potential strategy to reduce the toxicity of the gluten proteins in coeliac disease
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Dosyalar
Tarih
2012
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
With a prevalence of 1% in western populations, coeliac disease (CD) is one of the
better understood human leukocyte antigen system (HLA) linked disorders (Green
and Cellier 2007). Despite the fact that CD shares immunological features with
inflammatory bowel disease, it is characterized by: (1) a defined trigger (prolamins
from wheat, barley and rye and in some individuals, oats); (2) the presence of HLA
class II genes, HLA-DQ2 or HLA-DQ8, and (3) the generation of circulating auto antibodies to the enzyme tissue transglutaminase (TG2). TG2 catalyses the formation
of a covalent bond between protein free amino groups and the g-carboxamide groups
of glutamine residues, which constitute some 30-40 mol%, of the prolamins, this increases their affinity to HLA-DQ2 or HLA-DQ8 proteins (Schuppan 2000). As a
result, CD4 T-helper 1 T-cell activation occurs, which can result in intestinal mucosal
inflammation, malabsorption, and numerous secondary complications. When
conducting severity assessments of coeliac disease, duodenal histology showing
intraepithelial lymphocytosis, crypt hyperplasia, and various degrees of villous atrophy,
in conjunction with clinical observations, are considered to be the gold standard for
diagnosis.
Açıklama
Anahtar Kelimeler
Coeliac Disease, Gluten Proteins, Dietary Fibres, Disulphide Bonds
Kaynak
Biotechnology and Genetic Engineering Reviews
WoS Q Değeri
N/A
Scopus Q Değeri
Q2
Cilt
28
