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  • Genetic and functional analysis of pyroglutamyl-peptidase I in coeliac disease.

Genetic and functional analysis of pyroglutamyl-peptidase I in coeliac disease.

European journal of gastroenterology & hepatology (2006-05-17)
Alienke J Monsuur, Dariusz Stepniak, Begoña Diosdado, Martin C Wapenaar, Maria Luisa Mearin, Frits Koning, Cisca Wijmenga
ABSTRACT

Coeliac disease (CD) is an enteropathy caused by an immune reaction towards wheat gluten and similar proteins from barley and rye. It was shown that some gluten peptides spontaneously form N-terminal L-pyroglutamate. This modification could potentially make gluten more resistant to proteolytic degradation within the intestine. Pyroglutamyl-peptidase I (PGPEPI) is an enzyme that hydrolytically removes the L-pyroglutamyl residues that render the modified proteins and peptides more sensitive to degradation by other proteases. Interestingly, we found that the PGPEP1 gene is located in a CD susceptibility locus. As an impaired enzyme function caused by genetic alterations might increase the amount of immunogenic gluten peptides, we conducted a comprehensive functional genomics analysis of PGPEP1, including DNA sequencing, genetic association testing, and quantifying RNA expression. We also determined the enzymatic activity of PGPEPI in duodenal biopsies. Our results uniformly indicate that PGPEP1 is not involved in the aetiology and pathology of CD.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, 7-13 mU (per vial)
Sigma-Aldrich
Pyroglutamate Aminopeptidase from Pyrococcus furiosus, recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein