Kivonat:
BACKGROUND AND OBJECTIVES: Heat shock protein (HSP) 72, a known
chaperone, has potential epithelial barrier protecting,
antiapoptotic, and immune system regulatory effects; therefore,
our aim was to study its involvement in the pathology of celiac
disease (CD). PATIENTS AND METHODS: Duodenal biopsy specimens
were collected from children with untreated and treated CD and
from controls. mRNA expression, protein level, and localization
of HSP72 were determined. RESULTS: Elevated HSP72 mRNA
expression and higher protein levels were found in the duodenal
mucosa of children with untreated CD as well as in children with
treated CD compared with those in controls. In the duodenal
mucosa of children with treated CD, HSP72 mRNA expression was
decreased and HSP72 protein levels were lower than those in
children with untreated CD. We detected intensive HSP72
staining in the villous enterocytes and immune cells of the
lamina propria in the duodenal villi of children with untreated
CD compared with that in controls. CONCLUSIONS: The increased
expression and altered localization of HSP72 in CD indicate that
HSP72 should have a role in protection against gliadin-induced
cytotoxicity. HSP72 may exert antiapoptotic effect and
contribute to preservation of intestinal epithelial barrier
integrity. Moreover, HSP72 as a ligand of TLR2 and TLR4 may
promote innate immune responses and warn the cells of the
potential injury.