Both Heat Shock Protein 70 and Heat Shock Protein 90 Expression are Increased at the Protein Level in Adults with Untreated Celiac Disease

To date, there has been little research into the expression of two of the major heat shock proteins; hsp70 and hsp90 in untreated Celiac Disease (CD). To study these aims, sections from duodenal biopsies from patients with untreated CD and patients without CD were immuno-stained against hsp70 and hsp90 and both percentage positive tissue area and mean fluorescence intensity of each protein was calculated. Expression of HSF1 was then determined using qRT-PCR. In this small pilot study we showed that in untreated CD, a greater percentage of duodenal mucosal tissue stained positive for hsp70 and hsp70 itself was elevated in concentration. Additionally in untreated CD, a smaller percentage of tissue stained positive for hsp90 whilst the concentration of hsp90 was elevated. HSFI, a major upstream regulator of these proteins, was shown to be qualitatively upregulated in untreated CD suggesting that increased expression of hsp70 and hsp90 was driven by HSFl. At present, it is unclear if the roles of hsp70 and hsp90 in CD are beneficial or harmful and given the hsps ability to exhibit cytoprotective and immunoregulatory functions, more attention on their roles in inflammatory autoimmune disorders such as CD is warranted.