CONICET | Buscador de Institutos y Recursos Humanos

UDP-Glc:glycoprotein glucosyltransferase (now known as UGGT1) is a central key of the quality control mechanism that senses protein folding in the endoplasmic reticulum (ER), which normally operates in a cell. In case of homeostasis dysregulations, misfolded proteins can accumulate generating ?ER stress?, what in turn induces a compensatory response known as ?unfolded protein response? (UPR). UPR can get the cell back to basal conditions or can activate apoptosis pathways and contribute to cell inflammation. UGGT1 is induced during an UPR. The existence of a second isoform of UGGT was reported in 2000. In 2013, our group published the first report demonstrating that UGGT2 is biologically active in the mouse, which was later supported by other authors for humans. Up to the present, there are no reports about its biological function, its functional relationship with UGGT1 or the mechanisms that regulate its expression. In the present study we analyzed the influence of inflammatory conditions on the expression of each UGGT isoform. Considering that several evidences demonstrated that ER stress contributes to the perpetuation of inflammatory bowel diseases (IBD), in this work we employed a model of chronic intestinal inflammation induced by acoustic stress (AS) previously developed by us. The AS model consists of exposing mice to 24h of noise (4 pulses/min, 300Hz-70dB). Mice were killed: 1) after AS; 2) three weeks after AS; 3) mice were submitted to AS once a week during a month and then were killed. The control group did not receive AS. Small intestine was isolated from all groups. UGGT1/ UGGT2 expression was analyzed by immunohistochemistry and western-blot and the level of expression of the mRNA coding for UGGT1/UGGT2 by qRTPCR. Results showed that UGGTs are moderately expressed in normal conditions mainly in the epithelial lining and crypts. UGGT1 expression increases in all groups respect to the control (groups 1, 2 and 3 vs C, p

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