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Expression pattern of the endoplasmic reticulum stress protein gp96 in monophasic and chronic relapsing form of experimental autoimmune encephalomyelitis in rats

Gp96 is the endoplasmic reticulum (ER)-resident molecular chaperone, which is involved in the correction of unfolded proteins, in the activation of proteasome-dependent ER-associated degradation of the misfolded proteins and in activation of protein translation that modulates the polypeptide traffic into the ER. Furthermore, owing to its peptide chaperone capacity and ability to interact with professional antigen-presenting cells, as well as with growth factors, integrins and Toll-like receptors, it is also endowed with crucial immunological functions acting as a "danger signal" to the innate and adaptive immunity. Considering these properties, in the present study the tissue expression of gp96 was examined during the monophasic and chronic relapsing form of experimental autoimmune encephalomyelitis (CR-EAE), induced in genetically susceptible DA rats by subcutaneous injection of myelin basic protein (MBP) or bovine brain homogenate in complete Freund's adjuvant (CFA). Immunohistochemical analyses were made in periods of attacks and remissions of EAE, and the results were compared with findings in intact rats and those treated only with CFA. The data revealed that during the attacks of CR-EAE significantly diminished the constitutive gp96 expression, found in several neurons and glial cells in the brain and spinal cord of intact animals. On the contrary, the remission of disease was followed by high upregulation of gp96, mainly in the oligodendrocytes within the white matter, in the neurons of hippocampal area, as well as in the motoneurons of lumbar spinal cord, suggesting that gp96 might be involved in proteostasis and immune-related pathways linked with the reparative processes in the CNS.

Endoplasmic reticulum resident heat shock protein; gp96; monophasic and chronic relapsing experimental autoimmune encephalomyelitis; DA rats

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