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Stress-induced glucocorticoid elevation is a highly conserved response amongvertebrates. This facilitates stress adaptation and the mode of action involvesactivation of the intracellular glucocorticoid receptor leading to themodulation of target gene expression. However, this genomic effect is slowacting and, therefore, a role for glucocorticoid in the rapid response tostress is unclear. Here we show that stress levels of cortisol, the primaryglucocorticoid in teleosts, rapidly fluidizes rainbow trout (Oncorhynchusmykiss) liver plasma membranes in vitro. This involved incorporation of thesteroid into the lipid domains, as cortisol coupled to a membrane impermeablepeptide moiety, did not affect membrane order. Studies confirmed that cortisol,but not sex steroids, increases liver plasma membrane fluidity. Atomic forcemicroscopy revealed cortisol mediated changes to membrane surface topographyand viscoelasticity confirming changes to membrane order. Treating trouthepatocytes with stress levels of cortisol led to the modulation of cellsignaling pathways, including the phosphorylation status of putative PKA, PKCand AKT substrate proteins within 10 minutes. The phosphorylation by proteinkinases in the presence of cortisol was consistent with that seen with benzylalcohol, a known membrane fluidizer. Our results suggest that biophysicalchanges to plasma membrane properties, triggered by stressor inducedglucocorticoid elevation, act as a nonspecific stress response and may rapidlymodulate acute stress-signaling pathways.

Novel Nongenomic Signaling by Glucocorticoid May Involve Changes to Liver Membrane Order in Rainbow Trout