Glucocorticoid Receptor Mediates Cortisol Regulation of Glycogen Metabolism in Gills of the Euryhaline Tilapia (<i>Oreochromis mossambicus</i>)

Abstract

In this study, we investigated the effects of cortisol on the regulation of the glycogen metabolism biomarkers glycogen synthase (GS) and glycogen phosphorylase (GP) in the glycogen-rich cells of the gills of tilapia (Oreochromis mossambicus). In the gills of tilapia, GP, GS, and glycogen were immunocytochemically colocalized in a specific group of glycogen-rich cells adjacent to the gills’ main ionocytes and mitochondria-rich cells. Cortisol plays a vital role in the regulation of physiological functions in animals, including energy metabolism, respiration, immune response, and ion regulation. However, no studies have elucidated the mechanisms regulating cortisol and glycogen-rich cells in the gills. Therefore, we treated tilapia larvae with exogenous cortisol and a glucocorticoid receptor (GR) antagonist to investigate the regulatory mechanisms between cortisol and glycogen-rich cells in the gills. Our results showed that cortisol promoted the expression of gill glycogen phosphorylase isoform (GPGG) mRNA via GR, whereas the GS gene expression remained unaffected. We also found that GR mRNA was colocalized with some glycogen-rich cells in the gills, further confirming our hypothesis that cortisol directly acts on glycogen-rich cells in the gills of tilapia and regulates glycogen metabolism by promoting GPGG mRNA expression.

Keywords

• cortisol
• glycogen-rich cell
• glycogen phosphorylase
• glycogen synthase
• ionocytes
• glucocorticoid receptor