Abstract
After incubation with glucose a dramatic change in the intracellular distribution of glycogen synthase was observed in rat hepatocytes. Confocal laser scanning microscopy showed that glycogen synthase existed diffusely in the cytosol of control cells, whereas in cells incubated with glucose it accumulated at the cell periphery. Colocalization analysis between glycogen synthase immunostaining and actin filaments showed that the change in glycogen synthase distribution induced by glucose correlated with a marked increase in the co-distribution of the two proteins, indicating that, in response to glucose, glycogen synthase moves to the actin-rich area close to the membrane. When glycogen synthase was immunostained with rabbit anti-(glycogen synthase) and Protein A-colloidal gold, few particles were observed close to the membrane in control cells. In contrast, in cells incubated with glucose most of the gold particles were found near the membrane, confirming that glycogen synthase had moved to the cell cortex. Furthermore, in agreement with the glycogen synthase distribution, glycogen deposition appeared to be more active at the periphery of the cell.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.