Galanin enhanced insulin-mediated intracellular signaling by regulating the stability of membrane-localized insulin/IR.

Previous studies have shown that insulin has the important regulatory effect on the intestinal tract. However, until now, the biological properties of insulin on intestinal cell has not been revealed. Therefore, in the current research, we first studied the cell characteristics and signaling profiles of insulin in the intestinal cell model, and found that insulin can be internalized into the cytoplasm in a time-dependent manner. After internalization, insulin transported into different type of endosomes. More importantly, we explored the effect of galanin on insulin-mediated signaling pathways (galanin is a polypeptide composed of 29 amino acid residues, galanin is widely distributed in the central and peripheral nervous system and has a variety of biological activities), and found that galanin can increase insulin sensitivity by regulating insulin receptor (IR)-mediated signal transduction pathways. We further study the potential molecular mechanism by which galanin enhances insulin sensitivity, and found that galanin could increase the time of insulin acting on the cell membrane. Further experiments showed that galanin could stabilize the membrane-localized insulin/IR, which may be an important new potential mechanism by which galanin improves the biological activity of insulin. This study laid the foundation for exploring the relationship between galanin and insulin sensitivity.