Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells.

Mishra, R., Grzybek, M., Niki, T., Hirashima, M., Simons, K.
Journal   Proc Natl Acad Sci USA.
Analytes Measured  
Matrix Tested   Cell lysates, assay buffer
Year   2010
Volume   107
Page Numbers   17633-8
Application   Cytokines and Chemokines
Galectins are unconventionally secreted lectins that participate in the formation of glycoprotein lattices that perform a variety of cell surface functions. Galectins also bind glycosphingolipid headgroups with as yet unclear implications for cellular physiology. We report a specific interaction between galectin-9 and the Forssman glycosphingolipid (FGL) that is important for polarizing Madin-Darby canine kidney epithelial cells. Galectin-9 knockdown leads to a severe loss of epithelial polarity that can be rescued by addition of the recombinant protein. The FGL glycan is identified as the surface receptor that cycles galectin-9 to the Golgi apparatus from which the protein is recycled back to the apical surface. Together our results suggest a model wherein such glycosphingolipid-galectin couples form a circuit between the Golgi apparatus and the cell surface that in an epithelial context facilitates the apical sorting of proteins and lipids.

View Publications
Browse Our Products

By Analytes
By Applications
Customer Service/Orders

Scientific/Technical Support

Instrument Support

Company Headquarters