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. Author manuscript; available in PMC: 2016 Sep 19.
Published in final edited form as: Mol Cell Biochem. 2013 Jan 30;376(1-2):163–173. doi: 10.1007/s11010-013-1564-3

Figure 4. hGLUT9A chimeric proteins show an inability of the GLUT9A N-terminus to redirect an apical sorting signal.

Figure 4

The chimeric proteins were stably overexpressed in MDCK cells and visualized by immunofluorescence using a polyclonal antibody to the N-terminus of hGLUT9A. (A) hGLUT9A seen basolaterally (top) (B) hGLUT9A N-terminus spliced onto GLUT1, seen basolaterally (middle) (C) hGLUT9A N-terminus spliced onto GLUT3, seen apically (bottom). D. ATB-BMPA photolabeling of the basolateral surfaces was consistent with the confocal finding. GLUT9a protein was seen on the basolateral surface in Slc2a9A (1) and Slc2a9A/Slc2a1 (2), but not Slc2a9A/Slc2a3 (3). GLUT9 protein is detected as a highly glycosylated set of bands appearing as a smear between 50–75 kDa.