Biochemical evidence of glycosylation of CaV3.2 channels.

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Supplemental figure 1. The structures of the wild-type (left) and aberrant Man5GlcNAc2 N-glycan (right) is shown.

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Biochemical evidence of glycosylation of CaV3.2 channels. Biochemical evidence of glycosylation of CaV3.2 channels. Immunoblotting with FLAG antibody reveals a shift in apparent molecular weight of NH2-terminal fragment of CaV3.2 channel (bottom arrow) but not full channel (top arrow). Note that treatment with PNGase-F and Endo F1 but not Endo F2 and Endo F3 caused an obvious change in mobility of FLAG-labeled NH2-terminal fragment of CaV3.2 from ~60 to 50 KDa. Using mass spectrometry, we confirmed that the deglycosylated NH2-terminal fragment of CaV3.2 channels recognized by FLAG antibodies contains most of the repeat I of CaV3.2 channel (data not shown). N-term., NH2-terminal. Peihan Orestes et al. Diabetes 2013;62:3828-3838 ©2013 by American Diabetes Association