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. 2015 Aug 4;5(8):e612. doi: 10.1038/tp.2015.102

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Copyright © 2015 Macmillan Publishers Limited

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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The β2_52 kDa GABA_AR subunit isoform is N-glycosylated in postmortem human cortex. Representative images of western blots probed for the β2 GABA_AR subunit in total homogenate, ER and SYN fractions with and without N-glycans cleaved by treatment with the deglycosylating enzyme PNGase F and corresponding graphs of β2 GABA_AR subunit isoform protein expression as a percentage of total β2 GABA_AR subunit in each lane. In brief, subcellular fractions generated from cortical homogenates were denatured and deglycosylated with PNGase F. Image Studio software was used to measure the signal intensity of protein bands at 52, 50 and 48 kDa in each lane. The signal intensity of each isoform was then divided by the sum of signal intensities for all the three isoforms to determine the percentage of total β2 GABA_AR subunit expressed in the lane. After deglycosylation with PNGase F, the percentage of β2_52 kDa GABA_AR is greatly reduced with a corresponding increase of β2_50 kDa GABA_AR expressed in the SYN fraction. The calculated percentage of β2_48 kDa GABA_AR in the ER fraction is also reduced after PNGase F treatment; however, this is likely an artifact due to the low signal intensity values for protein bands measured in those lanes. ER, endoplasmic reticulum; GABA_AR, γ-aminobutyric acid type A receptor; PNGase F, peptide N-glycosidase F; SCZ, schizophrenia; SYN, synapse.