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. 2021 Aug 6;8(4):ENEURO.0069-21.2021. doi: 10.1523/ENEURO.0069-21.2021

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Copyright © 2021 Huang and Park

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license, which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Figure 1. — GPC4 is expressed on the astrocyte surface via a GPI-anchorage. A, Diagram of GPC4 sequence, protein, and posttranslational modifications. GPC4 contains an N-terminal signal peptide and GPI-anchor signal peptide for GPI-anchor attachment. Mature GPC4 is subject to furin cleavage, intrachain di-sulfide bonds, heparan sulfate attachment, and GPI-anchorage to the cell surface membrane. B, Western blotting of HA tagged GPC4 construct expressed in HEK293T cells. The ∼37-kDa band shows the HA tagged N-terminal GPC4 in the reducing condition. PI-PLC treatment in HEK293T cells drives robust release of GPC4; however, GPC4 is detected in media in the absence of PI-PLC. C, Western blotting of concentrated ACMs for endogenous GPC4, IGFBP2, and TSP1, with and without PI-PLC treatment. PI-PLC treatment strongly facilitates release of endogenous GPC4 from astrocytes. D, Biotinylation of surface GPC4 shows that pretreatment of PI-PLC removes endogenous GPC4 from the cell surface of astrocytes. Extended Data Figure 1-1 supports Figure 1.