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. 2021 Jul 28;163(4):753–764. doi: 10.1097/j.pain.0000000000002421

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Copyright © 2021 The Author(s). Published by Wolters Kluwer Health, Inc. on behalf of the International Association for the Study of Pain.

This is an open access article distributed under the terms of the Creative Commons Attribution-Non Commercial-No Derivatives License 4.0 (CCBY-NC-ND), where it is permissible to download and share the work provided it is properly cited. The work cannot be changed in any way or used commercially without permission from the journal.

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Figure 3. — Protein arginine methyltransferase 7 affects the current density of Na_V1.9 by promoting its accumulation on the cell membrane. (A) Representative whole-cell sodium currents evoked by voltage from Scn11a ^−/− mouse DRG neurons electroporated with SCN11A or SCN11A and PRMT7. (B) Current–voltage relationships in the indicated experimental groups. The peak current density (normalized by membrane capacitance) was statistically analysed (mock, n = 15; hNa_V1.9, n = 25; and hNa_V1.9 + hPRMT7, n = 23), and significant differences were tested by two-way ANOVA, followed by a post hoc Bonferroni test; infection × voltage: F(32, 948) = 5.846, P < 0.0001; infection: F(2, 948) = 66.28, P < 0.0001; voltage: F(15, 948) = 19.39, P<0.0001; *P < 0.05, **P < 0.01, and ***P < 0.001 compared with the mock group. (C) Representative whole-cell mNa_V1.9 currents evoked by voltage from Scn11a ^+/+ mouse small DRG neurons treated without (control) or with DS-437. (D) Quantification of the peak mNa_V1.9 current density in the experimental and control groups (control, n = 16; 10 μM DS-437, n = 13; 100 μM DS-437, n = 19). Significant differences were tested by two-way ANOVA, followed by a post hoc Bonferroni test; DS-437 × voltage: F(30, 693) = 3.237, P < 0.0001; DS-437: F(2, 693) = 27.49, P < 0.0001; voltage: F(15, 693) = 79.98, P < 0.0001; ***P < 0.001 compared with the control. (E) Schematic representation of the chimeric proteins. (F) HEK293T cells transiently expressing HA-CD4-hLoop1 and GFP-hPRMT7 or mock-transfected GFP cells were harvested and lysed, the whole-cell lysates (WCLs) were cleared of debris, and the postnuclear supernatant was fractionated into the membrane (Mem) and cytosolic (Cyto) fractions with a kit. Aliquots from all stages of fractionation were analysed by immunoblotting with the indicated antibodies. Na⁺K⁺-ATPase was used as a cell-surface–protein control. Quantification of Western blotting data showed that hPRMT7 significantly increased the amount of chimeras in plasma membranes (G) but did not affect the total expression level of the chimeric proteins (H). Data were statistically analysed by the unpaired Student t test; *P < 0.05 compared with GFP. All studies were repeated at least 3 times. DRG, dorsal root ganglion; hNa_V1.9, human Na_V1.9; PRMT7, protein arginine methyltransferase 7.