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. 2021 Nov 25;49(21):12284–12305. doi: 10.1093/nar/gkab1120

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Depletion of full-length hnRNP R results in an up-regulation of the hnRNP R-ΔN isoform. (A) Absolute mRNA copy numbers of wildtype and chimeric Hnrnpr isoforms normalized to copies of Gapdh in brains of Hnrnpr⁺^/+,Hnrnpr^tm1a/+ and Hnrnpr^tm1a/tm1a mice. Data are mean ± SD (n = 4 animals). (B) qPCR analysis of Hnrnpr pre-mRNA levels using primers specific to intron 1 in brains of Hnrnpr⁺^/+, Hnrnpr^tm1a/+ and Hnrnpr^tm1a/tm1a mice. Data are mean ± SD (n = 4 animals). Statistical analysis was performed using one-way ANOVA followed by Tukey's multiple comparison test; n.s., not significant. (C, D) qPCR analysis of Hnrnpr-FL (C) or Hnrnpr-ΔN (D) levels in primary motoneurons transduced with an shRNA against exon 3 for depletion of both hnRNP R isoforms (shRNA-FL+ΔN), or with different shRNAs against exon 2 for depletion of the full-length hnRNP R isoform (shRNA-FL-A, shRNA-FL-B and shRNA-FL-C). Absolute copy numbers of Hnrnpr-FL (C) and Hnrnpr-ΔN (D) mRNA isoforms were normalized to absolute copies of Gapdh, controls were set to 1. Data are mean ± SD (n = 4 independent experiments). Statistical analysis was performed using one-way ANOVA followed by Tukey's multiple comparison test; *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001. (E) Western blot analysis of hnRNP R isoforms using a C-terminal-specific antibody performed on motoneurons transduced with control lentivirus or with lentiviruses for expression of the indicated shRNAs. Gapdh was used as loading control.