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. 2022 Sep 20;13(9):803. doi: 10.1038/s41419-022-05239-0

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — A mRNA fold changes of target genes of Hif-1 signaling pathway of E18.5 CKO growth plate cartilage compared to WT according to RNA-seq results. B mRNA expression level of key enzymes of oxidative phosphorylation and glycolysis of E18.5 WT and CKO growth plate cartilage (left panel). Protein level of Pfkfb3 and Ldha of E18.5 WT and CKO growth plate cartilage (right panel). Red boxes: most active glycolytic enzymes in chondrocytes. n = 3 biological replicates. Densitometry results were expressed as fold change in protein levels compared with WT1 after normalized to β-actin. C mRNA expression level of key enzymes of oxidative phosphorylation and glycolysis of Hnrnpk^fl/fl chondrocytes infected with Ad-GFP or Ad-Cre under normoxic or hypoxic conditions. Statistical analysis was exerted between Hypoxia Ad-GFP and Hypoxia Ad-Cre. n = 3 biological replicates. D Protein level of Vegfa, Ldha, and Pfkfb3 of Hnrnpk^fl/fl chondrocytes infected with Ad-GFP or Ad-Cre under normoxic or hypoxic conditions. Densitometry results were expressed as fold change in protein levels compared with chondrocytes infected with Ad-GFP under normoxic condition after normalized to β-actin. E Protein level of Hif1α, Ldha, and Pfkfb3 of Hnrnpk^fl/fl chondrocytes treated with DMSO or Chetomin after being infected with Ad-GFP or Ad-Cre under hypoxic condition. Densitometry results were expressed as fold change in protein levels compared with chondrocytes infected with Ad-GFP under hypoxic condition after normalized to β-actin. F Glucose consumption, lactate production, and ratio of lactate/glucose of Hnrnpk^fl/fl chondrocytes infected with Ad-GFP or Ad-Cre under normoxia or hypoxic conditions. n = 3 biological replicates. G Diagram indicated the strategy of treating Hnrnpk^fl/fl chondrocytes with PBS or 3-BrPA after being infected with Ad-GFP or Ad-Cre under hypoxic condition. H mRNA expression level and protein level of Sox9 and Mmp13 in Hnrnpk^fl/fl chondrocytes treated with PBS or 3-BrPA after being infected with Ad-GFP or Ad-Cre under hypoxic condition. n = 3 biological replicates. Densitometry results were expressed as fold change in protein levels compared with chondrocytes infected with Ad-GFP under hypoxic condition after normalized to β-actin. p-value was calculated by one-way ANOVA followed by Tukey’s multiple comparisons tests (C, F, H) or two-tailed unpaired Student’s t-test (B). Data were shown as mean ± SD. *p < 0.05; **p < 0.01; ***p < 0.001; ns: not significant.