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human luad cell lines (h1299, a549, pc-9  (Shanghai GenePharma)
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Shanghai GenePharma human luad cell lines (h1299, a549, pc-9
CLCN3 was upregulated in human <t>LUAD</t> and facilitated tumor proliferation and migration. (a, b) Through IHC and IF analysis, the expression of CLCN3 was examined in a tissue microarray of 30 paraffin-embedded LUAD tissues and adjacent normal tissues (ANT) ( n = 30). (c, d) In human LUAD cell lines as well as in human bronchial epithelial cell lines, the basic protein expression of CLCN3 was measured ( n = 3). (e) The basic RNA level of CLCN3 was detected in human LUAD cell lines and a human bronchial epithelial cell line ( n = 3). (f) The protein expression of CLCN3 was inhibited after CLCN3 knockdown in <t>H1299</t> and <t>A549</t> cells. (g) RNA-seq was constructed after CLCN3 knockdown in H1299 cells. Locomotion and growth were significantly enriched as illustrated by GO analysis. (h) Knockdown of CLCN3 suppressed the clonogenicity of H1299 and A549 cells ( n = 3). (i) CLCN3 knockdown suppressed the invasion of H1299 and A549 cells ( n = 3). * P < 0.05.
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CLCN3 was upregulated in human LUAD and facilitated tumor proliferation and migration. (a, b) Through IHC and IF analysis, the expression of CLCN3 was examined in a tissue microarray of 30 paraffin-embedded LUAD tissues and adjacent normal tissues (ANT) ( n = 30). (c, d) In human LUAD cell lines as well as in human bronchial epithelial cell lines, the basic protein expression of CLCN3 was measured ( n = 3). (e) The basic RNA level of CLCN3 was detected in human LUAD cell lines and a human bronchial epithelial cell line ( n = 3). (f) The protein expression of CLCN3 was inhibited after CLCN3 knockdown in H1299 and A549 cells. (g) RNA-seq was constructed after CLCN3 knockdown in H1299 cells. Locomotion and growth were significantly enriched as illustrated by GO analysis. (h) Knockdown of CLCN3 suppressed the clonogenicity of H1299 and A549 cells ( n = 3). (i) CLCN3 knockdown suppressed the invasion of H1299 and A549 cells ( n = 3). * P < 0.05.

Journal: International Journal of Biological Sciences

Article Title: HNRNPK/CLCN3 axis facilitates the progression of LUAD through CAF-tumor interaction

doi: 10.7150/ijbs.76083

Figure Lengend Snippet: CLCN3 was upregulated in human LUAD and facilitated tumor proliferation and migration. (a, b) Through IHC and IF analysis, the expression of CLCN3 was examined in a tissue microarray of 30 paraffin-embedded LUAD tissues and adjacent normal tissues (ANT) ( n = 30). (c, d) In human LUAD cell lines as well as in human bronchial epithelial cell lines, the basic protein expression of CLCN3 was measured ( n = 3). (e) The basic RNA level of CLCN3 was detected in human LUAD cell lines and a human bronchial epithelial cell line ( n = 3). (f) The protein expression of CLCN3 was inhibited after CLCN3 knockdown in H1299 and A549 cells. (g) RNA-seq was constructed after CLCN3 knockdown in H1299 cells. Locomotion and growth were significantly enriched as illustrated by GO analysis. (h) Knockdown of CLCN3 suppressed the clonogenicity of H1299 and A549 cells ( n = 3). (i) CLCN3 knockdown suppressed the invasion of H1299 and A549 cells ( n = 3). * P < 0.05.

Article Snippet: After acquiring the human LUAD cell lines (H1299, A549, and PC-9), authentication was done using STR profiling from Shanghai GenePharma Co. (Shanghai, China).

Techniques: Migration, Expressing, Microarray, RNA Sequencing Assay, Construct

HNRNPK was identified and validated as a CLCN3 promoter-binding transcription factor. (a) To identify putative transcription factors that bind to the CLCN3 promoter, nuclear protein extracts were subjected to incubation with a biotin-labeled DNA probe that included the promoter region. Following the SDS-PAGE separation and silver staining, a protein band with differential expression was identified after which it was excised and subjected to mass spectrometry (MS) analysis. (b) By employing either a synthesized probe or a nonspecific probe (NSP) in the nuclear protein/DNA complex, western blot analysis detected binding between HNRNPK and the CLCN3 promoter. (c) ChIP assays were performed and an HNRNPK antibody was used to immunoprecipitate the fragmented DNA in H1299 cells. The HNRNPK protein band was substantially enriched in the IP group in contrast to the IgG control. (d) The ChIP-seq data showed that the recruitment of HNRNPK was mostly enriched in the upstream and downstream TSS of the CLCN3 promoter region (NM_001829, chr4: 169620033-169620797, region -538/+226 bp). (e) The CLCN3 RNA level was inhibited following HNRNPK knockdown ( n = 3). (f) HNRNPK knockdown disrupted the promoter activities of the pGL4.10-CLCN3-538 reporter plasmid (region -538/+226 bp) in H1299 cells, and the binding motifs 'GCGAGG/CTAATG' from ChIP-seq data were enriched in this region ( n = 3). (g) GO analysis revealed that cell proliferation and migration were the biological functions of HNRNPK. (h) KEGG pathway analysis illustrated that cell growth and death, cell motility, transcription, translation, and other signaling pathways were mainly enriched after HNRNPK knockdown. (i) The luciferase activity was considerably reduced in HNRNPK knockdown cells transfected with a pGL4.10-CLCN3-538 plasmid (n = 3). * P < 0.05, ** P < 0.01.

Journal: International Journal of Biological Sciences

Article Title: HNRNPK/CLCN3 axis facilitates the progression of LUAD through CAF-tumor interaction

doi: 10.7150/ijbs.76083

Figure Lengend Snippet: HNRNPK was identified and validated as a CLCN3 promoter-binding transcription factor. (a) To identify putative transcription factors that bind to the CLCN3 promoter, nuclear protein extracts were subjected to incubation with a biotin-labeled DNA probe that included the promoter region. Following the SDS-PAGE separation and silver staining, a protein band with differential expression was identified after which it was excised and subjected to mass spectrometry (MS) analysis. (b) By employing either a synthesized probe or a nonspecific probe (NSP) in the nuclear protein/DNA complex, western blot analysis detected binding between HNRNPK and the CLCN3 promoter. (c) ChIP assays were performed and an HNRNPK antibody was used to immunoprecipitate the fragmented DNA in H1299 cells. The HNRNPK protein band was substantially enriched in the IP group in contrast to the IgG control. (d) The ChIP-seq data showed that the recruitment of HNRNPK was mostly enriched in the upstream and downstream TSS of the CLCN3 promoter region (NM_001829, chr4: 169620033-169620797, region -538/+226 bp). (e) The CLCN3 RNA level was inhibited following HNRNPK knockdown ( n = 3). (f) HNRNPK knockdown disrupted the promoter activities of the pGL4.10-CLCN3-538 reporter plasmid (region -538/+226 bp) in H1299 cells, and the binding motifs 'GCGAGG/CTAATG' from ChIP-seq data were enriched in this region ( n = 3). (g) GO analysis revealed that cell proliferation and migration were the biological functions of HNRNPK. (h) KEGG pathway analysis illustrated that cell growth and death, cell motility, transcription, translation, and other signaling pathways were mainly enriched after HNRNPK knockdown. (i) The luciferase activity was considerably reduced in HNRNPK knockdown cells transfected with a pGL4.10-CLCN3-538 plasmid (n = 3). * P < 0.05, ** P < 0.01.

Article Snippet: After acquiring the human LUAD cell lines (H1299, A549, and PC-9), authentication was done using STR profiling from Shanghai GenePharma Co. (Shanghai, China).

Techniques: Binding Assay, Incubation, Labeling, SDS Page, Silver Staining, Expressing, Mass Spectrometry, Synthesized, Western Blot, ChIP-sequencing, Plasmid Preparation, Migration, Luciferase, Activity Assay, Transfection

HNRNPK/CLCN3 axis facilitated LUAD progression through interaction between tumor cells and CAFs. (a) Primary human CAFs and paired NFs were extracted from fresh LUAD samples. The expression of CAF markers was increased in CAFs compared to NFs, which was in accord with the typical characteristic of CAFs. (b) The levels of CLCN3 were detected in the culture supernatants of LUAD cells, and the data indicated that decreased extracellular CLCN3 secretion could be induced by HNRNPK knockdown. (c-e) The supernatants (HNRNPK knockdown and control) of LUAD cells were incubated with CAFs for 24 h. We confirmed that the PI3K-AKT signaling pathway was significantly enriched in CAFs. (f) The levels of p-AKT, α-SMA, FAP, and COL1A1 were decreased when CAFs were stimulated with the supernatants of HNRNPK-knockdown cells. After CLCN3 knockdown in CAFs, the levels of p-AKT, α-SMA, FAP, and COL1A1 were also effectively inhibited. (g) Due to the activation inhibition, the CAFs co-cultured with HNRNPK-knockdown LUAD cells were then considered as inhibited CAFs. The analysis by ELISA revealed that the TGF-β1 production of inhibited CAFs was significantly decreased ( n = 7). (h) The supernatants of inhibited CAFs attenuated the expression of HNRNPK protein in the H1299 nucleus, and the attenuation effect was reversed after TGF-β1 treatment. (i) The supernatants of inhibited CAFs attenuated the fluorescence intensity of HNRNPK in the H1299 nucleus, which was also reversed after the addition of exogenous TGF-β1. (j, k) The supernatants of inhibited CAFs markedly attenuated the clonogenicity and invasion of LUAD cells, and this phenomenon was further reversed after the addition of TGF-β1 ( n = 3). *P < 0.05.

Journal: International Journal of Biological Sciences

Article Title: HNRNPK/CLCN3 axis facilitates the progression of LUAD through CAF-tumor interaction

doi: 10.7150/ijbs.76083

Figure Lengend Snippet: HNRNPK/CLCN3 axis facilitated LUAD progression through interaction between tumor cells and CAFs. (a) Primary human CAFs and paired NFs were extracted from fresh LUAD samples. The expression of CAF markers was increased in CAFs compared to NFs, which was in accord with the typical characteristic of CAFs. (b) The levels of CLCN3 were detected in the culture supernatants of LUAD cells, and the data indicated that decreased extracellular CLCN3 secretion could be induced by HNRNPK knockdown. (c-e) The supernatants (HNRNPK knockdown and control) of LUAD cells were incubated with CAFs for 24 h. We confirmed that the PI3K-AKT signaling pathway was significantly enriched in CAFs. (f) The levels of p-AKT, α-SMA, FAP, and COL1A1 were decreased when CAFs were stimulated with the supernatants of HNRNPK-knockdown cells. After CLCN3 knockdown in CAFs, the levels of p-AKT, α-SMA, FAP, and COL1A1 were also effectively inhibited. (g) Due to the activation inhibition, the CAFs co-cultured with HNRNPK-knockdown LUAD cells were then considered as inhibited CAFs. The analysis by ELISA revealed that the TGF-β1 production of inhibited CAFs was significantly decreased ( n = 7). (h) The supernatants of inhibited CAFs attenuated the expression of HNRNPK protein in the H1299 nucleus, and the attenuation effect was reversed after TGF-β1 treatment. (i) The supernatants of inhibited CAFs attenuated the fluorescence intensity of HNRNPK in the H1299 nucleus, which was also reversed after the addition of exogenous TGF-β1. (j, k) The supernatants of inhibited CAFs markedly attenuated the clonogenicity and invasion of LUAD cells, and this phenomenon was further reversed after the addition of TGF-β1 ( n = 3). *P < 0.05.

Article Snippet: After acquiring the human LUAD cell lines (H1299, A549, and PC-9), authentication was done using STR profiling from Shanghai GenePharma Co. (Shanghai, China).

Techniques: Expressing, Incubation, Activation Assay, Inhibition, Cell Culture, Enzyme-linked Immunosorbent Assay, Fluorescence

HNRNPK regulated the expression and function of CLCN3 in vivo . (a) In mouse xenograft models, stable HNRNPK-knockdown cells (H1299) and rescue model cells were administered to the nude mice via subcutaneous injection into their left flank. The representative figure of tumors formed in each group is shown ( n = 7). (b, c) The tumor weight and tumor growth curve were suppressed when HNRNPK was knocked down, and this inhibition was reversed by CLCN3 overexpression ( n = 7). (d) In tumor xenografts, the expression of CLCN3 was decreased following HNRNPK knockdown, however, this reduction was reversed by CLCN3 overexpression ( n = 7). (e) Nude mice received an injection with stable HNRNPK-knockdown cells (H1299) and rescue model cells into their tail veins. HNRNPK knockdown effectively decreased the average radiance of lung metastatic lesions, and the reduction was rescued by CLCN3 overexpression ( n = 7). (f) In paraffin sections of nude mouse lung metastases, we found that HNRNPK knockdown caused a reduction of lung metastasis area, which was rescued by CLCN3 overexpression ( n = 7). * P < 0.05.

Journal: International Journal of Biological Sciences

Article Title: HNRNPK/CLCN3 axis facilitates the progression of LUAD through CAF-tumor interaction

doi: 10.7150/ijbs.76083

Figure Lengend Snippet: HNRNPK regulated the expression and function of CLCN3 in vivo . (a) In mouse xenograft models, stable HNRNPK-knockdown cells (H1299) and rescue model cells were administered to the nude mice via subcutaneous injection into their left flank. The representative figure of tumors formed in each group is shown ( n = 7). (b, c) The tumor weight and tumor growth curve were suppressed when HNRNPK was knocked down, and this inhibition was reversed by CLCN3 overexpression ( n = 7). (d) In tumor xenografts, the expression of CLCN3 was decreased following HNRNPK knockdown, however, this reduction was reversed by CLCN3 overexpression ( n = 7). (e) Nude mice received an injection with stable HNRNPK-knockdown cells (H1299) and rescue model cells into their tail veins. HNRNPK knockdown effectively decreased the average radiance of lung metastatic lesions, and the reduction was rescued by CLCN3 overexpression ( n = 7). (f) In paraffin sections of nude mouse lung metastases, we found that HNRNPK knockdown caused a reduction of lung metastasis area, which was rescued by CLCN3 overexpression ( n = 7). * P < 0.05.

Article Snippet: After acquiring the human LUAD cell lines (H1299, A549, and PC-9), authentication was done using STR profiling from Shanghai GenePharma Co. (Shanghai, China).

Techniques: Expressing, In Vivo, Injection, Inhibition, Over Expression

A schematic representation of the relationship between CLCN3 and HNRNPK in LUAD progression. Firstly, CLCN3 was upregulated in human LUAD and facilitated tumor proliferation and migration. Secondly, HNRNPK was validated as a CLCN3 promoter-binding transcription factor, and the binding motif 'GCGAGG' and binding site '-538/-248 bp' were identified. Finally, the expression and function of CLCN3 were regulated by HNRNPK in vitro and in vivo , and the HNRNPK-CLCN3 axis facilitated LUAD progression in a feedback way through CAF-tumor interaction in the TME.

Journal: International Journal of Biological Sciences

Article Title: HNRNPK/CLCN3 axis facilitates the progression of LUAD through CAF-tumor interaction

doi: 10.7150/ijbs.76083

Figure Lengend Snippet: A schematic representation of the relationship between CLCN3 and HNRNPK in LUAD progression. Firstly, CLCN3 was upregulated in human LUAD and facilitated tumor proliferation and migration. Secondly, HNRNPK was validated as a CLCN3 promoter-binding transcription factor, and the binding motif 'GCGAGG' and binding site '-538/-248 bp' were identified. Finally, the expression and function of CLCN3 were regulated by HNRNPK in vitro and in vivo , and the HNRNPK-CLCN3 axis facilitated LUAD progression in a feedback way through CAF-tumor interaction in the TME.

Article Snippet: After acquiring the human LUAD cell lines (H1299, A549, and PC-9), authentication was done using STR profiling from Shanghai GenePharma Co. (Shanghai, China).

Techniques: Migration, Binding Assay, Expressing, In Vitro, In Vivo