SENP1 knockdown-mediated CTCF SUMOylation enhanced its stability and alleviated lipopolysaccharide-evoked inflammatory injury in human lung fibroblasts via regulation of FOXA2 transcription
Copyright © 2023 Elsevier B.V. All rights reserved..
BACKGROUND: Excessive inflammation is the main cause of treatment failure in neonatal pneumonia (NP). CCCTC-binding factor (CTCF) represents an important node in various inflammatory diseases. In the present study, we tried to clarify the function and underlying molecular mechanism of CTCF on an in vitro cellular model of NP, which was generated by simulating the human lung fibroblast cell line WI-38 with lipopolysaccharide (LPS).
METHODS: The SUMOylation level and protein interaction were verified by Co-immunoprecipitation assay. Cell viability was measured by Cell Counting Kit-8 assay. Inflammatory factors were examined by Enzyme-linked immunosorbent assay. Cell apoptosis was evaluated by TUNEL assay. The binding activity of CTCF to target promoter was tested by chromatin immunoprecipitation and luciferase reporter assay.
RESULTS: LPS treatment restrained cell viability, promoted the production of inflammatory factors, and enhanced cell apoptosis. CTCF overexpression played anti-inflammatory and anti-apoptotic roles. Furthermore, CTCF was modified by SUMOylation with small ubiquitin-like modifier protein 1 (SUMO1). Interfering with sumo-specific protease 1 (SENP1) facilitated CTCF SUMOylation and protein stability, thus suppressing LPS-evoked inflammatory and apoptotic injuries. Moreover, CTCF could bind to the forkhead box protein A2 (FOXA2) promoter region to promote FOXA2 expression. The anti-inflammatory and anti-apoptotic roles of CTCF are associated with FOXA2 activation. In addition, SENP1 knockdown increased FOXA2 expression by enhancing the abundance and binding ability of CTCF.
CONCLUSIONS: SUMOylation of CTCF by SENP1 knockdown enhanced its protein stability and binding ability and it further alleviated LPS-evoked inflammatory injury in human lung fibroblasts by positively regulating FOXA2 transcription.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2024 |
|---|---|
| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:1868 |
|---|---|
| Enthalten in: |
Biochimica et biophysica acta. General subjects - 1868(2024), 1 vom: 31. Jan., Seite 130500 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Kang, Le [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 16.12.2023 Date Revised 29.12.2023 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1016/j.bbagen.2023.130500 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM364060387 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM364060387 | ||
| 003 | DE-627 | ||
| 005 | 20240108135937.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231226s2024 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.bbagen.2023.130500 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n1242.xml |
| 035 | |a (DE-627)NLM364060387 | ||
| 035 | |a (NLM)37914145 | ||
| 035 | |a (PII)S0304-4165(23)00198-8 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Kang, Le |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a SENP1 knockdown-mediated CTCF SUMOylation enhanced its stability and alleviated lipopolysaccharide-evoked inflammatory injury in human lung fibroblasts via regulation of FOXA2 transcription |
| 264 | 1 | |c 2024 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 16.12.2023 | ||
| 500 | |a Date Revised 29.12.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2023 Elsevier B.V. All rights reserved. | ||
| 520 | |a BACKGROUND: Excessive inflammation is the main cause of treatment failure in neonatal pneumonia (NP). CCCTC-binding factor (CTCF) represents an important node in various inflammatory diseases. In the present study, we tried to clarify the function and underlying molecular mechanism of CTCF on an in vitro cellular model of NP, which was generated by simulating the human lung fibroblast cell line WI-38 with lipopolysaccharide (LPS) | ||
| 520 | |a METHODS: The SUMOylation level and protein interaction were verified by Co-immunoprecipitation assay. Cell viability was measured by Cell Counting Kit-8 assay. Inflammatory factors were examined by Enzyme-linked immunosorbent assay. Cell apoptosis was evaluated by TUNEL assay. The binding activity of CTCF to target promoter was tested by chromatin immunoprecipitation and luciferase reporter assay | ||
| 520 | |a RESULTS: LPS treatment restrained cell viability, promoted the production of inflammatory factors, and enhanced cell apoptosis. CTCF overexpression played anti-inflammatory and anti-apoptotic roles. Furthermore, CTCF was modified by SUMOylation with small ubiquitin-like modifier protein 1 (SUMO1). Interfering with sumo-specific protease 1 (SENP1) facilitated CTCF SUMOylation and protein stability, thus suppressing LPS-evoked inflammatory and apoptotic injuries. Moreover, CTCF could bind to the forkhead box protein A2 (FOXA2) promoter region to promote FOXA2 expression. The anti-inflammatory and anti-apoptotic roles of CTCF are associated with FOXA2 activation. In addition, SENP1 knockdown increased FOXA2 expression by enhancing the abundance and binding ability of CTCF | ||
| 520 | |a CONCLUSIONS: SUMOylation of CTCF by SENP1 knockdown enhanced its protein stability and binding ability and it further alleviated LPS-evoked inflammatory injury in human lung fibroblasts by positively regulating FOXA2 transcription | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a CTCF | |
| 650 | 4 | |a FOXA2 | |
| 650 | 4 | |a Inflammatory injury | |
| 650 | 4 | |a Neonatal pneumonia | |
| 650 | 4 | |a SENP1 | |
| 650 | 4 | |a SUMOylation | |
| 650 | 7 | |a Lipopolysaccharides |2 NLM | |
| 650 | 7 | |a Peptide Hydrolases |2 NLM | |
| 650 | 7 | |a EC 3.4.- |2 NLM | |
| 650 | 7 | |a CCCTC-Binding Factor |2 NLM | |
| 650 | 7 | |a Cysteine Endopeptidases |2 NLM | |
| 650 | 7 | |a EC 3.4.22.- |2 NLM | |
| 650 | 7 | |a Anti-Inflammatory Agents |2 NLM | |
| 650 | 7 | |a SENP1 protein, human |2 NLM | |
| 650 | 7 | |a EC 3.4.- |2 NLM | |
| 650 | 7 | |a FOXA2 protein, human |2 NLM | |
| 650 | 7 | |a Hepatocyte Nuclear Factor 3-beta |2 NLM | |
| 650 | 7 | |a 135845-92-0 |2 NLM | |
| 700 | 1 | |a Wang, Xinhua |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Jianfang |e verfasserin |4 aut | |
| 700 | 1 | |a Guo, Jing |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Wang |e verfasserin |4 aut | |
| 700 | 1 | |a Lei, Ruirui |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochimica et biophysica acta. General subjects |d 2017 |g 1868(2024), 1 vom: 31. Jan., Seite 130500 |w (DE-627)NLM258373482 |x 1872-8006 |7 nnns |
| 773 | 1 | 8 | |g volume:1868 |g year:2024 |g number:1 |g day:31 |g month:01 |g pages:130500 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1016/j.bbagen.2023.130500 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 1868 |j 2024 |e 1 |b 31 |c 01 |h 130500 | ||