LACTB promotes metastasis of nasopharyngeal carcinoma via activation of ERBB3/EGFR-ERK signaling resulting in unfavorable patient survival
Copyright © 2020 Elsevier B.V. All rights reserved..
Nasopharyngeal carcinoma (NPC) originates in the nasopharyngeal epithelium and has the highest metastatic rate among head and neck cancers. Distant metastasis is the main reason for treatment failure with the underlying mechanisms remaining unclear. By comparing the expression profiling of NPCs versus non-cancerous nasopharyngeal tissues, we found LACTB was highly expressed in the tumor tissues. We found that elevated expression of the LACTB protein in primary NPCs correlated with poorer patient survival. LACTB is known to be a serine protease and a ubiquitous mitochondrial protein localized in the intermembrane space. Its role in tumor biology remains controversial. We found that the different methylation pattern of LACTB promoter led to its differential expression in NPC cells. Overexpressing LACTB in NPC cells promoted their motility in vitro and metastasis in vivo. While knocking down LACTB reduced the metastasis capability of NPC cells. However, LACTB did not influence cellular proliferation. We further found the role of LACTB in promoting NPC metastasis depended on the activation of ERBB3/EGFR-ERK signaling, which in turn, affected the stability and the following acetylation of histone H3. These findings may shed light on unveiling the mechanisms of NPC metastasis.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:498 |
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| Enthalten in: |
Cancer letters - 498(2021) vom: 01. Feb., Seite 165-177 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Peng, Li-Xia [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 30.04.2021 Date Revised 30.04.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.canlet.2020.10.051 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM317205390 |
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| 100 | 1 | |a Peng, Li-Xia |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a LACTB promotes metastasis of nasopharyngeal carcinoma via activation of ERBB3/EGFR-ERK signaling resulting in unfavorable patient survival |
| 264 | 1 | |c 2021 | |
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| 500 | |a Date Completed 30.04.2021 | ||
| 500 | |a Date Revised 30.04.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2020 Elsevier B.V. All rights reserved. | ||
| 520 | |a Nasopharyngeal carcinoma (NPC) originates in the nasopharyngeal epithelium and has the highest metastatic rate among head and neck cancers. Distant metastasis is the main reason for treatment failure with the underlying mechanisms remaining unclear. By comparing the expression profiling of NPCs versus non-cancerous nasopharyngeal tissues, we found LACTB was highly expressed in the tumor tissues. We found that elevated expression of the LACTB protein in primary NPCs correlated with poorer patient survival. LACTB is known to be a serine protease and a ubiquitous mitochondrial protein localized in the intermembrane space. Its role in tumor biology remains controversial. We found that the different methylation pattern of LACTB promoter led to its differential expression in NPC cells. Overexpressing LACTB in NPC cells promoted their motility in vitro and metastasis in vivo. While knocking down LACTB reduced the metastasis capability of NPC cells. However, LACTB did not influence cellular proliferation. We further found the role of LACTB in promoting NPC metastasis depended on the activation of ERBB3/EGFR-ERK signaling, which in turn, affected the stability and the following acetylation of histone H3. These findings may shed light on unveiling the mechanisms of NPC metastasis | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Histone H3 acetylation | |
| 650 | 4 | |a LACTB | |
| 650 | 4 | |a Metastasis | |
| 650 | 4 | |a Nasopharyngeal carcinoma | |
| 650 | 7 | |a Membrane Proteins |2 NLM | |
| 650 | 7 | |a Mitochondrial Proteins |2 NLM | |
| 650 | 7 | |a EGFR protein, human |2 NLM | |
| 650 | 7 | |a EC 2.7.10.1 |2 NLM | |
| 650 | 7 | |a ERBB3 protein, human |2 NLM | |
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| 650 | 7 | |a Receptor, ErbB-3 |2 NLM | |
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| 650 | 7 | |a LACTB protein, human |2 NLM | |
| 650 | 7 | |a EC 3.4.- |2 NLM | |
| 650 | 7 | |a beta-Lactamases |2 NLM | |
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| 700 | 1 | |a Wang, Ming-Dian |e verfasserin |4 aut | |
| 700 | 1 | |a Xie, Ping |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Jun-Ping |e verfasserin |4 aut | |
| 700 | 1 | |a Sun, Rui |e verfasserin |4 aut | |
| 700 | 1 | |a Zheng, Li-Sheng |e verfasserin |4 aut | |
| 700 | 1 | |a Mei, Yan |e verfasserin |4 aut | |
| 700 | 1 | |a Meng, Dong-Fang |e verfasserin |4 aut | |
| 700 | 1 | |a Peng, Xing-Si |e verfasserin |4 aut | |
| 700 | 1 | |a Lang, Yan-Hong |e verfasserin |4 aut | |
| 700 | 1 | |a Qiang, Yuan-Yuan |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Chang-Zhi |e verfasserin |4 aut | |
| 700 | 1 | |a Xu, Liang |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Zhi-Jie |e verfasserin |4 aut | |
| 700 | 1 | |a Guo, Ling-Ling |e verfasserin |4 aut | |
| 700 | 1 | |a Xie, De-Huan |e verfasserin |4 aut | |
| 700 | 1 | |a Shu, Di-Tian |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Si-Ting |e verfasserin |4 aut | |
| 700 | 1 | |a Luo, Fei-Fei |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Bi-Jun |e verfasserin |4 aut | |
| 700 | 1 | |a Qian, Chao-Nan |e verfasserin |4 aut | |
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