LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway

LIM domain only 3 (LMO3) interacts with transcription factors to regulate target genes involved in embryonic development. The oncogenic role of LMO3 in hepatocellular carcinoma, gastric cancer, and neuroblastoma has been reported recently. However, little is known about the biological function of LM...

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Main Authors: Ling Zeyi, Long Xiaoli, Wu Ying, Li Jie, Feng Mingliang
Format: Article
Language:English
Published: De Gruyter 2022-03-01
Series:Open Medicine
Subjects:
Online Access:https://doi.org/10.1515/med-2022-0419
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author Ling Zeyi
Long Xiaoli
Wu Ying
Li Jie
Feng Mingliang
author_facet Ling Zeyi
Long Xiaoli
Wu Ying
Li Jie
Feng Mingliang
author_sort Ling Zeyi
collection DOAJ
description LIM domain only 3 (LMO3) interacts with transcription factors to regulate target genes involved in embryonic development. The oncogenic role of LMO3 in hepatocellular carcinoma, gastric cancer, and neuroblastoma has been reported recently. However, little is known about the biological function of LMO3 in papillary thyroid carcinoma (PTC). First, expression of LMO3 was dramatically enhanced in the PTC tissues and cell lines. Second, knockdown of LMO3 in PTC cells repressed cell proliferation and promoted cell apoptosis with downregulated Bcl-2 and upregulated cleaved caspase-3/PARP. In vitro cell migration and invasion of PTC were also retarded by siRNA-mediated silence of LMO3. Third, protein expression of LIM kinase (LIMK) 1-mediated phosphorylation of cofilin and nuclear translocation of β-catenin were reduced by the knockdown of LMO3. pcDNA-mediated overexpression of LIMK1 promoted cofilin phosphorylation and attenuated LMO3 silence-induced decrease of cofilin phosphorylation. Last, enhanced LIMK1 expression promoted PTC cell proliferation and metastasis and counteracted the suppressive effects of LMO3 silence on PTC cell proliferation and metastasis. In conclusion, LMO3 promoted PTC cell proliferation and metastasis by regulating LIMK1-mediated cofilin and the β-catenin pathway.
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spelling doaj.art-a0a7b645066b4f8195c49b2f5dd67d542022-12-22T03:51:06ZengDe GruyterOpen Medicine2391-54632022-03-0117145346210.1515/med-2022-0419LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathwayLing Zeyi0Long Xiaoli1Wu Ying2Li Jie3Feng Mingliang4Department of Otorhinolaryngology Head and Neck Surgery, Yongchuan Hospital of Chongqing Medical University, Chongqing, 402160, ChinaDepartment of Geriatrics, Yongchuan Hospital of Chongqing Medical University, No. 439, Xuanhua Road, Yongchuan District, Chongqing, 402160, ChinaDepartment of Otorhinolaryngology Head and Neck Surgery, Yongchuan Hospital of Chongqing Medical University, Chongqing, 402160, ChinaDepartment of Otorhinolaryngology Head and Neck Surgery, Yongchuan Hospital of Chongqing Medical University, Chongqing, 402160, ChinaDepartment of Otorhinolaryngology Head and Neck Surgery, Yongchuan Hospital of Chongqing Medical University, Chongqing, 402160, ChinaLIM domain only 3 (LMO3) interacts with transcription factors to regulate target genes involved in embryonic development. The oncogenic role of LMO3 in hepatocellular carcinoma, gastric cancer, and neuroblastoma has been reported recently. However, little is known about the biological function of LMO3 in papillary thyroid carcinoma (PTC). First, expression of LMO3 was dramatically enhanced in the PTC tissues and cell lines. Second, knockdown of LMO3 in PTC cells repressed cell proliferation and promoted cell apoptosis with downregulated Bcl-2 and upregulated cleaved caspase-3/PARP. In vitro cell migration and invasion of PTC were also retarded by siRNA-mediated silence of LMO3. Third, protein expression of LIM kinase (LIMK) 1-mediated phosphorylation of cofilin and nuclear translocation of β-catenin were reduced by the knockdown of LMO3. pcDNA-mediated overexpression of LIMK1 promoted cofilin phosphorylation and attenuated LMO3 silence-induced decrease of cofilin phosphorylation. Last, enhanced LIMK1 expression promoted PTC cell proliferation and metastasis and counteracted the suppressive effects of LMO3 silence on PTC cell proliferation and metastasis. In conclusion, LMO3 promoted PTC cell proliferation and metastasis by regulating LIMK1-mediated cofilin and the β-catenin pathway.https://doi.org/10.1515/med-2022-0419lmo3papillary thyroid carcinomametastasisproliferationlimk1cofilinβ-catenin
spellingShingle Ling Zeyi
Long Xiaoli
Wu Ying
Li Jie
Feng Mingliang
LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
Open Medicine
lmo3
papillary thyroid carcinoma
metastasis
proliferation
limk1
cofilin
β-catenin
title LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
title_full LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
title_fullStr LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
title_full_unstemmed LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
title_short LMO3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating LIMK1-mediated cofilin and the β-catenin pathway
title_sort lmo3 promotes proliferation and metastasis of papillary thyroid carcinoma cells by regulating limk1 mediated cofilin and the β catenin pathway
topic lmo3
papillary thyroid carcinoma
metastasis
proliferation
limk1
cofilin
β-catenin
url https://doi.org/10.1515/med-2022-0419
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