Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.

In previous research, we found α-enolase to be inversely correlated with progression-free and overall survival in lung cancer patients and detected α-enolase on the surface of lung cancer cells. Based on these findings, we hypothesized that surface α-enolase has a significant role in cancer metastas...

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Autores principales: Kuan-Chung Hsiao, Neng-Yao Shih, Hsun-Lang Fang, Tze-Sing Huang, Ching-Chuan Kuo, Pei-Yi Chu, Yi-Mei Hung, Shao-Wen Chou, Yi-Yuan Yang, Gee-Chen Chang, Ko-Jiunn Liu
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Publicado: Public Library of Science (PLoS) 2013
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spelling oai:doaj.org-article:a9063f637cb3400187053e54a3d1f4b42021-11-18T09:03:47ZSurface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.1932-620310.1371/journal.pone.0069354https://doaj.org/article/a9063f637cb3400187053e54a3d1f4b42013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23894455/?tool=EBIhttps://doaj.org/toc/1932-6203In previous research, we found α-enolase to be inversely correlated with progression-free and overall survival in lung cancer patients and detected α-enolase on the surface of lung cancer cells. Based on these findings, we hypothesized that surface α-enolase has a significant role in cancer metastasis and tested this hypothesis in the current study. We found that α-enolase was co-immunoprecipitated with urokinase-type plasminogen activator, urokinase-type plasminogen activator receptor, and plasminogen in lung cancer cells and interacted with these proteins in a cell-free dot blotting assay, which can be interrupted by α-enolase-specific antibody. α-Enolase in lung cancer cells co-localized with these proteins and was present at the site of pericellular degradation of extracellular matrix components. Treatment with antibody against α-enolase in vitro suppressed cell-associated plasminogen and matrix metalloproteinase activation, collagen and gelatin degradation, and cell invasion. Examination of the effect of treatment with shRNA plasmids revealed that down regulation of α-enolase decreases extracellular matrix degradation by and the invasion capacity of lung cancer cells. Adoptive transfer of α-enolase-specific antibody to mice resulted in accumulation of antibody in subcutaneous tumor and inhibited the formation of tumor metastasis in lung and bone. This study demonstrated that surface α-enolase promotes extracellular matrix degradation and invasion of cancer cells and that targeting surface α-enolase is a promising approach to suppress tumor metastasis.Kuan-Chung HsiaoNeng-Yao ShihHsun-Lang FangTze-Sing HuangChing-Chuan KuoPei-Yi ChuYi-Mei HungShao-Wen ChouYi-Yuan YangGee-Chen ChangKo-Jiunn LiuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 7, p e69354 (2013)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Kuan-Chung Hsiao
Neng-Yao Shih
Hsun-Lang Fang
Tze-Sing Huang
Ching-Chuan Kuo
Pei-Yi Chu
Yi-Mei Hung
Shao-Wen Chou
Yi-Yuan Yang
Gee-Chen Chang
Ko-Jiunn Liu
Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
description In previous research, we found α-enolase to be inversely correlated with progression-free and overall survival in lung cancer patients and detected α-enolase on the surface of lung cancer cells. Based on these findings, we hypothesized that surface α-enolase has a significant role in cancer metastasis and tested this hypothesis in the current study. We found that α-enolase was co-immunoprecipitated with urokinase-type plasminogen activator, urokinase-type plasminogen activator receptor, and plasminogen in lung cancer cells and interacted with these proteins in a cell-free dot blotting assay, which can be interrupted by α-enolase-specific antibody. α-Enolase in lung cancer cells co-localized with these proteins and was present at the site of pericellular degradation of extracellular matrix components. Treatment with antibody against α-enolase in vitro suppressed cell-associated plasminogen and matrix metalloproteinase activation, collagen and gelatin degradation, and cell invasion. Examination of the effect of treatment with shRNA plasmids revealed that down regulation of α-enolase decreases extracellular matrix degradation by and the invasion capacity of lung cancer cells. Adoptive transfer of α-enolase-specific antibody to mice resulted in accumulation of antibody in subcutaneous tumor and inhibited the formation of tumor metastasis in lung and bone. This study demonstrated that surface α-enolase promotes extracellular matrix degradation and invasion of cancer cells and that targeting surface α-enolase is a promising approach to suppress tumor metastasis.
format article
author Kuan-Chung Hsiao
Neng-Yao Shih
Hsun-Lang Fang
Tze-Sing Huang
Ching-Chuan Kuo
Pei-Yi Chu
Yi-Mei Hung
Shao-Wen Chou
Yi-Yuan Yang
Gee-Chen Chang
Ko-Jiunn Liu
author_facet Kuan-Chung Hsiao
Neng-Yao Shih
Hsun-Lang Fang
Tze-Sing Huang
Ching-Chuan Kuo
Pei-Yi Chu
Yi-Mei Hung
Shao-Wen Chou
Yi-Yuan Yang
Gee-Chen Chang
Ko-Jiunn Liu
author_sort Kuan-Chung Hsiao
title Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
title_short Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
title_full Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
title_fullStr Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
title_full_unstemmed Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
title_sort surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.
publisher Public Library of Science (PLoS)
publishDate 2013
url https://doaj.org/article/a9063f637cb3400187053e54a3d1f4b4
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