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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2013
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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) |
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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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