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...
Main Authors: | , , , , , , , , , , |
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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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Series: | PLoS ONE |
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23894455/?tool=EBI |
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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 |
collection | DOAJ |
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. |
first_indexed | 2024-12-14T08:43:02Z |
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id | doaj.art-a9063f637cb3400187053e54a3d1f4b4 |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-14T08:43:02Z |
publishDate | 2013-01-01 |
publisher | Public Library of Science (PLoS) |
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series | PLoS ONE |
spelling | doaj.art-a9063f637cb3400187053e54a3d1f4b42022-12-21T23:09:16ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0187e6935410.1371/journal.pone.0069354Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target.Kuan-Chung HsiaoNeng-Yao ShihHsun-Lang FangTze-Sing HuangChing-Chuan KuoPei-Yi ChuYi-Mei HungShao-Wen ChouYi-Yuan YangGee-Chen ChangKo-Jiunn LiuIn 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23894455/?tool=EBI |
spellingShingle | 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. PLoS ONE |
title | 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_short | 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 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23894455/?tool=EBI |
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