Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma
Abstract Hepatocellular carcinoma (HCC) is a serious threat to human health. The carbohydrate recognition domain of Galectin-3 (Gal3C) has been reported to be an anti-tumour molecule. In this study, we aim to explore effects of Gal3C in HCC and its possible molecular mechanism with quantitative prot...
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oai:doaj.org-article:534728dd2e804e51b68716bf3d2f71bd2021-12-02T12:30:13ZQuantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma10.1038/s41598-017-05419-52045-2322https://doaj.org/article/534728dd2e804e51b68716bf3d2f71bd2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05419-5https://doaj.org/toc/2045-2322Abstract Hepatocellular carcinoma (HCC) is a serious threat to human health. The carbohydrate recognition domain of Galectin-3 (Gal3C) has been reported to be an anti-tumour molecule. In this study, we aim to explore effects of Gal3C in HCC and its possible molecular mechanism with quantitative proteomics approach. We found that rGal3C stimulation could inhibit cell viability, migration and invasion of HepG2. After rGal3C stimulating, 190 proteins were differentially expressed. Eighty up-regulated proteins located mainly in extracellular exosome and involved in cell adhesion and metabolism, and 110 down-regulated proteins located in mitochondria and extracellular exosome, and related to processes of metabolism and oxidation-reduction. Of the differentially expressed proteins, CLU, NDRG1, CD166, S100A11 and Galectin-1 were carcinoma-related proteins affected by rGal3C. Potential receptors of rGal3C were explored by an UV cross-linking capture strategy. We showed that rGal3C could induce dephosphorylating of FAK/SRC. Blocking of the FAK/SRC pathway resulted in down-regulation of NDRG1. Immunofluorescence suggested that rGal3C could disrupt integrin clustering. Our study provides valuable insight into the anti-tumour mechanism of rGal3C in HCC on a proteomics level and is the first to reveal the possible mechanism involving integrin/FAK/SRC pathway and NDRG1. These results provide useful guidance of developing new therapies for HCC.Mingchao WangFang TianWantao YingXiaohong QianNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-17 (2017) |
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Medicine R Science Q Mingchao Wang Fang Tian Wantao Ying Xiaohong Qian Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
description |
Abstract Hepatocellular carcinoma (HCC) is a serious threat to human health. The carbohydrate recognition domain of Galectin-3 (Gal3C) has been reported to be an anti-tumour molecule. In this study, we aim to explore effects of Gal3C in HCC and its possible molecular mechanism with quantitative proteomics approach. We found that rGal3C stimulation could inhibit cell viability, migration and invasion of HepG2. After rGal3C stimulating, 190 proteins were differentially expressed. Eighty up-regulated proteins located mainly in extracellular exosome and involved in cell adhesion and metabolism, and 110 down-regulated proteins located in mitochondria and extracellular exosome, and related to processes of metabolism and oxidation-reduction. Of the differentially expressed proteins, CLU, NDRG1, CD166, S100A11 and Galectin-1 were carcinoma-related proteins affected by rGal3C. Potential receptors of rGal3C were explored by an UV cross-linking capture strategy. We showed that rGal3C could induce dephosphorylating of FAK/SRC. Blocking of the FAK/SRC pathway resulted in down-regulation of NDRG1. Immunofluorescence suggested that rGal3C could disrupt integrin clustering. Our study provides valuable insight into the anti-tumour mechanism of rGal3C in HCC on a proteomics level and is the first to reveal the possible mechanism involving integrin/FAK/SRC pathway and NDRG1. These results provide useful guidance of developing new therapies for HCC. |
format |
article |
author |
Mingchao Wang Fang Tian Wantao Ying Xiaohong Qian |
author_facet |
Mingchao Wang Fang Tian Wantao Ying Xiaohong Qian |
author_sort |
Mingchao Wang |
title |
Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
title_short |
Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
title_full |
Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
title_fullStr |
Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
title_full_unstemmed |
Quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of Galectin-3 in Hepatocellular carcinoma |
title_sort |
quantitative proteomics reveal the anti-tumour mechanism of the carbohydrate recognition domain of galectin-3 in hepatocellular carcinoma |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/534728dd2e804e51b68716bf3d2f71bd |
work_keys_str_mv |
AT mingchaowang quantitativeproteomicsrevealtheantitumourmechanismofthecarbohydraterecognitiondomainofgalectin3inhepatocellularcarcinoma AT fangtian quantitativeproteomicsrevealtheantitumourmechanismofthecarbohydraterecognitiondomainofgalectin3inhepatocellularcarcinoma AT wantaoying quantitativeproteomicsrevealtheantitumourmechanismofthecarbohydraterecognitiondomainofgalectin3inhepatocellularcarcinoma AT xiaohongqian quantitativeproteomicsrevealtheantitumourmechanismofthecarbohydraterecognitiondomainofgalectin3inhepatocellularcarcinoma |
_version_ |
1718394396840296448 |