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An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
Arginine is a semiessential amino acid required for the growth of melanoma and hepatocellular carcinoma, and the enzymatic removal of arginine by pegylated arginine deiminase (ADI) or arginase is being tested clinically. Here, we report a genetically engineered arginase FC fusion protein exhibiting...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662114/ https://www.ncbi.nlm.nih.gov/pubmed/23737831 http://dx.doi.org/10.1155/2013/423129 |
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author | Li, Lihua Wang, Yan Chen, Jun Cheng, Bi Hu, Jiehua Zhou, Yuehua Gao, Xin Gao, Liucun Mei, Xifan Sun, Meiyan Zhang, Zhuomei Song, Haifeng |
author_facet | Li, Lihua Wang, Yan Chen, Jun Cheng, Bi Hu, Jiehua Zhou, Yuehua Gao, Xin Gao, Liucun Mei, Xifan Sun, Meiyan Zhang, Zhuomei Song, Haifeng |
author_sort | Li, Lihua |
collection | PubMed |
description | Arginine is a semiessential amino acid required for the growth of melanoma and hepatocellular carcinoma, and the enzymatic removal of arginine by pegylated arginine deiminase (ADI) or arginase is being tested clinically. Here, we report a genetically engineered arginase FC fusion protein exhibiting a prolonged half-life and enhanced efficacy. The use of this enzyme to treat different tumor lines both inhibited cell proliferation and impaired cellular migration in vitro and in vivo. Our data reinforce the hypothesis that nutritional depletion is a key strategy for cancer treatment. |
format | Online Article Text |
id | pubmed-3662114 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-36621142013-06-04 An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo Li, Lihua Wang, Yan Chen, Jun Cheng, Bi Hu, Jiehua Zhou, Yuehua Gao, Xin Gao, Liucun Mei, Xifan Sun, Meiyan Zhang, Zhuomei Song, Haifeng Evid Based Complement Alternat Med Research Article Arginine is a semiessential amino acid required for the growth of melanoma and hepatocellular carcinoma, and the enzymatic removal of arginine by pegylated arginine deiminase (ADI) or arginase is being tested clinically. Here, we report a genetically engineered arginase FC fusion protein exhibiting a prolonged half-life and enhanced efficacy. The use of this enzyme to treat different tumor lines both inhibited cell proliferation and impaired cellular migration in vitro and in vivo. Our data reinforce the hypothesis that nutritional depletion is a key strategy for cancer treatment. Hindawi Publishing Corporation 2013 2013-05-08 /pmc/articles/PMC3662114/ /pubmed/23737831 http://dx.doi.org/10.1155/2013/423129 Text en Copyright © 2013 Lihua Li et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Li, Lihua Wang, Yan Chen, Jun Cheng, Bi Hu, Jiehua Zhou, Yuehua Gao, Xin Gao, Liucun Mei, Xifan Sun, Meiyan Zhang, Zhuomei Song, Haifeng An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo |
title | An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
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title_full | An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
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title_fullStr | An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
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title_full_unstemmed | An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
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title_short | An Engineered Arginase FC Protein Inhibits Tumor Growth In Vitro and In Vivo
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title_sort | engineered arginase fc protein inhibits tumor growth in vitro and in vivo |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3662114/ https://www.ncbi.nlm.nih.gov/pubmed/23737831 http://dx.doi.org/10.1155/2013/423129 |
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