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Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer

Abnormal expression of annexin A2 contributes to metastasis and infiltration of cancer cells. To elucidate the cause of abnormal expression of annexin A2, Western blotting, immunoproteomics and immunohistochemical staining were performed to analyze differentially ubiquitinated proteins between fresh...

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Detalles Bibliográficos
Autores principales: Deng, Shishan, Jing, Baoqian, Xing, Tianyong, Hou, Lingmi, Yang, Zhengwei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5054490/
https://www.ncbi.nlm.nih.gov/pubmed/22917188
http://dx.doi.org/10.1016/j.gpb.2011.12.001
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author Deng, Shishan
Jing, Baoqian
Xing, Tianyong
Hou, Lingmi
Yang, Zhengwei
author_facet Deng, Shishan
Jing, Baoqian
Xing, Tianyong
Hou, Lingmi
Yang, Zhengwei
author_sort Deng, Shishan
collection PubMed
description Abnormal expression of annexin A2 contributes to metastasis and infiltration of cancer cells. To elucidate the cause of abnormal expression of annexin A2, Western blotting, immunoproteomics and immunohistochemical staining were performed to analyze differentially ubiquitinated proteins between fresh breast cancer tissue and its adjacent normal breast tissue from five female volunteers. We detected an ubiquitinated protein that was up-regulated in the cancer tissue, which was further identified as annexin A2 by mass spectrometry. These results suggest that abnormal ubiquitination and/or degradation of annexin A2 may lead to presence of annexin A2 at high level, which may further promote metastasis and infiltration of the breast cancer cells.
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spelling pubmed-50544902016-10-14 Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer Deng, Shishan Jing, Baoqian Xing, Tianyong Hou, Lingmi Yang, Zhengwei Genomics Proteomics Bioinformatics Original Research Abnormal expression of annexin A2 contributes to metastasis and infiltration of cancer cells. To elucidate the cause of abnormal expression of annexin A2, Western blotting, immunoproteomics and immunohistochemical staining were performed to analyze differentially ubiquitinated proteins between fresh breast cancer tissue and its adjacent normal breast tissue from five female volunteers. We detected an ubiquitinated protein that was up-regulated in the cancer tissue, which was further identified as annexin A2 by mass spectrometry. These results suggest that abnormal ubiquitination and/or degradation of annexin A2 may lead to presence of annexin A2 at high level, which may further promote metastasis and infiltration of the breast cancer cells. Elsevier 2012-06 2012-06-26 /pmc/articles/PMC5054490/ /pubmed/22917188 http://dx.doi.org/10.1016/j.gpb.2011.12.001 Text en © 2012 Beijing Institute of Genomics, Chinese Academy of Sciences and Genetics Society of China. Published by Elsevier Ltd and Science Press. All rights reserved. http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open access article under the CC BY-NC-SA license (http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Original Research
Deng, Shishan
Jing, Baoqian
Xing, Tianyong
Hou, Lingmi
Yang, Zhengwei
Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title_full Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title_fullStr Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title_full_unstemmed Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title_short Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer
title_sort overexpression of annexin a2 is associated with abnormal ubiquitination in breast cancer
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5054490/
https://www.ncbi.nlm.nih.gov/pubmed/22917188
http://dx.doi.org/10.1016/j.gpb.2011.12.001
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