Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl

TMEM88, a newly discovered protein localized on the cell membrane, inhibits canonical Wnt signaling. Immunohistochemic alanalysis of 139 breast cancers pecimens(64 triple-negative cancers and 75 non-triple-negative cancers) indicated that TMEM88 is expressed at significantly higher levels in breast...

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Main Authors:	Yu, Xinmiao, Zhang, Xiupeng, Zhang, Yong, Jiang, Guiyang, Mao, Xiaoyun, Jin, Feng
Format:	Online
Language:	English
Published:	Impact Journals LLC 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694813/

id	pubmed-4694813
recordtype	oai_dc
spelling	pubmed-46948132016-01-20 Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl Yu, Xinmiao Zhang, Xiupeng Zhang, Yong Jiang, Guiyang Mao, Xiaoyun Jin, Feng Research Paper TMEM88, a newly discovered protein localized on the cell membrane, inhibits canonical Wnt signaling. Immunohistochemic alanalysis of 139 breast cancers pecimens(64 triple-negative cancers and 75 non-triple-negative cancers) indicated that TMEM88 is expressed at significantly higher levels in breast cancer tissues (71.22%, 99/139) than in normal breast tissues (11.4%, 4/35; p < 0.001). The cytosolic and nuclear expression rates of TMEM88 were 57.81% and 9.37% in triple-negative and 52% and 33.33% (p = 0.5 and p = 0.001) in the non-triple-negative breast cancer tissues, respectively. Western blot analyses indicated that TMEM88 promoted Snail expression and inhibited Zo-1 and Occludin expression by interacting with dishevelled (Dvl) proteins, thereby stimulating invasion and metastasis in breast cancer. While cytosolic TMEM88 did not affect canonical Wnt signaling, cytosolic localization of this protein was positively correlated with both advanced TNM stage (p = 0.038 and p < 0.001) and lymph node metastasis (p = 0.01 and p = 0.002) in all and triple-negative specimens, respectively, and stimulated cell invasion by interacting with Dvls. Meanwhile, nuclear localization of TMEM88 was negatively correlated with lymph node metastasis (p = 0.046). Lastly, the increased prevalence of TMEM88 nuclear localization observed in non-triple-negative, compared to triple-negative tissues, suggests that the biological roles of TMEM88 differ depending on the subcellular localization. Impact Journals LLC 2015-06-29 /pmc/articles/PMC4694813/ /pubmed/26325443 Text en Copyright: © 2015 Yu et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Yu, Xinmiao Zhang, Xiupeng Zhang, Yong Jiang, Guiyang Mao, Xiaoyun Jin, Feng
spellingShingle	Yu, Xinmiao Zhang, Xiupeng Zhang, Yong Jiang, Guiyang Mao, Xiaoyun Jin, Feng Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
author_facet	Yu, Xinmiao Zhang, Xiupeng Zhang, Yong Jiang, Guiyang Mao, Xiaoyun Jin, Feng
author_sort	Yu, Xinmiao
title	Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
title_short	Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
title_full	Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
title_fullStr	Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
title_full_unstemmed	Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl
title_sort	cytosolic tmem88 promotes triple-negative breast cancer by interacting with dvl
description	TMEM88, a newly discovered protein localized on the cell membrane, inhibits canonical Wnt signaling. Immunohistochemic alanalysis of 139 breast cancers pecimens(64 triple-negative cancers and 75 non-triple-negative cancers) indicated that TMEM88 is expressed at significantly higher levels in breast cancer tissues (71.22%, 99/139) than in normal breast tissues (11.4%, 4/35; p < 0.001). The cytosolic and nuclear expression rates of TMEM88 were 57.81% and 9.37% in triple-negative and 52% and 33.33% (p = 0.5 and p = 0.001) in the non-triple-negative breast cancer tissues, respectively. Western blot analyses indicated that TMEM88 promoted Snail expression and inhibited Zo-1 and Occludin expression by interacting with dishevelled (Dvl) proteins, thereby stimulating invasion and metastasis in breast cancer. While cytosolic TMEM88 did not affect canonical Wnt signaling, cytosolic localization of this protein was positively correlated with both advanced TNM stage (p = 0.038 and p < 0.001) and lymph node metastasis (p = 0.01 and p = 0.002) in all and triple-negative specimens, respectively, and stimulated cell invasion by interacting with Dvls. Meanwhile, nuclear localization of TMEM88 was negatively correlated with lymph node metastasis (p = 0.046). Lastly, the increased prevalence of TMEM88 nuclear localization observed in non-triple-negative, compared to triple-negative tissues, suggests that the biological roles of TMEM88 differ depending on the subcellular localization.
publisher	Impact Journals LLC
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694813/
_version_	1613517764039802880

Cytosolic TMEM88 promotes triple-negative breast cancer by interacting with Dvl

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