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EpCAM associates with endoplasmic reticulum aminopeptidase 2 (ERAP2) in breast cancer cells
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2013 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 439, no 2, 203-208 p.Article in journal (Refereed) Published
Abstract [en]

Epithelial cell adhesion molecule (EpCAM) is an epithelial and cancer cell marker and there is a cumulative and growing evidence of its signaling role. Its importance has been recognized as part of the breast cancer stem cell phenotype, the tumorigenic breast cancer stem cell is EpCAM(+). In spite of its complex functions in normal cell development and cancer, relatively little is known about EpCAM-interacting proteins. We used breast cancer cell lines and performed EpCAM co-immunoprecipitation followed by mass spectrometry in search for novel potentially interacting proteins. The endoplasmic reticulum aminopeptidase 2 (ERAP2) was found to co-precipitate with EpCAM and to co-localize in the cytoplasm/ER and the plasma membrane. ERAP2 is a proteolytic enzyme set in the endoplasmic reticulum (ER) where it plays a central role in the trimming of peptides for presentation by MHC class I molecules. Expression of EpCAM and ERAP2 in vitro in the presence of dog pancreas rough microsomes (ER vesicles) confirmed N-linked glycosylation, processing in ER and the size of EpCAM. The association between ERAP2 and EpCAM is a unique and novel finding that provides new ideas on EpCAM processing and on how antigen presentation may be regulated in cancer.

Place, publisher, year, edition, pages
2013. Vol. 439, no 2, 203-208 p.
Keyword [en]
ERAP2, EpCAM, Co-localization, Cleavage, Glycosylation
National Category
Biochemistry and Molecular Biology Biophysics
Identifiers
URN: urn:nbn:se:su:diva-95770DOI: 10.1016/j.bbrc.2013.08.059ISI: 000325304900008OAI: oai:DiVA.org:su-95770DiVA: diva2:661757
Note

AuthorCount:7;

Available from: 2013-11-04 Created: 2013-11-04 Last updated: 2017-12-06Bibliographically approved

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Öjemalm, KarinVasquez, Patricia LaraNilsson, IngMarie
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