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EpCAM associates with endoplasmic reticulum aminopeptidase 2 (ERAP2) in breast cancer cells
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Vise andre og tillknytning
2013 (engelsk)Inngår i: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 439, nr 2, s. 203-208Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2013. Vol. 439, nr 2, s. 203-208
Emneord [en]
ERAP2, EpCAM, Co-localization, Cleavage, Glycosylation
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Identifikatorer
URN: urn:nbn:se:su:diva-95770DOI: 10.1016/j.bbrc.2013.08.059ISI: 000325304900008OAI: oai:DiVA.org:su-95770DiVA, id: diva2:661757
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AuthorCount:7;

Tilgjengelig fra: 2013-11-04 Laget: 2013-11-04 Sist oppdatert: 2022-02-24bibliografisk kontrollert

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Öjemalm, KarinLara Vasquez, PatriciaNilsson, IngMarie

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