caa a22 4500 606235418 CHVBK 20210128101242.0 cr unu---uuuuu 210128e20151001xx s 000 0 eng 10.1007/s11010-015-2502-3 doi (NATIONALLICENCE)springer-10.1007/s11010-015-2502-3 The metastasis-inducing protein AGR2 is O -glycosylated upon secretion from mammary epithelial cells [Elektronische Daten] [Christopher Clarke, Philip Rudland, Roger Barraclough] AGR2 is overexpressed in multiple cancers, particularly those arising from breast and prostate tissues, and higher levels of AGR2 are associated with earlier patient death. Although AGR2 is normally resident within the endoplasmic reticulum, the protein has been found in the extracellular space in several model systems. However, it has never been expressly demonstrated that this extracellular form of the protein is secreted and does not just accumulate in the extracellular space as a result of cell lysis. We show in this paper that AGR2 protein is secreted by both human and rat mammary epithelial cells in culture. Furthermore, this secreted form of AGR2 becomes O-glycosylated, with no detectable presence of N-glycosylation. Importantly, this post-translationally modified AGR2 is only detected in the conditioned medium from non-leaky cells, suggesting that membrane integrity must be maintained to allow AGR2 glycosylation. The results suggest a possible role for O-glycosylation in modulating the extracellular functions of AGR2. The Author(s), 2015 AGR2 nationallicence Glycosylation nationallicence Secretion nationallicence Adhesion nationallicence Clarke Christopher Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut Rudland Philip Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut Barraclough Roger Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut Molecular and Cellular Biochemistry Springer US; http://www.springer-ny.com 408/1-2(2015-10-01), 245-252 0300-8177 408:1-2<245 2015 408 11010 https://doi.org/10.1007/s11010-015-2502-3 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 brief-communication jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s11010-015-2502-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Clarke Christopher Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut NATIONALLICENCE 700 1- Rudland Philip Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut NATIONALLICENCE 700 1- Barraclough Roger Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, L69 7ZB, Liverpool, UK aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Springer US; http://www.springer-ny.com 408/1-2(2015-10-01), 245-252 0300-8177 408:1-2<245 2015 408 11010