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dc.contributor.authorVandsemb, Esten Nymoen
dc.contributor.authorBertilsson, Helena
dc.contributor.authorAbdollahi, Pegah
dc.contributor.authorStørkersen, Øystein
dc.contributor.authorVåtsveen, Thea Kristin
dc.contributor.authorRye, Morten Beck
dc.contributor.authorRø, Torstein Baade
dc.contributor.authorBørset, Magne
dc.contributor.authorSlørdahl, Tobias Schmidt
dc.date.accessioned2016-07-04T13:45:54Z
dc.date.accessioned2016-07-05T09:06:06Z
dc.date.available2016-07-04T13:45:54Z
dc.date.available2016-07-05T09:06:06Z
dc.date.issued2016
dc.identifier.citationJournal of Translational Medicine 2016, 14(1)nb_NO
dc.identifier.issn1479-5876
dc.identifier.urihttp://hdl.handle.net/11250/2395602
dc.description.abstractBackground: PRL-3 is a phosphatase implicated in oncogenesis in multiple cancers. In some cancers, notably carcinomas, PRL-3 is also associated with inferior prognosis and increased metastatic potential. In this study we investigated the expression of PRL-3mRNA in fresh-frozen samples from patients undergoing radical prostatectomy because of prostate cancer (PC) and the biological function of PRL-3 in prostate cancer cells. Methods: Samples from 41 radical prostatectomy specimens (168 samples in total) divided into low (Gleason score ≤ 6), intermediate (Gleason score = 7) and high (Gleason score ≥ 8) risk were analyzed with gene expression profiling and compared to normal prostate tissue. PRL-3was identified as a gene with differential expression between healthy and cancerous tissue in these analyses. We used the prostate cancer cell lines PC3 and DU145 and a small molecular inhibitor of PRL-3 to investigate whether PRL-3 had a functional role in cancer. Relative ATP-measurement and thymidine incorporation were used to assess the effect of PRL-3 on growth of the cancer cells. We performed an in vitro scratch assay to investigate the involvement of PRL-3 in migration. Immunohistochemistry was used to identify PRL-3 protein in prostate cancer primary tumor and corresponding lymph node metastases. Results: Compared to normal prostate tissue, the prostate cancer tissue expressed a significantly higher level of PRL-3. We found PRL-3 to be present in both PC3 and DU145, and that inhibition of PRL-3 led to growth arrest and apoptosis in these two cell lines. Inhibition of PRL-3 led to reduced migration of the PC3 cells. Immunohistochemistry showed PRL-3 expression in both primary tumor and corresponding lymph node metastases. Conclusions: PRL-3 mRNA was expressed to a greater extent in prostate cancer tissue compared to normal prostate tissue. PRL-3 protein was expressed in both prostate cancer primary tumor and corresponding lymph node metastases. The results from our in vitro assays suggest that PRL-3 promotes growth and migration in prostate cancer. In conclusion, these results imply that PRL-3 has a role in the pathogenesis of prostate cancer.nb_NO
dc.language.isoengnb_NO
dc.publisherBioMed Centralnb_NO
dc.rightsNavngivelse 3.0 Norge*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/no/*
dc.titlePhosphatase of regenerating liver 3 (PRL-3) is overexpressed in human prostate cancer tissue and promotes growth and migrationnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.date.updated2016-07-04T13:45:53Z
dc.source.volume14nb_NO
dc.source.journalJournal of Translational Medicinenb_NO
dc.source.issue1nb_NO
dc.identifier.doi10.1186/s12967-016-0830-z
dc.identifier.cristin1355702
dc.description.localcodeThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.nb_NO


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