Knock-down of the 37kDa/67kDa laminin receptor LRP/LR impedes telomerase activity.

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dc.contributor.author Naidoo, K.
dc.contributor.author Malindisa, S.T.
dc.contributor.author Otgaar, T.C.
dc.contributor.author Da Costa Dias, B.
dc.contributor.author Ferreirra, E.
dc.contributor.author Reusch, U.
dc.contributor.author Knackmuss, S.
dc.contributor.author Little, M.
dc.contributor.author Weiss, S.F.T.
dc.contributor.author Letsolo, B.T.
dc.date.accessioned 2016-09-16T10:02:02Z
dc.date.available 2016-09-16T10:02:02Z
dc.date.issued 2015-11-06
dc.identifier.citation Naidoo, K. et al. 2015. Knock-down of the 37kDa/67kDa laminin receptor LRP/LR impedes telomerase activity. PLoS ONE 10(11): e0141618. en_ZA
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10539/21037
dc.description.abstract Cancer has become a major problem worldwide due to its increasing incidence and mortality rates. Both the 37kDa/67kDa laminin receptor (LRP/LR) and telomerase are overexpressed in cancer cells. LRP/LR enhances the invasiveness of cancer cells thereby promoting metastasis, supporting angiogenesis and hampering apoptosis. An essential component of telomerase, hTERT is overexpressed in 85-90% of most cancers. hTERT expression and increased telomerase activity are associated with tumor progression. As LRP/LR and hTERT both play a role in cancer progression, we investigated a possible correlation between LRP/LR and telomerase. LRP/LR and hTERT co-localized in the perinuclear compartment of tumorigenic breast cancer (MDA-MB231) cells and non-tumorigenic human embryonic kidney (HEK293) cells. FLAG® Co-immunoprecipitation assays confirmed an interaction between LRP/LR and hTERT. In addition, flow cytometry revealed that both cell lines displayed high cell surface and intracellular LRP/LR and hTERT levels. Knock-down of LRP/LR by RNAi technology significantly reduced telomerase activity. These results suggest for the first time a novel function of LRP/LR in contributing to telomerase activity. siRNAs targeting LRP/LR may act as a potential alternative therapeutic tool for cancer treatment by (i) blocking metastasis (ii) promoting angiogenesis (iii) inducing apoptosis and (iv) impeding telomerase activity. en_ZA
dc.description.sponsorship This work was supported by the National Research Foundation, the Republic of South Africa. en_ZA
dc.language.iso en en_ZA
dc.publisher Public Library of Science. en_ZA
dc.rights © 2015 Naidoo et al. 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. en_ZA
dc.subject laminin receptor; en_ZA
dc.subject small interfering RNA; en_ZA
dc.subject telomerase; en_ZA
dc.subject breast cancer; en_ZA
dc.subject cancer cell line; en_ZA
dc.subject cell level; en_ZA
dc.subject cell nucleus; en_ZA
dc.subject cell surface; en_ZA
dc.subject controlled study; en_ZA
dc.subject embryo; en_ZA
dc.subject enzyme activity; en_ZA
dc.subject gene silencing; en_ZA
dc.subject HEK293 cell line; en_ZA
dc.subject human; human cell; en_ZA
dc.subject MB231 cell line; en_ZA
dc.subject protein function; en_ZA
dc.subject protein localization; en_ZA
dc.subject protein protein interaction; en_ZA
dc.subject RNA interference; en_ZA
dc.title Knock-down of the 37kDa/67kDa laminin receptor LRP/LR impedes telomerase activity. en_ZA
dc.type Article en_ZA
dc.journal.volume 10 en_ZA
dc.journal.title PLOS ONE en_ZA
dc.description.librarian NCS2016 en_ZA
dc.citation.doi 10.1371/journal.pone.0141618. en_ZA
dc.citation.issue 11 en_ZA


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