EDI3 links choline metabolism to integrin expression, cell adhesion and spreading

EDI3 links choline metabolism to integrin expression, cell adhesion and spreading

Endometrial carcinoma differential 3 (EDI3) was the first member of the glycerophosphodiesterase (GDE) protein family shown to be associated with cancer. Our initial work demonstrated that endometrial and ovarian cancer patients with primary tumors overexpressing EDI3 had a higher risk of developing...

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Main Authors: Lesjak, Michaela S, Marchan, Rosemarie, Stewart, Joanna D, Rempel, Eugen, Rahnenführer, Jörg, Hengstler, Jan G
Format: Online
Language:English
Published: Taylor & Francis 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4594537/
id pubmed-4594537
recordtype oai_dc
spelling pubmed-45945372015-10-31 EDI3 links choline metabolism to integrin expression, cell adhesion and spreading Lesjak, Michaela S Marchan, Rosemarie Stewart, Joanna D Rempel, Eugen Rahnenführer, Jörg Hengstler, Jan G Research Paper Endometrial carcinoma differential 3 (EDI3) was the first member of the glycerophosphodiesterase (GDE) protein family shown to be associated with cancer. Our initial work demonstrated that endometrial and ovarian cancer patients with primary tumors overexpressing EDI3 had a higher risk of developing metastasis and decreased survival. Further analysis indicated that EDI3 cleaves glycerophosphocholine to choline and glycerol-3-phosphate, increases the levels of active PKC, and enhances the migratory activity of tumor cells. Despite these initial findings, EDI3 remained mainly uncharacterized. Therefore, to obtain an overview of processes in which EDI3 may be involved, gene array analysis was performed using MCF-7 breast cancer cells after EDI3 knockdown compared with a non-targeting control siRNA. Several biological motifs were altered, including an enrichment of genes involved in integrin-mediated signaling. More specifically, silencing of EDI3 in MCF-7 and OVCAR-3 cells was associated with reduced expression of the key receptor subunit integrin β1, leading to decreased cell attachment and spreading accompanied by delayed formation of cell protrusions. To confirm these results, we stably overexpressed EDI3 in MCF-7 cells which led to elevated integrin β1 expression associated with enhanced cell attachment and spreading - two processes critical for metastasis. In conclusion, our data provide further insight into the role of EDI3 during cancer progression. Taylor & Francis 2014-10-31 /pmc/articles/PMC4594537/ /pubmed/25482527 http://dx.doi.org/10.4161/cam.29284 Text en © 2014 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lesjak, Michaela S
Marchan, Rosemarie
Stewart, Joanna D
Rempel, Eugen
Rahnenführer, Jörg
Hengstler, Jan G
spellingShingle Lesjak, Michaela S
Marchan, Rosemarie
Stewart, Joanna D
Rempel, Eugen
Rahnenführer, Jörg
Hengstler, Jan G
EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
author_facet Lesjak, Michaela S
Marchan, Rosemarie
Stewart, Joanna D
Rempel, Eugen
Rahnenführer, Jörg
Hengstler, Jan G
author_sort Lesjak, Michaela S
title EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
title_short EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
title_full EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
title_fullStr EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
title_full_unstemmed EDI3 links choline metabolism to integrin expression, cell adhesion and spreading
title_sort edi3 links choline metabolism to integrin expression, cell adhesion and spreading
description Endometrial carcinoma differential 3 (EDI3) was the first member of the glycerophosphodiesterase (GDE) protein family shown to be associated with cancer. Our initial work demonstrated that endometrial and ovarian cancer patients with primary tumors overexpressing EDI3 had a higher risk of developing metastasis and decreased survival. Further analysis indicated that EDI3 cleaves glycerophosphocholine to choline and glycerol-3-phosphate, increases the levels of active PKC, and enhances the migratory activity of tumor cells. Despite these initial findings, EDI3 remained mainly uncharacterized. Therefore, to obtain an overview of processes in which EDI3 may be involved, gene array analysis was performed using MCF-7 breast cancer cells after EDI3 knockdown compared with a non-targeting control siRNA. Several biological motifs were altered, including an enrichment of genes involved in integrin-mediated signaling. More specifically, silencing of EDI3 in MCF-7 and OVCAR-3 cells was associated with reduced expression of the key receptor subunit integrin β1, leading to decreased cell attachment and spreading accompanied by delayed formation of cell protrusions. To confirm these results, we stably overexpressed EDI3 in MCF-7 cells which led to elevated integrin β1 expression associated with enhanced cell attachment and spreading - two processes critical for metastasis. In conclusion, our data provide further insight into the role of EDI3 during cancer progression.
publisher Taylor & Francis
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4594537/
_version_ 1613483868933849088

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