dc.contributor.author | Olsen, Oddrun Elise | |
dc.contributor.author | Wader, Karin Fahl | |
dc.contributor.author | Hella, Hanne | |
dc.contributor.author | Mylin, Anne K. | |
dc.contributor.author | Turesson, Ingemar | |
dc.contributor.author | Nesthus, Ingerid | |
dc.contributor.author | Waage, Anders | |
dc.contributor.author | Sundan, Anders | |
dc.contributor.author | Holien, Toril | |
dc.date.accessioned | 2015-06-15T11:51:17Z | |
dc.date.accessioned | 2015-09-01T09:06:21Z | |
dc.date.available | 2015-06-15T11:51:17Z | |
dc.date.available | 2015-09-01T09:06:21Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Cell Communication and Signaling 2015, 13(1):27 | nb_NO |
dc.identifier.issn | 1478-811X | |
dc.identifier.uri | http://hdl.handle.net/11250/298334 | |
dc.description | - | nb_NO |
dc.description.abstract | Background: Activins are members of the TGF-β family of ligands that have multiple biological functions in
embryonic stem cells as well as in differentiated tissue. Serum levels of activin A were found to be elevated in
pathological conditions such as cachexia, osteoporosis and cancer. Signaling by activin A through canonical
ALK4-ACVR2 receptor complexes activates the transcription factors SMAD2 and SMAD3. Activin A has a strong
affinity to type 2 receptors, a feature that they share with some of the bone morphogenetic proteins (BMPs). Activin
A is also elevated in myeloma patients with advanced disease and is involved in myeloma bone disease.
Results: In this study we investigated effects of activin A binding to receptors that are shared with BMPs using
myeloma cell lines with well-characterized BMP-receptor expression and responses. Activin A antagonized BMP-6
and BMP-9, but not BMP-2 and BMP-4. Activin A was able to counteract BMPs that signal through the type 2
receptors ACVR2A and ACVR2B in combination with ALK2, but not BMPs that signal through BMPR2 in combination
with ALK3 and ALK6.
Conclusions: We propose that one important way that activin A regulates cell behavior is by antagonizing
BMP-ACVR2A/ACVR2B/ALK2 signaling. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | BioMed Central | nb_NO |
dc.title | Activin A inhibits BMP-signaling by binding ACVR2A and ACVR2B | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | en_GB |
dc.date.updated | 2015-06-15T11:51:17Z | |
dc.source.volume | 13 | nb_NO |
dc.source.journal | Cell Communication and Signaling | nb_NO |
dc.source.issue | 1 | nb_NO |
dc.identifier.doi | 10.1186/s12964-015-0104-z | |
dc.identifier.cristin | 1248282 | |
dc.description.localcode | © 2015 Olsen et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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 |