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  Decreased E-Cadherin in MCF7 Human Breast Cancer Cells Forming Multicellular Spheroids Exposed to Simulated Microgravity

Sahana, J., Nassef, M. Z., Wehland, M., Kopp, S., Krueger, M., Corydon, T. J., et al. (2018). Decreased E-Cadherin in MCF7 Human Breast Cancer Cells Forming Multicellular Spheroids Exposed to Simulated Microgravity. Proteomics, 18(13): 1800015. doi:10.1002/pmic.201800015.

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 Creators:
Sahana, Jayashree1, Author
Nassef, Mohamed Zakaria1, Author
Wehland, Markus1, Author
Kopp, Sascha1, Author
Krueger, Marcus1, Author
Corydon, Thomas J.1, Author
Infanger, Manfred1, Author
Bauer, Johann2, Author              
Grimm, Daniela1, Author
Affiliations:
1external, ou_persistent22              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: ANAPHASE-PROMOTING COMPLEX; RANDOM POSITIONING MACHINE; HUMAN ENDOTHELIAL-CELLS; 3-DIMENSIONAL GROWTH; QUANTITATIVE PROTEOMICS; DOWN-REGULATION; THYROID-CELLS; IDENTIFICATION; ADHESION; SPACEBiochemistry & Molecular Biology; cell interaction; ISG15; proteome data; Reactome; signaling pathways; simulated microgravity;
 Abstract: MCF7 human breast cancer cells were cultured under normal gravity (1 g) and on a random positioning machine (RPM) preventing sedimentation. After 2 weeks, adherent 1 g-control and adherent RPM cells (AD) as well as multicellular spheroids (MCS) were harvested. AD and MCS had been exposed to the RPM in the same culture flask. In a subsequent proteome analysis, the majority of the proteins detected showed similar label-free quantification (LFQ) scores in each of the respective subpopulations, but in both AD or MCS cultures, proteins were also found whose LFQs deviated at least twofold from their counterparts in the 1 g-control cells. They included the cell junction protein E-cadherin, which was diminished in MCS cells, where proteins of the E-cadherin autodegradation pathway were enhanced and c-Src (proto-oncogene tyrosine-protein kinase c-Src) was detected. Spheroid formation was prevented by inhibition of c-Src but promoted by antibodies blocking E-cadherin activity. An interaction analysis of the detected proteins that are involved in forming and regulating junctions or adhesion complexes and in E-cadherin autodegradation indicated connections between the two protein groups. This suggests that the balance of proteins that up- or downregulate E-cadherin mediates the tendency of MCF7 cells to form MCS during RPM exposure.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000436943500007
DOI: 10.1002/pmic.201800015
 Degree: -

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Title: Proteomics
Source Genre: Journal
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Publ. Info: Weinheim : WILEY-VCH
Pages: - Volume / Issue: 18 (13) Sequence Number: 1800015 Start / End Page: - Identifier: ISSN: 1615-9853
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000294310