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Tytuł:
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Initial assessment of suitability of MCF-7 and HepG2 cancer cell lines for AQP3 research in cancer biology.
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Autorzy:
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Oberska P; Department of Physiology, Cytobiology and Proteomics, West Pomeranian University of Technology, Klemensa Janickiego 29, 71-270, Szczecin, Poland.
Jedrzejczak-Silicka M; Laboratory of Cytogenetics, West Pomeranian University of Technology, Klemensa Janickiego 29, 71-270, Szczecin, Poland. Electronic address: .
Michałek K; Department of Physiology, Cytobiology and Proteomics, West Pomeranian University of Technology, Klemensa Janickiego 29, 71-270, Szczecin, Poland.
Grabowska M; Department of Histology and Developmental Biology, Pomeranian Medical University, Żołnierska 48, 71-210, Szczecin, Poland.
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Źródło:
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Acta histochemica [Acta Histochem] 2021 May; Vol. 123 (4), pp. 151716. Date of Electronic Publication: 2021 Apr 29.
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Typ publikacji:
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Journal Article
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Język:
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English
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Imprint Name(s):
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Original Publication: Jena Gustav Fischer Verlag
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MeSH Terms:
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Adenocarcinoma/*metabolism
Aquaporin 3/*metabolism
Breast Neoplasms/*metabolism
Carcinoma, Hepatocellular/*metabolism
Liver Neoplasms/*metabolism
Neoplasm Proteins/*metabolism
Adenocarcinoma/pathology ; Breast Neoplasms/pathology ; Carcinoma, Hepatocellular/pathology ; Female ; Hep G2 Cells ; Humans ; Liver Neoplasms/pathology ; MCF-7 Cells ; Male
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Contributed Indexing:
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Keywords: Aquaporin-3; Breast cancer; Cancer cell line; Cell culture; Liver cancer
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Substance Nomenclature:
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0 (AQP3 protein, human)
0 (Neoplasm Proteins)
158801-98-0 (Aquaporin 3)
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Entry Date(s):
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Date Created: 20210502 Date Completed: 20211129 Latest Revision: 20211129
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Update Code:
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20240105
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DOI:
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10.1016/j.acthis.2021.151716
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PMID:
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33933702
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Cancer cell lines are widely used as in vitro models to elucidate biological processes in cancer, and as a tool to evaluate anticancer agents. In fact, the use of an appropriate cancer cell line in cancer research is crucial for investigating new, potential factors involved in carcinogenesis. One of them is aquaporin-3 (AQP3), which is a small, hydrophobic, integral membrane protein with a predominant role in water and glycerol transport. Recently, altered expression of AQP3 has been reported in many types of cancer. Increasing evidence strongly suggests that AQP3 plays a key role in cancer cell proliferation, migration and invasion. In this study, we performed an insightful characteristic of AQP3 location and its protein expression in MCF-7 human breast adenocarcinoma and HepG2 hepatocellular carcinoma cell lines in the context of cancer biology using immunocytochemistry, immunofluorescence and Western blot analyses. AQP3 was found to be located in the cell membrane and cytoplasm of MCF-7 cells, and in the cytoplasm and nuclear membrane of HepG2 cells. Immunoblotting of proteins derived from both cell lines revealed a clear band with a molecular weight of approx. 30 kDa representing an unglycosylated form of AQP3. However, the expression of this protein was higher in MCF-7 than in HepG2. Concluding, our results clearly indicated variability in both the expression levels and subcellular location of the AQP3 protein in MCF-7 and HepG2 cell lines. This leads to the possibility that the expression patterns and subcellular location of AQP3 in the tested cancer cell lines are tissue-of-origin specific, and may be related to the aggressiveness of cancer cells and their mobility.
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