Transgelin Silencing Induces Different Processes in Different Breast Cancer Cell Lines
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
32061197
DOI
10.1002/pmic.201900383
Knihovny.cz E-zdroje
- Klíčová slova
- apoptosis, breast cancer, cytoskeleton, metastasis, migration, transgelin,
- MeSH
- apoptóza * MeSH
- chromatografie kapalinová MeSH
- down regulace MeSH
- genový knockdown MeSH
- lidé MeSH
- MFC-7 buňky MeSH
- mikrofilamentové proteiny genetika metabolismus MeSH
- nádorové buněčné linie MeSH
- nádory prsu genetika metabolismus patofyziologie MeSH
- pohyb buněk * MeSH
- proteomika MeSH
- regulace genové exprese u nádorů * MeSH
- svalové proteiny genetika metabolismus MeSH
- tandemová hmotnostní spektrometrie MeSH
- umlčování genů MeSH
- Check Tag
- lidé MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- mikrofilamentové proteiny MeSH
- svalové proteiny MeSH
- transgelin MeSH Prohlížeč
Transgelin is a protein reported to be a marker of several cancers. However, previous studies have shown both up- and down-regulation of transgelin in tumors when compared with non-tumor tissues and the mechanisms whereby transgelin may affect the development of cancer remain largely unknown. Transgelin is especially abundant in smooth muscle cells and is associated with actin stress fibers. These contractile structures participate in cell motility, adhesion, and the maintenance of cell morphology. Here, the role of transgelin in breast cancer is focused on. Initially, the effects of transgelin on cell migration of the breast cancer cell lines, BT 549 and PMC 42, is studied. Interestingly, transgelin silencing increased the migration of PMC 42 cells, but decreased the migration of BT 549 cells. To clarify these contradictory results, the changes in protein abundances after transgelin silencing in these two cell lines are analyzed using quantitative proteomics. The results confirmed the role of transgelin in the migration of BT 549 cells and suggest the involvement of transgelin in apoptosis and small molecule biochemistry in PMC 42 cells. The context-dependent function of transgelin reflects the different molecular backgrounds of these cell lines, which differ in karyotypes, mutation statuses, and proteome profiles.
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H. Yamamura, H. Masuda, W. Ikeda, T. Tokuyama, M. Takagi, N. Shibata, M. Tatsuta, K. Takahashi, J. Biochem. 1997, 122, 157.
C. Shapland, P. Lowings, D. Lawson, J. Cell Biol. 1988, 107, 153.
M. Han, L. H. Dong, B. Zheng, J. H. Shi, J. K. Wen, Y. Cheng, Life Sci. 2009, 84, 394.
S. Tojkander, G. Gateva, P. Lappalainen, J. Cell Sci. 2012, 125, 1855.
H. Yu, M. Konigshoff, A. Jayachandran, D. Handley, W. Seeger, N. Kaminski, O. Eickelberg, FASEB J. 2008, 22, 1778.
C. B. Marshall, R. D. Krofft, M. J. Blonski, J. Kowalewska, C. M. Logar, J. W. Pippin, F. Kim, R. Feil, C. E. Alpers, S. J. Shankland, Am. J. Physiol.: Renal Physiol. 2011, 300, F1026.
M. Dvorakova, R. Nenutil, P. Bouchal, Expert Rev. Proteomics 2014, 11, 149.
Q. Li, R. Shi, Y. Wang, X. Niu, Tumor Biol. 2013, 34, 505.
Z. Yang, Y. J. Chang, H. Miyamoto, J. Ni, Y. Niu, Z. Chen, Y. L. Chen, J. L. Yao, P. A. di Sant'Agnese, C. Chang, Mol. Endocrinol. 2007, 21, 343.
M. Yeo, H. J. Park, D. K. Kim, Y. B. Kim, J. Y. Cheong, K. J. Lee, S. W. Cho, Cancer 2010, 116, 2581.
Z. W. Zhang, Z. M. Yang, Y. C. Zheng, Z. D. Chen, Asian J. Androl. 2010, 12, 186.
http://129.187.44.58:7070/NCI60/protein/show/14592 (accessed: December 2019).
N. Sayar, G. Karahan, O. Konu, B. Bozkurt, O. Bozdogan, I. G. Yulug, Clin. Epigenet. 2015, 7, 104.
I. S. Fenne, T. Helland, M. H. Flageng, S. N. Dankel, G. Mellgren, J. V. Sagen, PLoS One 2013, 8, e70096.
R. J. Price, K. A. Lillycrop, G. C. Burdge, J. Nutr. Sci. 2016, 5, e17.
A. R. Aikins, M. Kim, B. Raymundo, C. W. Kim, Exp. Biol. Med. 2017, 242, 573.
E. K. Lee, G. Y. Han, H. W. Park, Y. J. Song, C. W. Kim, J. Proteome Res. 2010, 9, 5108.
Y. Lin, P. J. Buckhaults, J. R. Lee, H. Xiong, C. Farrell, R. H. Podolsky, R. R. Schade, W. S. Dynan, Neoplasia 2009, 11, 864.
R. R. Nair, J. Solway, D. D. Boyd, J. Biol. Chem. 2006, 281, 26424.
J. Zhang, M. Q. Song, J. S. Zhu, Z. Zhou, Z. P. Xu, W. X. Chen, N. W. Chen, Int. J. Immunopathol. Pharmacol. 2011, 24, 849.
P. Bouchal, M. Dvorakova, A. Scherl, S. D. Garbis, R. Nenutil, B. Vojtesek, Proteomics 2013, 13, 1053.
I. Prochazkova, J. Lenco, A. Fucikova, J. Dresler, L. Capkova, R. Hrstka, R. Nenutil, P. Bouchal, Biochim. Biophys. Acta, Proteins Proteomics 2017, 1865, 488.
V. Pernikarova, V. Sedlacek, D. Potesil, I. Prochazkova, Z. Zdrahal, P. Bouchal, I. Kucera, J. Proteomics 2015, 125, 68.
Y. Perez-Riverol, A. Csordas, J. Bai, M. Bernal-Llinares, S. Hewapathirana, D. J. Kundu, A. Inuganti, J. Griss, G. Mayer, M. Eisenacher, E. Perez, J. Uszkoreit, J. Pfeuffer, T. Sachsenberg, S. Yilmaz, S. Tiwary, J. Cox, E. Audain, M. Walzer, A. F. Jarnuczak, T. Ternent, A. Brazma, J. A. Vizcaino, Nucleic Acids Res. 2019, 47, D442.
http://www.pawefish.path.cam.ac.uk/cell%20line%20catalogues/breast-cell-lines.htm (accessed: January 2020).
https://www.lgcstandards-atcc.org/products/all/HTB-122.aspx#characteristics (accessed: January 2020).
S. Bhatia, J. Monkman, T. Blick, P. H. Duijf, S. H. Nagaraj, E. W. Thompson, J. Clin. Med. 2019, 8, E1253.
https://portals.broadinstitute.org/ccle/page?cell_line=BT549_BREAST (accessed: January 2020).
A. Hall, Cancer Metastasis Rev. 2009, 28, 5.
R. H. Whitehead, I. Bertoncello, L. M. Webber, J. S. Pedersen, J. Natl. Cancer Inst. 1983, 70, 649.
A. Git, I. Spiteri, C. Blenkiron, M. J. Dunning, J. C. Pole, S. F. Chin, Y. Wang, J. Smith, F. J. Livesey, C. Caldas, Breast Cancer Res. 2008, 10, R54.
A. V. Le, M. Szaumkessel, T. Z. Tan, J. P. Thiery, E. W. Thompson, A. Dobrovic, Int. J. Mol. Sci. 2018, 19, E2553.
D. Rao, B. F. Kimler, W. B. Nothnick, M. K. Davis, F. Fan, O. Tawfik, Hum. Pathol. 2015, 46, 876.
H. M. Zhou, Y. Y. Fang, P. M. Weinberger, L. L. Ding, J. K. Cowell, F. Z. Hudson, M. Ren, J. R. Lee, Q. K. Chen, H. Su, W. S. Dynan, Y. Lin, BMC Cancer 2016, 16, 55.
H. Zhou, Y. Zhang, Q. Chen, Y. Lin, Dig. Dis. Sci. 2016, 61, 1091.
K. H. Tsui, Y. H. Lin, K. S. Chang, C. P. Hou, P. J. Chen, T. H. Feng, H. H. Juang, Int. J. Mol. Sci. 2019, 20, E4946.
L. Chunhua, L. Donglan, F. Xiuqiong, Z. Lihua, F. Qin, L. Yawei, Z. Liang, W. Ge, J. Linlin, Z. Ping, L. Kun, S. Xuegang, J. Nutr. Biochem. 2013, 24, 1766.
S. Diemert, A. M. Dolga, S. Tobaben, J. Grohm, S. Pfeifer, E. Oexler, C. Culmsee, J. Neurosci. Methods 2012, 203, 69.
R. Limame, A. Wouters, B. Pauwels, E. Fransen, M. Peeters, F. Lardon, O. De Wever, P. Pauwels, PLoS One 2012, 7, e46536.
L. H. Dong, J. K. Wen, G. Liu, M. A. McNutt, S. B. Miao, R. Gao, B. Zheng, H. Zhang, M. Han, Arterioscler., Thromb., Vasc. Biol. 2010, 30, 683.
P. Lv, S. B. Miao, Y. N. Shu, L. H. Dong, G. Liu, X. L. Xie, M. Gao, Y. C. Wang, Y. J. Yin, X. J. Wang, M. Han, Circ. Res. 2012, 111, 697.
X. L. Xie, X. Nie, J. Wu, F. Zhang, L. L. Zhao, Y. L. Lin, Y. J. Yin, H. Liu, Y. N. Shu, S. B. Miao, H. Li, P. Chen, M. Han, J. Mol. Med. 2015, 93, 547.
C. W. Gourlay, L. N. Carpp, P. Timpson, S. J. Winder, K. R. Ayscough, J. Cell Biol. 2004, 164, 803.
Y. Kato, B. C. Salumbides, X. F. Wang, D. Z. Qian, S. Williams, Y. Wei, T. B. Sanni, P. Atadja, R. Pili, Mol. Cancer Ther. 2007, 6, 70.
O. Thompson, J. S. Moghraby, K. R. Ayscough, S. J. Winder, BMC Cell Biol. 2012, 13, 1.
R. J. Mailloux, R. Beriault, J. Lemire, R. Singh, D. R. Chenier, R. D. Hamel, V. D. Appanna, PLoS One 2007, 2, e690.
T. Tanaka, F. Hosoi, Y. Yamaguchi-Iwai, H. Nakamura, H. Masutani, S. Ueda, A. Nishiyama, S. Takeda, H. Wada, G. Spyrou, J. Yodoi, EMBO J. 2002, 21, 1695.
M. Dvorakova, J. Jerabkova, I. Prochazkova, J. Lenco, R. Nenutil, P. Bouchal, J. Proteomics 2016, 132, 103.
