Proteomics Identification and Validation of Desmocollin-1 and Catechol-O-Methyltransferase as Proteins Associated with Breast Cancer Cell Migration and Metastasis
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
31617665
DOI
10.1002/pmic.201900073
Knihovny.cz E-zdroje
- Klíčová slova
- breast cancer, mass spectrometry, metastasis, sequential window acquisition of all theoretical, transmembrane proteins,
- MeSH
- analýza přežití MeSH
- buněčná membrána metabolismus MeSH
- desmokoliny genetika metabolismus MeSH
- fenotyp MeSH
- invazivní růst nádoru MeSH
- katechol-O-methyltransferasa genetika metabolismus MeSH
- lidé MeSH
- lymfatické metastázy patologie MeSH
- nádorové buněčné linie MeSH
- nádory prsu genetika metabolismus patologie MeSH
- pohyb buněk * genetika MeSH
- proteomika * MeSH
- receptor erbB-2 MeSH
- regulace genové exprese u nádorů MeSH
- triple-negativní karcinom prsu genetika metabolismus patologie MeSH
- upregulace genetika MeSH
- Check Tag
- lidé MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- COMT protein, human MeSH Prohlížeč
- desmokoliny MeSH
- DSC1 protein, human MeSH Prohlížeč
- ERBB2 protein, human MeSH Prohlížeč
- katechol-O-methyltransferasa MeSH
- receptor erbB-2 MeSH
Biological treatment of many cancers currently targets membrane bound receptors located on a cell surface. To identify novel membrane proteins associated with migration and metastasis of breast cancer cells, a more migrating subpopulation of MDA-MB-231 breast cancer cell line is selected and characterized. A high-resolution quantitative mass spectrometry with SILAC labeling is applied to analyze their surfaceome and it is compared with that of parental MDA-MB-231 cells. Among 824 identified proteins (FDR < 0.01), 128 differentially abundant cell surface proteins with at least one transmembrane domain are found. Of these, i) desmocollin-1 (DSC1) is validated as a protein connected with lymph node status of luminal A breast cancer, tumor grade, and Her-2 status by immunohistochemistry in the set of 96 primary breast tumors, and ii) catechol-O-methyltransferase is successfully verified as a protein associated with lymph node metastasis of triple negative breast cancer as well as with tumor grade by targeted data extraction from the SWATH-MS data of the same set of tissues. The findings indicate importance of both proteins for breast cancer development and metastasis and highlight the potential of biomarker validation strategy via targeted data extraction from SWATH-MS datasets.
Zobrazit více v PubMed
X. Dai, L. Xiang, T. Li, Z. Bai, J. Cancer 2016, 7, 1281.
B. Weigelt, J. L. Peterse, L. J. van ’t Veer, Nat. Rev. Cancer 2005, 5, 591.
S. Al-Mahmood, J. Sapiezynski, O. B. Garbuzenko, T. Minko, Drug Delivery Transl. Res. 2018, 8, 1483.
S. B. Scheurer, C. Roesli, D. Neri, G. Elia, Proteomics 2005, 5, 3035.
P. Kischel, F. Guillonneau, B. Dumont, A. Bellahcène, V. Stresing, P. Clézardin, E. A. De Pauw, V. Castronovo, Neoplasia 2008, 10, 1014.
C. Roesli, B. Borgia, C. Schliemann, M. Gunthert, H. Wunderli-Allenspach, R. Giavazzi, D. Neri, Cancer Res. 2009, 69, 5406.
B. Borgia, C. Roesli, T. Fugmann, C. Schliemann, M. Cesca, D. Neri, R. Giavazzi, Cancer Res. 2010, 70, 309.
H. Qiu, Y. Wang, J. Proteome Res. 2008, 7, 1904.
A. Shevchenko, H. Tomas, J. Havlis, J. V. Olsen, M. Mann, Nat. Protoc. 2006, 1, 2856.
P. Bouchal, M. Dvořáková, T. Roumeliotis, Z. Bortlíček, I. Ihnatová, I. Procházková, J. T. Ho, J. Maryáš, H. Imrichová, E. Budinská, R. Vyzula, S. G. Garbis, B. Vojtěšek, R. Nenutil, Mol. Cell. Proteomics 2015, 14, 1814.
P. Bouchal, O. T. Schubert, J. Faktor, L. Čápková, H. Imrichová, K. Zoufalová, V. Paralová, R. Hrstka, Y. Liu, H. A. Ebhardt, E. Budinská, R. Nenutil, R. Aebersold, Cell Rep. 2019, 28, 832.
A. Lanczky, A. Nagy, G. Bottai, G. Munkacsy, A. Szabo, L. Santarpia, B. Győrffy, Breast Cancer Res. Treat. 2016, 160, 439.
A. J. Minn, G. P. Gupta, P. M. Siegel, P. D. Bos, W. Shu, D. D. Giri, A. Viale, A. B. Olshen, W. L. Gerald, J. Massagué, Nature 2005, 436, 518.
P. Bouchal, M. Dvořáková, A. Scherl, S. D. Garbis, R. Nenutil, B. Vojtěšek, Proteomics 2013, 13, 1053.
J. Maryáš, J. Faktor, L. Čápková, P. Müller, P. Skládal, P. Bouchal, Cancer Genomics - Proteomics 2018, 15, 395.
Y. Perez-Riverol, A. Csordas, J. Bai, M. Bernal-Llinares, S. Hewapathirana, D. J. Kundu, A. Inuganti, J. Griss, G. Mayer, M. Eisenacher, E. Pérez, 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. Vizcaíno, Nucleic Acids Res. 2019, 47, D442.
A. Krogh, B. Larsson, G. Heijne, E. L. L. Sonnhammer, TMHMM Server v. 2.0 2001, retrieved from http://www.cbs.dtu.dk/services/TMHMM
E. E. Hedlund, P. C. McDonald, O. Nemirovsky, S. Awrey, L. D. E. Jensen, S. Dedhar, Cancers 2019, 11, 1002.
J. Zhang, Z. Zheng, M. Wu, L. Zhang, J. Wang, W. Fu, N. Xu, Z. Zhao, Y. Lao, H. Xu Cell Death Dis. 2019, 10, 554.
C. Montemagno, L. Dumas, P. Cavaillès, M. Ahmadi, S. Bacot, M. Debiossat, A. Soubies, L. Djaïleb, J. Leenhardt, N. Leiris, M. Dufies, G. Pagès, S. Hernot, N. Devoogdt, P. Perret, L. Riou, D. Fagret, C. Ghezzi, A. Broisat, Cancers (Basel) 2019, 11, 1.
Y. W. Chu, P. C. Yang, S. C. Yang, Y. C. Shyu, M. J. Hendrix, R. Wu, C. W. Wu, Am. J. Respir. Cell Mol. Biol. 1997, 17, 353.
W. T. Kao, C. Y. Lin, L. T. Lee, P. P. Lee, C. C. Hung, Y. S. Lin, S. H. Chen, F. C. Ke, J. J. Hwang, M. T. Lee, Anticancer Res. 2008, 28, 2109.
D. Jia, M. Yan, X. Wang, X. Hao, L. Liang, L. Liu, H. Kong, X. He, J. Li, M. Yao, BMC Cancer 2010, 10, 364.
M. Abdelkarim, N. Vintonenko, A. Starzec, A. Robles, J. Aubert, M. L. Martin, S. Mourah, M. P. Podgorniak, S. Rodrigues-Ferreira, C. Nahmias, P. O. Couraud, C. Doliger, O. Sainte-Catherine, N. Peyri, L. Chen, J. Mariau, M. Etienne, G. Y. Perret, M. Crepin, J. L. Poyet, A. M. Khatib, M. Di Benedetto, PLoS One 2011, 6, e23334.
J. Banyard, I. Chung, M. Migliozzi, D. T. Phan, A. M. Wilson, B. R. Zetter, D. R. Bielenber, BMC Cancer 2014, 14, 387.
O. Mendez, V. Peg, C. Salvans, M. Pujals, Y. Fernández, I. Abasolo, J. Perez, A. Matres, M. Valeri, J. Gregori, L. Villarreal, S. Schwartz Jr, Y. Ramon, S. Cajal, J. Tabernero, J. Cortes, J. Arribas, J. Villanueva, Clin. Cancer Res. 2018, 24, 6367.
S. E. Ong, M. Mann, Nat. Protoc. 2006, 1, 2650.
E. Thanopoulou, G. Kotzamanis, I. S. Pateras, N. Ziras, A. Papalambros, T. Mariolis-Sapsakos, F. Sigala, E. Johnson, A. Kotsinas, A. Scorilas, V. G. Gorgoulis, Tumor Biology 2012, 33,1429.
Y. Usami, K. Ishida, S. Sato, M. Kishino, M. Kiryu, Y. Ogawa, M. Okura, Y. Fukuda S. Toyosawa, Int. J. Cancer 2013, 133, 568.
L. Liu, M. Sun, D. Song, Z. Wang, Mol. Biol. Rep. 2013, 40, 1855.
N. V. Whittock, D. M. Hunt, L. Rickman, S. Malhi, A. P. Vogazianou, L. F. Dawson, R. A. Eady, R. S. Buxton, J. A. McGrath, Biochem. Biophys. Res. Commun. 2000, 276, 454.
Y. Kitajima, Kaohsiung J. Med. Sci. 2013, 29, 1.
K. Khan, R. Hardy, A. Haq, O. Ogunbiyi, D. Morton, Br. J. Cancer 2006, 95, 1367.
Y. Wang, C. Chen, X. Wang, F. Jin, Y. Liu, H. Liu, T. Li, J. Fu, J. Cancer Res. Clin. Oncol. 2016, 142, 2461.
T. Knösel, Y. Chen, S. Hotovy, U. Settmacher, A. Altendorf-Hofmann, I. Petersen, Int. J. Colorectal Dis. 2012, 27, 1391.
V. Jurčić, J. Kukovič, N. Zidar, Histol. Histopathol. 2015, 30, 945.
T. Cui, Y. Chen, L. Yang, M. Mireskandari, T. Knösel, Q. Zhang, L. H. Kohler, A. Kunze, N. Presselt, I. Petersen, J. Clin. Pathol. 2012, 65, 1100.
L. E. Kiss, P. Soares-da-Silva, J. Med. Chem. 2014, 57, 8692.
B. C. Lee, K. Cha, S. Avraham, H. K. Avraham, Int. J. Oncol. 2004, 24, 847.
W. Wu, J. Zhang, L. Zhou, L. You, Y. Zhao, J. Li, Sci. China Life Sci. 2012, 55, 747.
G. X. Wan, Y. W. Cao, W. Q. Li, Y. C. Li, F. Li, J. Breast Cancer 2014, 17, 149.
X. F. He, W. Wei, S. X. Li, J. Su, Y. Zhang, X. H. Ye, Y. Liu, W. Wang, Mol. Biol. Rep. 2012, 39, 6811.
J. Weisz, G. Fritz-Wolz, S. Gestl, G. A. Clawson, C. R. Creveling, J. G. Liehr, D. Dabbs, Am. J. Pathol. 2000, 156, 1841.
