2018
Remšík, Ján; Binó, Lucia; Kahounová, Zuzana; Kharaishvili, Gvantsa; Šimecková, Šárka; Fedr, Radek; Kucírková, Tereza; Lenárt, Sára; Muresan, Ximena Maria; Slabáková, Eva; Knopfová, Lucia; Bouchal, Jan; Král, Milan; Beneš, Petr; Soucek, Karel
Trop-2 plasticity is controlled by epithelial-to-mesenchymal transition. Journal Article
In: Carcinogenesis, vol. 39, no. 11, pp. 1411–1418, 2018, ISSN: 1460-2180 0143-3334, (Place: England).
Abstract | Links | BibTeX | Tags: Animals, Antigens, Breast Neoplasms/mortality/*pathology, Cadherins/biosynthesis, Carcinoma/*pathology, CD/biosynthesis, Cell Adhesion Molecules/genetics/*metabolism, Cell Line, Disease Progression, DNA Methylation/genetics, Epithelial Cells/*metabolism, Epithelial-Mesenchymal Transition/physiology, Female, Humans, Inbred BALB C, Male, Mice, Neoplasm/genetics/*metabolism, Prostatic Neoplasms/mortality/*pathology, Tumor, Xenograft Model Antitumor Assays
@article{remsik_trop-2_2018,
title = {Trop-2 plasticity is controlled by epithelial-to-mesenchymal transition.},
author = {Ján Remšík and Lucia Binó and Zuzana Kahounová and Gvantsa Kharaishvili and Šárka Šimecková and Radek Fedr and Tereza Kucírková and Sára Lenárt and Ximena Maria Muresan and Eva Slabáková and Lucia Knopfová and Jan Bouchal and Milan Král and Petr Beneš and Karel Soucek},
doi = {10.1093/carcin/bgy095},
issn = {1460-2180 0143-3334},
year = {2018},
date = {2018-12-01},
journal = {Carcinogenesis},
volume = {39},
number = {11},
pages = {1411–1418},
abstract = {The cell surface glycoprotein Trop-2 is commonly overexpressed in carcinomas and represents an exceptional antigen for targeted therapy. Here, we provide evidence that surface Trop-2 expression is functionally connected with an epithelial phenotype in breast and prostate cell lines and in patient tumor samples. We further show that Trop-2 expression is suppressed epigenetically or through the action of epithelial-to-mesenchymal transition transcription factors and that deregulation of Trop-2 expression is linked with cancer progression and poor patient prognosis. Moreover, our data suggest that the cancer plasticity-driven intratumoral heterogeneity in Trop-2 expression may significantly contribute to response and resistance to therapies targeting Trop-2-expressing cells.},
note = {Place: England},
keywords = {Animals, Antigens, Breast Neoplasms/mortality/*pathology, Cadherins/biosynthesis, Carcinoma/*pathology, CD/biosynthesis, Cell Adhesion Molecules/genetics/*metabolism, Cell Line, Disease Progression, DNA Methylation/genetics, Epithelial Cells/*metabolism, Epithelial-Mesenchymal Transition/physiology, Female, Humans, Inbred BALB C, Male, Mice, Neoplasm/genetics/*metabolism, Prostatic Neoplasms/mortality/*pathology, Tumor, Xenograft Model Antitumor Assays},
pubstate = {published},
tppubtype = {article}
}
2006
Soucek, Karel; Kamaid, Andrés; Phung, Anh D.; Kubala, Lukás; Bulinski, J. Chloë; Harper, Richart W.; Eiserich, Jason P.
Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications. Journal Article
In: The Prostate, vol. 66, no. 9, pp. 954–965, 2006, ISSN: 0270-4137, (Place: United States).
Abstract | Links | BibTeX | Tags: *Protein Processing, Acetylation, Androgen/analysis, Androgens/physiology, Blotting, Cell Line, Disease Progression, Electrophoresis, Epithelium/chemistry/metabolism/pathology, Fluorescence, Humans, Male, Microscopy, Peptide Synthases/analysis/metabolism, Polyacrylamide Gel, Polyglutamic Acid/analysis, Post-Translational, Prostate/*chemistry/cytology/metabolism, Prostatic Neoplasms/*chemistry/metabolism/pathology, Receptors, Tubulin/*analysis/*metabolism, Tumor, Tyrosine/analysis, Western
@article{soucek_normal_2006,
title = {Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications.},
author = {Karel Soucek and Andrés Kamaid and Anh D. Phung and Lukás Kubala and J. Chloë Bulinski and Richart W. Harper and Jason P. Eiserich},
doi = {10.1002/pros.20416},
issn = {0270-4137},
year = {2006},
date = {2006-06-01},
journal = {The Prostate},
volume = {66},
number = {9},
pages = {954–965},
abstract = {BACKGROUND: Multiple diverse posttranslational modifications of alpha-tubulin such as detyrosination, further cleavage of the penultimate glutamate residue (Delta2-tubulin), acetylation, and polyglutamylation increase the structural and functional diversity of microtubules. METHODS: Herein, we characterized the molecular profile of alpha-tubulin posttranslational modifications in normal human prostate epithelial cells (PrEC), immortalized normal prostate epithelial cells (PZ-HPV-7), androgen-dependent prostate cancer cells (LNCaP), transitional androgen-independent prostate cancer cells (LNCaP-cds and CWR22Rv1), and androgen-independent prostate cancer cells (PC3). RESULTS: Compared to PrEC and PZ-HPV-7 cells, all cancer cells exhibited elevated levels of detyrosinated and polyglutamylated alpha-tubulin, that was paralleled by decreased protein levels of tubulin tyrosine ligase (TTL). In contrast, PrEC and PZ-HPV-7 cells expressed markedly higher levels of Delta2-tubulin. Whereas alpha-tubulin acetylation levels were generally equivalent in all the cell lines, PC3 cells did not display detectable levels of Ac-tubulin. CONCLUSION: These data may reveal novel biomarkers of prostate cancer and new therapeutic targets.},
note = {Place: United States},
keywords = {*Protein Processing, Acetylation, Androgen/analysis, Androgens/physiology, Blotting, Cell Line, Disease Progression, Electrophoresis, Epithelium/chemistry/metabolism/pathology, Fluorescence, Humans, Male, Microscopy, Peptide Synthases/analysis/metabolism, Polyacrylamide Gel, Polyglutamic Acid/analysis, Post-Translational, Prostate/*chemistry/cytology/metabolism, Prostatic Neoplasms/*chemistry/metabolism/pathology, Receptors, Tubulin/*analysis/*metabolism, Tumor, Tyrosine/analysis, Western},
pubstate = {published},
tppubtype = {article}
}