Parameters of cell death and proliferation of prostate cancer cells with altered expression of myosin 1C isoforms

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Abstract

Myosin 1C is a monomeric myosin motor with a truncated tail domain. Such motors are referred as slow “tension sensors”. Three isoforms of myosin 1C differ in short N-termed amino acid sequences, the functional differences between isoforms have not been elucidated. Myosin 1C isoform A has been described as a diagnostic marker for prostate cancer, but its role in tumor transformation remains unknown. Based on data on the functions of myosin 1C, we hypothesized the potential role of myosin 1C isoforms in maintaining the tumor phenotype of prostate cancer cells. In our work, we showed that a decrease in the expression level of myosin 1C isoform C leads to an increase in the proliferative activity of prostate tumor cells.

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About the authors

E. S. Solomatina

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: saidova@mail.bio.msu.ru
Russian Federation, Moscow

E. N. Nishkomaeva

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: saidova@mail.bio.msu.ru
Russian Federation, Moscow

A. V. Kovaleva

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences; Lomonosov Moscow State University

Email: saidova@mail.bio.msu.ru

Faculty of Biology

Russian Federation, Moscow; Moscow

A. V. Tvorogova

A. N. Belozersky Research Institute of Physico-Chemical Biology MSU

Email: saidova@mail.bio.msu.ru
Russian Federation, Moscow

D. M. Potashnikova

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences

Email: saidova@mail.bio.msu.ru
Russian Federation, Moscow

A. A. Saidova

Engelhardt Institute of Molecular Biology, Russian Academy of Sciences; Lomonosov Moscow State University

Author for correspondence.
Email: saidova@mail.bio.msu.ru
Russian Federation, Moscow; Moscow

References

  1. Greenberg M., Lin T., Goldman Y., et al. Myosin IC generates power over a range of loads via a new tension-sensing mechanism // PNAS. 2012. E2433–40.
  2. Bond L., Brandstaetter H., Kendrick-Jones J., et al. Functional roles for myosin 1c in cellular signaling pathways // Cellular signalling. 2013. V. 25. P. 229–235.
  3. Ihnatovych I., Migocka-Patrzalek M., Dukh M., et al. Identification and characterization of a novel myosin Ic isoform that localizes to the nucleus // Cytoskeleton. 2012. V. 69. P. 555–565.
  4. Pestic-Dragovich L., Stojiljkovic L., Philimonenko A., et al. A myosin I isoform in the nucleus // Science. 2000. V. 290. P. 337–341.
  5. Schwab R., Ihnatovych I., Yunus S., et al. Identification of signals that facilitate isoform specific nucleolar localization of myosin IC. // Exp Cell Res. 2013. V. 319. P. 1111–1112.
  6. Tokuo H, Coluccio LM. Myosin-1c regulates the dynamic stability of E-cadherin-based cell-cell contacts in polarized Madin-Darby canine kidney cells. // Mol Biol Cell. 2013. V. 24. P. 2820–2833.
  7. Arif E., Wager M., Johstone D. et al. Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane // Molecular and cellular biology. 2011. V. 31. P. 2134–2150.
  8. Diefenbach T., Latham Vol., Yimlamay D. et al. Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone // J Cell Biol. 2002. V. 158. P. 1207–1217.
  9. Bose A., Robida S., Furciitti P. et al. Unconventional myosin Myo1c promotes membrane fusion in a regulated exocytic pathway // Mol Cell Biol. 2004. V. 24. P. 5447–5458.
  10. Stauffer E., Scarborough J., Hirono M. et al. Fast adaptation in vestibular hair cells requires myosin-1c activity // Neuron. 2005. V. 47. P. 541–553.
  11. Ihnatovych I., Sielski N., Hofmann W. Selective expression of myosin IC Isoform A in mouse and human cell lines and mouse prostate cancer tissues // PlosOne. 2014. V. 9. P. e108609.
  12. Saidova A., Potashinkova D., Tvorogova A. et al. Specific and reliable detection of Myosin 1C isoform A by RTqPCR in prostate cancer cells // Peer J. 2018. V. 6. P. e5970.
  13. Saidova A., Potashinkova D., Tvorogova A. et al. Myosin 1C isoform A is a novel candidate diagnostic marker for prostate cancer // Plos One. 2021. V. 16. P. e0251961.
  14. Vandesompele J., De Preter K., Pattyn F. et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes // Genome Biol. 2002. V. 3. P. research0034.1.
  15. Potashnikova D., Golyshev S., Penin A. et al. FACS Isolation of Viable Cells in Different Cell Cycle Stages from Asynchronous Culture for RNA Sequencing // Methods Mol Biol. 2018. V. 1745. P. 315–335.
  16. Potashnikova D., Saidova A., Tvorogova A. et al. Non-linear Dose Response of Lymphocyte Cell Lines to Microtubule Inhibitors // Front Pharmacol. 2019. V. 10. P. 436.
  17. Brandstaetter H., Kishi-Itakura C., Tumbarello D., et al. Loss of functional MYO1C/myosin 1c, a motor protein involved in lipid raft trafficking, disrupts autophagosome-lysosome fusion // Autophagy. 2014. V. 10. P. 2310–2323.
  18. Hanahan D., Weinberg R. Hallmarks of cancer: the next generation // Cell. 2011. V. 144. P. 646–674.
  19. Ouderkirk J., Krendel M. Non‐muscle myosins in tumor progression, cancer cell invasion, and metastasis // Cytoskeleton. 2014. V. 71. P. 447–463.
  20. Tiwari A., Jung J., Inamdar S. et al. The myosin motor Myo1c is required for VEGFR2 delivery to the cell surface and for angiogenic signaling // Am J Physiol Heart Circ Physiol. 2013. V. 304. P. H687–H696.

Supplementary files

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2. Fig. 1. Expression of myosin 1C isoforms in model cell lines. a is the expression level of the mRNA isoforms A and C of myosin 1C in the control (1), when miRNA was added to the isoform A of myosin 1C (2) and when miRNA was added to the isoform C of myosin 1C (3). Average and standard deviations are shown, data are normalized for the reference genes YWHAZ, GAPDH and HPRT1; 5 are given independent experiments. b – expression of myosin 1C isoforms A and C in LNCaP cells under control and with the addition of doxycycline (Dox). I – staining with antibodies to pan-myosin 1C, II – staining with antibodies to the FLAG label, III – staining with antibodies to α-tubulin; 1 – control, 2 – FLAG-Myo1C-isoA line, 3 – FLAG-Myo1C-isoC line.

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3. Fig. 2. The main parameters of proliferation and cell death in the prostate cancer cell line PC-3 in control (1), with suppression of the expression of myosin 1C isoform A (2) and with suppression of the expression of myosin 1C isoform C (3). a – histograms of cell distribution over the cell cycle. b – the representation of Ki-67+ cells in the samples. b - histograms of the distribution of cells by stages of cell death. 3 independent experiments are presented, * – significant differences between groups, p<0.05, the Kraskell-Wallis test, the Dunn post-test.

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4. Fig. 3. The main parameters of proliferation and cell death in the LNCaP 3 prostate cancer cell line in the control (1), with overexpression of myosin 1C isoform A (2) and with overexpression of myosin 1C isoform C (3). a - histograms of cell distribution over the cell cycle. b – the representation of Ki‑67+ cells in the samples. b –histograms of the distribution of cells by stages of cell death. 3 independent experiments are presented, * – significant differences between groups, p < 0.05, the Kraskell–Wallis test, the Dunn post-test.

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