Skip to main content

Relationship Estimation of Cell Mobility Proteins Level with Processes of Proteolysis and Lymphogenic Metastasis in Breast Cancer

Abstract

The biological aggressiveness of a tumor is determined by the ability of tumor cells to invade and metastasize which is a consequence of their acquisition of a number of phenotypic characteristics. Remodeling of the actin cytoskeleton occurs during cell migration which is carried out by various groups of actin binding proteins in the regulation of which proteasomes and calpains play an important role. Therefore the study of the relationship of proteins associated with cell motility with the processes of lymphogenous metastasis as well as the assessment of the regulatory role of intracellular proteases in these processes is extremely important for fundamental oncology. This study demonstrates the associations of actin-binding proteins with the activity of proteasomes and calpain, which are specific for tumors and metastases of the mammary gland. We proposed a possible scheme of the relationship of intracellular systems with the actin-binding proteins. The results obtained expand the fundamental understanding of the processes of tumor progression and can also be used in the search for proteins-targets for therapeutic action in molecular targeted cancer therapy.

This is a preview of subscription content, access via your institution.

Fig. 1.
Fig. 2.

REFERENCES

  1. 1

    Dos Remedios, C.G., Chhabra, D., Kekic, M., et al., Actin binding proteins: regulation of cytoskeletal microfilaments (review), Physiol. Rev., 2003, vol. 83, no. 2, pp. 433–473.

    CAS  Article  Google Scholar 

  2. 2

    Guo, X., Wang, X., Wang , Z., et al., Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis, Nat. Cell Biol., 2016, vol. 18, no. 2, pp. 202–212.

    Google Scholar 

  3. 3

    Kakurina, G.V., Kondakova, I.V., Spirina, L.V., et al., Expression of genes encoding cell motility proteins during progression of head and neck squamous cell carcinoma, Bull. Exp. Biol. Med., 2018, vol. 166, no. 2, pp. 250–252.

    CAS  Article  Google Scholar 

  4. 4

    Islam S.M.-A., Patel, R., and Bommareddy, R.R., The modulation of actin dynamics via atypical protein kinase-C activated cofilin regulates metastasis of colorectal cancer cells, Cell Adh. Migr., 2018, no. 10, pp. 1–15.

  5. 5

    Del Carmen, Lafita-Navarro, M., and Conacci-Sorrell, M., Identification of calpain-activated protein functions, Methods Mol. Biol., 2019, vol. 1915, pp. 149–160.

    Article  Google Scholar 

  6. 6

    Stepanova, A.A., Lyupina, Yu.V., Sharova, N.P., et al., Native structure of rat liver immune proteasomes, Dokl. Akad. Nauk, 2016, vol. 468, no. 1, pp. 200–202.

    CAS  Google Scholar 

  7. 7

    Collins, G.A. and Goldberg, A.L., The logic of the 26S proteasome, Cell, 2017, vol. 169, no. 5, pp. 792–806.

    CAS  Article  Google Scholar 

  8. 8

    Jung, T. and Grune, T., Structure of the proteasome, Prog. Mol. Biol. Transl. Sci., 2012, vol. 109, pp. 1–39.

    CAS  Article  Google Scholar 

  9. 9

    Shashova, E.E., Astakhova, T.M., Plekhanova, A.S., et al., Changes in proteasome chymotrypsin-like activity during the development of human mammary and thyroid carcinomas, Bull. Exp. Biol. Med., 2013, vol. 156, no. 2, pp. 242–244.

    CAS  Article  Google Scholar 

  10. 10

    Shashova, E.E., Kondakova, I.V., Slonimskaya, E.M., et al., Changes in proteasome chymotrypsin-like and caspase-like activities depending on the prevalence of breast cancer, Sib. Onkol. Zh., 2013, no. 5, pp. 45–49.

  11. 11

    Shashova, E.E., Kolegova, E.S., Zav’yalov, A.A., et al., Changes in proteasome chymotrypsin-like activity during the development of human mammary and thyroid carcinomas, Bull. Exp. Biol. Med., 2017, vol. 163, no. 4, pp. 486–489.

    CAS  Article  Google Scholar 

  12. 12

    Shortrede, J.E., Uzair, I.D., Neira, F.J., et al., Paxillin, a novel controller in the signaling of estrogen to FAK/N-WASP/Arp2/3 complex in breast cancer cells, Mol. Cell Endocrinol., 2016, vol. 430, pp. 56–67.

    CAS  Article  Google Scholar 

  13. 13

    Molinie, N. and Gautreau, A., The Arp2/3 regulatory system and its deregulation in cancer, Physiol. Rev., 2018, vol. 98, no. 1, pp. 215–238.

    CAS  Article  Google Scholar 

  14. 14

    Shang, S., Hua, F., and Hu, Z.W., The regulation of β-catenin activity and function in cancer: therapeutic opportunities, Oncotarget, 2017, vol. 8, no. 20, pp. 33972–33989.

    Article  Google Scholar 

  15. 15

    Carragher, N.O., Assaying calpain activity, Methods Mol. Biol., 2007, vol. 370, pp. 109–120.

    CAS  Article  Google Scholar 

Download references

Author information

Affiliations

Authors

Corresponding author

Correspondence to E. E. Sereda.

Ethics declarations

Conflict of interest. All authors declare no conflicts of interest.

Statement of compliance with standards of research involving humans as subjects. The work was carried out in accordance with the principles of the Declaration of Helsinki of the World Medical Association “Ethical Principles for Conducting Scientific Medical Research with Human Participation,” as amended in 2000. In addition, informed consent was obtained from each patient included in the study, as well as the permission of the Ethics Committee of the Research Institute of Oncology, TNIMC.

Rights and permissions

Reprints and Permissions

About this article

Verify currency and authenticity via CrossMark

Cite this article

Sereda, E.E., Kolegova, E.S., Kakurina, G.V. et al. Relationship Estimation of Cell Mobility Proteins Level with Processes of Proteolysis and Lymphogenic Metastasis in Breast Cancer. Dokl Biochem Biophys 499, 211–214 (2021). https://doi.org/10.1134/S1607672921040153

Download citation

Keywords:

  • breast cancer
  • actin binding proteins
  • proteasomes
  • calpains
  • lymphogenous metastases