S100 PROTEIN EXPRESSION AND THEIR SIGNIFICANCE IN DISSEMINATED BREAST CANCER
Keywords:
S100 proteins, Ca2+-dependent signaling, biomarkers, anti-cancer therapyAbstract
S100 proteins are small calcium-binding molecules with a specific EF-hand structure. These proteins are found throughout vertebrate bodies and serve many vital functions. Different cell types contain specific sets of S100 proteins, which ensures their targeted action.
Inside cells, S100 proteins control various enzymes and other proteins. Outside cells, they work as messenger molecules carrying signals between cells. S100 proteins manage calcium levels and affect how cells divide, mature, and die.
During tumor growth, S100 protein levels often change. Higher levels of certain S100 family members are found in breast cancer, lung cancer, and melanoma. These proteins also play a role in inflammation and some nervous system disorders.
Doctors measure S100 protein levels to diagnose various diseases. Scientists are creating drugs that target these proteins to treat cancer and other illnesses. However, we still don't fully understand how S100 proteins work.
Currently, researchers are studying how S100 proteins affect breast cancer. They aim to develop new treatments by controlling these proteins' activity. Their findings could lead to better ways to fight cancer.
Research shows that S100 proteins can both increase and decrease inflammation. This makes them promising targets for anti-inflammatory drugs. More research is needed to fully understand these unique proteins' role in the body.
This translation maintains the key information while using clear, direct language and avoiding abstract concepts. It's structured in short, focused paragraphs that each address a specific aspect of S100 proteins and their relationship to breast cancer.
References
Moore B. W. A soluble protein characteristic of the nervous system //Biochemical and biophysical research communications. – 1965. – Т. 19. – №. 6. – С. 739-744.
Isobe T., Okuyama T. The amino‐acid sequence of S‐100 protein (PAP I‐b protein) and its relation to the calcium‐binding proteins //European Journal of Biochemistry. – 1978. – Т. 89. – №. 2. – С. 379-388.
Isobe T., Okuyama T. The amino‐acid sequence of the α subunit in bovine brain S‐100a protein //European journal of biochemistry. – 1981. – Т. 116. – №. 1. – С. 79-86.
Kozlyuk N. et al. S100 proteins in the innate immune response to pathogens //Calcium-binding proteins of the EF-hand superfamily: from basics to medical applications. – 2019. – С. 275-290.
Singh P., Ali S. A. Multifunctional role of S100 protein family in the immune system: an update //Cells. – 2022. – Т. 11. – №. 15. – С. 2274.
Inciarte-Mundo J., Frade-Sosa B., Sanmartí R. From bench to bedside: Calprotectin (S100A8/S100A9) as a biomarker in rheumatoid arthritis //Frontiers in Immunology. – 2022. – Т. 13. – С. 1001025.
Gaynor, R.; Irie, R.; Morton, D.; Herschman, H.R. S100 protein is present in cultured human malignant melanomas. Nature 1980, 286, 400–401
Takashi, M.; Haimoto, H.; Murase, T.; Mitsuya, H.; Kato, K. An immunochemical and immunohistochemical study of S100 protein in renal cell carcinoma. Cancer 1988, 61, 889–895.
Gillett, C.E.; Bobrow, L.G.; Millis, R.R. S100 protein in human mammary tissue--immunoreactivity in breast carcinoma, including Paget’s disease of the nipple, and value as a marker of myoepithelial cells. J. Pathol. 1990, 160, 19–24
Li H. et al. S100A5 attenuates efficiency of anti‐PD‐L1/PD‐1 immunotherapy by inhibiting CD8+ T cell‐mediated anti‐cancer immunity in bladder carcinoma //Advanced Science. – 2023. – Т. 10. – №. 25. – С. 2300110.
Wang M. et al. Molecular mechanisms and clinical management of cancer bone metastasis //Bone research. – 2020. – Т. 8. – №. 1. – С. 30.
Sugino H., Sawada Y. Influence of S100A2 in human diseases //Diagnostics. – 2022. – Т. 12. – №. 7. – С. 1756.
Girish V. et al. Oncogene-like addiction to aneuploidy in human cancers //Science. – 2023. – Т. 381. – №. 6660. – С. eadg4521.
Zhang S. et al. Distinct prognostic values of S100 mRNA expression in breast cancer //Scientific reports. – 2017. – Т. 7. – №. 1. – С. 39786.
Li, Z.H.; Dulyaninova, N.G.; House, R.P.; Almo, S.C.; Bresnick, A.R. S100A4 regulates macrophage chemotaxis. Mol. Biol. Cell 2019, 21, 2598–2610.
Barraclough, R.; Rudland, P.S. The S-100-related calcium-binding protein, p9Ka, and metastasis in rodent and human mammary cells. Eur. J. Cancer 2019, 30a, 1570–1576.
Chen, P.S.; Wang, M.Y.; Wu, S.N.; Su, J.L.; Hong, C.C.; Chuang, S.E.; Chen, M.W.; Hua, K.T.; Wu, Y.L.; Cha, S.T.; et al. CTGF enhances the motility of breast cancer cells via an integrin-alphavbeta3-ERK1/2-dependent S100A4-upregulated pathway. J. Cell Sci. 2017, 120, 2053–2065.
Wang, G.; Zhang, S.; Fernig, D.G.; Martin-Fernandez, M.; Rudland, P.S.; Barraclough, R. Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes. Oncogene 2020, 24, 1445–1454.
Allgöwer C, Kretz A-L, von Karstedt S, Wittau M, Henne-Bruns D, Lemke J. Friend or Foe: S100 Proteins in Cancer. Cancers. 2020; 12(8):2037. https://doi.org/10.3390/cancers12082037
Shakhanova Shakhnoza , Rakhimov Nodir , Zaripova Parvina . Breast tumors in adolescent girls // Journal of Biomedicine and Practice. 2022, vol . 7, issue3, pp.266-273
Yorov , L. Sh., Juraev , M. D., Rakhimov, N. M. , Shakhanova , Sh. Sh. (2022). Assessment of the immune status in patients with breast cancer with determination of the effectiveness of neoadjuvant polychemotherapy . Journal of Biomedicine and Practice , 7 (5).
Lutfillo Yorov , Mirjalol Djuraev , Nodir Raximov , Shakhnoza Shakhanova . Evaluation of the state of the immune status in patients with breast cancer with the determination of the effectiveness of neoadjuvant polychemotherapy. Journal of Biomedicine and Practice. 2022, vol. 7, issue 5, pp.211-216