The The analysis of the secondary structure of the proteins in blood serum of patients with multiple myeloma*

Авторы

  • Елена Чихиржина Институт цитологии Российской академии наук
  • Андрей Гарифуллин Russian Scientific Research Institute of Hematology and Transfusiology, 16, 2-ya Sovetskaya ul., St. Petersburg, 191024, Russian Federation https://orcid.org/0000-0003-0946-383X
  • Алексей Кувшинов Russian Scientific Research Institute of Hematology and Transfusiology, 16, 2-ya Sovetskaya ul., St. Petersburg, 191024, Russian Federation
  • Людмила Плотникова St. Petersburg State University, 7–9, Universitetskaya nab., St. Petersburg, 199034, Russian Federation https://orcid.org/0000-0002-3143-7630
  • Александр Поляничко Institute of Cytology of the Russian Academy of Sciences, 4, Tikhoretsky pr., St. Petersburg, 194064, Russian Federation;St. Petersburg State University, 7–9, Universitetskaya nab., St. Petersburg, 199034, Russian Federation
  • Елизавета Тельная St. Petersburg State University, 7–9, Universitetskaya nab., St. Petersburg, 199034, Russian Federation ; Pavlov First St. Petersburg State Medical University, 6–8, L’va Tolstogo ul., St. Petersburg, 197022, Russian Federation
  • Сергей Волошин Russian Scientific Research Institute of Hematology and Transfusiology, 16, 2-ya Sovetskaya ul., St. Petersburg, 191024, Russian Federation ; North-Western State Medical University named after I.I.Mechnikov, 41, Kirochnaya ul., St. Petersburg, 191015, Russian Federation ;S.M.Kirov Military Medical Academy, 6, ul. Akademika Lebedeva, St. Petersburg, 194044, Russian Federation https://orcid.org/0000-0003-1784-0375

DOI:

https://doi.org/10.21638/spbu11.2019.435

Аннотация

Multiple myeloma (MM) is one of the most common hematologic diseases in the world, which is characterized by the proliferation of clonal plasma cells in the bone marrow producing a monoclonal immunoglobulin. In this research, analysis of the secondary structure of proteins in blood serum of patients with MM and healthy donors was carried out by an infrared spectroscopy method. There were shown a decrease in the average content of α-helical sites and an increase in the number of β-layered structures in blood serum proteins of patients with MM compared to healthy donors.

Ключевые слова:

multiple myeloma, infrared spectroscopy, secondary structure of proteins

Скачивания

Данные скачивания пока недоступны.
 

Библиографические ссылки

Hallek M. 2019. Chronic lymphocytic leukemia: 2020 update on diagnosis, risk stratification and treatment. Am J Hematol. 94, 1266-1287.

Mimura N., Hideshima T., Anderson K.C. Novel therapeutic strategies for multiple myeloma. Exp. Hematol., 2015, vol. 43(8), pp. 732-741.

Rajkumar S.V., Kumar S. Multiple Myeloma: Diagnosis and Treatment. Mayo Clinic Proc., 2014, vol. 91, no. 1, pp. 101-119.

Kyle R.A., Rajkumar S.V. Criteria for diagnosis, staging, risk stratification and response assessment of multiple myeloma. Leukemia, 2009, vol. 23, no. 1, pp. 3-9.

Lee A.H., Iwakoshi N.N., Glimcher L.H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell Biol., 2003, vol. 23, no. 21, pp. 7448-7459.

Garcia-Carbonero R., Carnero A., Paz-Ares L. Inhibition of HSP90 molecular chaperones: moving into the clinic. Lancet Oncol., 2013, vol. 14, no. 9, pp. e358-369.

Polyanichko A.M., Andrushchenko V.V., Chikhirzhina E.V. et al. The effect of manganese(II) on DNA structure: electronic and vibrational circular dichroism studies. Nucl. Acids Res., 2004, vol. 32, no. 3, pp. 989-996.

Polyanichko A.M., Romanov N.M., Starkova T.Yu. et al. Analysis of the secondary structure of linker histone H1 based on IR absorption spectra. Cell Tiss. Biology, 2014, vol. 8, no. 4, pp. 352-358.

Plotnikova L., Polyanichko A., Nosenko T. et al. Characterization of the infrared spectra of serum from patients with multiple myeloma. AIP Conference processing, 2016, 1760, pp. 020052

Yang H., Yang S., Kong J. et al. Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy. Nat. Protoc., 2015, vol. 10, no. 3, pp. 382-396.

Susi H., Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol., 1986, vol. 130, pp. 290-311.

Barth A., Zscherp C. What vibrations tell about proteins. Quarterly Reviews of Biophysics, 2002, vol. 35, no. 4, pp. 369-430.

Kong J., Yu S. Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim. Biophys. Sin (Shanghai), 2007, vol. 39, no. 8, pp. 549-559.

Polyanichko A.M., Rodionova T.J., Vorob’ev V.I. et al. Conformational properties of nuclear protein HMGB1 and specificity of its interaction with DNA. Cell Tiss. Biology, 2011, vol. 5, no. 2, pp. 114-119.

Fonin A.V., Stepanenko O.V., Sitdikova A.K. et al. Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. Intern. J. Biol. Macromol., 2019, vol. 125, pp. 244-255.

Загрузки

Опубликован

15.06.2020

Как цитировать

Чихиржина, Е., Гарифуллин , А., Кувшинов, А., Плотникова, Л., Поляничко, А., Тельная, Е., & Волошин, С. (2020). The The analysis of the secondary structure of the proteins in blood serum of patients with multiple myeloma*. Вестник Санкт-Петербургского университета. Медицина, 14(4), 394–398. https://doi.org/10.21638/spbu11.2019.435

Выпуск

Том 14 № 4 (2019)

Раздел

Онкология

Лицензия

Статьи журнала «Вестник Санкт-Петербургского университета. Медицина» находятся в открытом доступе и распространяются в соответствии с условиями Лицензионного Договора с Санкт-Петербургским государственным университетом, который бесплатно предоставляет авторам неограниченное распространение и самостоятельное архивирование.