Email this article HUMAN RECOMBINANT ANTI-MULLERIAN HORMONE: A SELF-ACTIVATING DRUG
- Authors: Rak A.Y.1,2, Trofimov A.V.1, Ischenko A.M.1
-
Affiliations:
- State Research Institute for Highly Pure Biopreparations
- Saint-Petersburg State University
- Issue: Vol 22, No 2-1 (2019)
- Pages: 486-488
- Section: ORIGINAL ARTICLES
- Submitted: 12.05.2020
- Accepted: 12.05.2020
- Published: 15.04.2019
- URL: https://rusimmun.ru/jour/article/view/191
- DOI: https://doi.org/10.31857/S102872210006939-7
- ID: 191
Cite item
Full Text
Abstract
Here, the autoproteolytic activity of human recombinant anti-Mullerian hormone (rAMH), a potential antineoplastic drug, was investigated. It was shown that the hormone is not only able to activate itself by the limited proteolysis, but also specifically interacts with the proteolytic inhibitor aprotinin. The involvement of the rAMH specific proteolysis site in interaction with a specifi c receptor type II (MISRII) was found. The data obtained may be useful to clarify some aspects of the native AMH biochemistry and pharmacodynamics of the recombinant hormone.
Keywords
About the authors
A. Ya. Rak
State Research Institute for Highly Pure Biopreparations;Saint-Petersburg State University
Author for correspondence.
Email: a.ya.rak@hpb.spb.ru
Junior Researcher of the Protein Biochemistry Laboratory;
PhD student,
St. Petersburg
Russian FederationA. V. Trofimov
State Research Institute for Highly Pure Biopreparations
Email: fake@neicon.ru
Group Head of the Protein Biochemistry Laboratory,
St. Petersburg
Russian FederationA. M. Ischenko
State Research Institute for Highly Pure Biopreparations
Email: fake@neicon.ru
PhD, Head of the Protein Biochemistry Laboratory,
St. Petersburg
Russian FederationReferences
- MacLaughlin D. T., Donahoe P. K.Müllerian inhibiting substance/anti-Müllerian hormone: a potential therapeutic agent for human ovarian and other cancers. Future Oncol. 2010, 6(3), 391–405.
- Jung Y. S., Kim H. J., Seo S. K., Choi Y. S., Nam E. J., Kim S. W., Han H. D., Kim J. W., Kim Y. T. Anti-proliferative and apoptotic activities of Müllerian inhibiting substance combined with calcitriol in ovarian cancer cell lines. Yonsei Med J. 2016, 57(1), 33–40.
- Di Clemente N., Jamin S. P., Lugovskoy A., Carmillo P., Ehrenfels C., Picard J. Y., Whitty A., Josso N., Pepinsky R. B., Cate R. L. Processing of anti-mullerian hormone regulates receptor activation by a mechanism distinct from TGF-β. Mol Endocrinol. 2010, 24(11), 2193–2206.
- Rak A. Ya., Trofi mov A. V., Protasov E. A., Rodin S. V., Zhakhov A. V., Zabrodskaya Ya. A., Ischenko A. M. Spontaneous proteolytic processing of human recombinant anti-mullerian hormone: structural and functional differences of the molecular forms. Appl Biochem Microbiol. 2019, 55(1),13–20.
- Рак А. Я., Трофимов А. В., Колобов А. А., Ищенко А. М. Моноклональные антитела против С-концевого фрагмента рекомбинантного антимюллерова гормона человека: инструмент для очистки, детекции и исследования. Цитокины и воспаление. 2018, 17(1–4), 72–79.
- Rak A. Ya., Trofimov A. V., Pigareva N. V., Simbirtsev A. S., Ischenko A. M. The cytotoxic effect of activated recombinant anti-mullerian hormone as a basis for the development of a new drug. Cell Tissue Biol. 2018, 12(6), 460–467.
Supplementary files
СМИ зарегистрировано Федеральной службой по надзору в сфере связи, информационных технологий и массовых коммуникаций (Роскомнадзор).