title: Is the hormone a protease? Proteolytic properties of human recombinant anti-mullerian hormone
metadata.name: dc.contributor.author
metadata.value: Rak, Alexandra
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Trofimov, Alexander
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Stefanov, Vasily
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Ischenko, Alexander
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2019-11-22T20:41:40Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2019-11-22T20:41:40Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2019-09
metadata.lang: -
metadata.name: dc.identifier.citation
metadata.value: Rak, A., Trofimov, A., Stefanov, V., and Ischenko, A. 2019. Is the hormone a protease? Proteolytic properties of human recombinant anti-mullerian hormone. Bio. Comm. 64(3): 201–210.
metadata.lang: en_GB
metadata.name: dc.identifier.other
metadata.value: https://doi. org/10.21638/spbu03.2019.304
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/16625
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: Anti-mullerian hormone (AMH) is a glycoprotein of the TGF-β cytokine superfamily
  that regulates the development of the mammalian reproductive system,
  as well as the functioning of mature gonads. Recombinant AMH (rAMH) is also
  able to induce apoptosis of malignant cells bearing AMH type II receptors (MISRII)
  on the surface. Development of rAMH-based anticancer drugs is hampered
  by the lack of accurate information about the tissues where the AMH active
  form is generated and about the enzyme that activates the hormone by specific
  proteolysis. According to one hypothesis, the proteolytic processing of the hormone
  is autocatalytic. The goal of this work was to investigate the proteolytic
  activity of rAMH and its biologically active form — C-terminal AMH fragment
  (C‑AMH). We showed that two forms of the hormone possess both autoproteolytic
  activity and the ability to influence the structure of other proteins. A
  full-length molecule of the hormone, as well as C-AMH, also forms complexes
  with aprotinin, an inhibitor of trypsin-like serine proteases. We determined that
  aprotinin competes for binding to C-AMH with antibodies blocking C-AMH interaction
  with MISRII. The obtained data suggest that AMH has proteolytic properties
  and that the site of specific AMH cleavage is involved in the interaction of
  the hormone with a specific receptor.
metadata.lang: en_GB
metadata.name: dc.language.iso
metadata.value: en
metadata.lang: en_GB
metadata.name: dc.publisher
metadata.value: St Petersburg State University
metadata.lang: en_GB
metadata.name: dc.relation.ispartofseries
metadata.value: Biological Communications;Volume 64; Issue 3
metadata.lang: -
metadata.name: dc.subject
metadata.value: anti-mullerian hormone
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: AMH
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: aprotinin
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: autoproteolysis
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: MIS
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protease
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: recombinant protein
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: Is the hormone a protease? Proteolytic properties of human recombinant anti-mullerian hormone
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: 201-210.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/16625/1/201-210.pdf
resources.format: Adobe PDF
resources.size: 982,16 kB