Physicochemical and Biological Characterization of rhC1INH Expressed in CHO Cells

التفاصيل البيبلوغرافية
العنوان: Physicochemical and Biological Characterization of rhC1INH Expressed in CHO Cells
المؤلفون: E. V. Zubareva, Ivan Lyagoskin, Maria Zhiliaeva, Rahim Shukurov, Maksim Degterev, Madina Iskakova, Ksenia Ulyanova, Maksim Smolov, Vladimir Simonov, Alexander Kazarov, Anna Azarova
المصدر: Pharmaceuticals
Volume 14
Issue 11
Pharmaceuticals, Vol 14, Iss 1180, p 1180 (2021)
سنة النشر: 2021
مصطلحات موضوعية: Ruconest®, Pharmaceutical Science, Berinert®, Article, rhC1INH, C1-inhibitor, law.invention, Blood serum, Pharmacy and materia medica, law, Drug Discovery, medicine, characterization, IC50, C1 inhibitor, biology, Molecular mass, acquired angioedema (AAE), Chemistry, Chinese hamster ovary cell, CHO cells, medicine.disease, Molecular biology, RS1-441, analytical methods, Hereditary angioedema, hereditary angioedema (HAE), biology.protein, Recombinant DNA, Molecular Medicine, Medicine, Specific activity
الوصف: The disfunction or deficiency of the C1 esterase inhibitor (C1INH) is associated with hereditary or acquired angioedema (HAE/AAE), a rare life-threatening condition characterized by swelling in the skin, respiratory and gastrointestinal tracts. The current treatment options may carry the risks of either viral infection (plasma-derived Berinert®) or immune reaction (human recombinant C1INH from rabbit milk, Ruconest®). This study describes the physicochemical and biological characterization of a novel recombinant human C1 esterase inhibitor (rhC1INH) from Chinese hamster ovary (CHO) cells for the treatment of hereditary angioedema compared to the marketed products Berinert® and Ruconest®. The mass spectrometry results of total deglycosylated rhC1INH revealed a protein with a molecular mass of 52,846 Da. Almost full sequence coverage (98.6%) by nanoLC-MS/MS peptide mapping was achieved. The purity and C1s inhibitory activity of rhC1INH from CHO cells are comparable with Ruconest®, although we found differences in charge isoforms distribution, intact mass values, and N-glycans profile. Comparison of the specific activity (IC50 value) of the rhC1INH with human C1 esterase inhibitor from blood serum showed similar inhibitory properties. These data allow us to conclude that the novel rhC1INH molecule could become a potential therapeutic option for patients with HAE/AAE.
وصف الملف: application/pdf
تدمد: 1424-8247
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aa34c4254abd99833665427e9ce8e82Test
https://pubmed.ncbi.nlm.nih.gov/34832963Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....4aa34c4254abd99833665427e9ce8e82
قاعدة البيانات: OpenAIRE