کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359972 | 1542326 | 2015 | 25 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The human rhabdomyosarcoma cell line TE671 - Towards an innovative production platform for glycosylated biopharmaceuticals
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کلمات کلیدی
PTMGM-CSFFCSNeu5AcIMACNeu5GcGlcNAcMALDI-TOFA1ATN-glycosylation - N-گلیکوزیلتalpha-1-antitrypsin - آلفا 1-آنتی تیپسینN-acetylneuraminic acid - اسید N-استیلون اورامینیکN-glycolylneuraminic acid - اسید N-گلیکولیل نورامنیکpost-translational modification - اصلاح post-translationalfetal calf serum - سرم گوساله جنینgranulocyte–macrophage colony-stimulating factor - عامل گرانولوسیت-ماکروفاژ colony-stimulating factorMatrix-Assisted Laser Desorption/Ionization Time-of-Flight - مدت زمان پرواز یونیزاسیون لیزر ماتریکس کمک می کندN-acetylglucosamine - نیتستیگلوکوزامینimmobilized metal ion affinity chromatography - کروماتوگرافی جذب یون فلز بی حرکتی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The market of therapeutic glycoproteins (including coagulation factors, antibodies, cytokines and hormones) is one of the profitable, fast-growing and challenging sectors of the biopharmaceutical industry. Although mammalian cell culture is still expensive and technically complex, the ability to produce desired post-translational modifications, in particular glycosylation, is a major issue. Glycans can influence ligand binding, serum half-life as well as biological activity or product immunogenicity. Aiming to establish a novel production platform for recombinant glycoproteins, the human TE671 cell line was investigated. Since the initial analysis of cell membrane proteins showed a promising glycosylation of TE671 cells for biotechnological purposes, we focused on the recombinant expression of two model glycoproteins of therapeutical relevance. The optimization of the cell transfection procedure and serum-free expression succeeded for the human serine protease inhibitor alpha-1-antitrypsin (A1AT) and the hematopoietic cytokine granulocyte-macrophage colony-stimulating factor (GM-CSF). N-glycan analyses of both purified proteins by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry provided first fundamental insights into the TE671 glycosylation potential. Besides protein specific pattern, strong distinctions - in particular for N-glycan fucosylation and sialylation - were observed depending on the medium conditions of the respective TE671 cell cultivations. The cell line's ability to synthesize complex and highly sialylated N-glycan structures has been shown. Our results demonstrate the TE671 cell line as a serious alternative to other existing human expression systems.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 83-94
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 83-94
نویسندگان
Julia Rosenlöcher, Constanze Weilandt, Grit Sandig, Stefan O. Reinke, Véronique Blanchard, Stephan Hinderlich,