Production of Recombinant Human Thyroid Peroxidase in Chinese Hamster Ovary Cells

1995 ◽  
pp. 385-389 ◽  
Author(s):  
I. I. Toshihiro ◽  
Makoto Murakami ◽  
Masahiro Mizuguchi ◽  
Ken Matsumoto ◽  
Kazukiyo Onodera
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Ovary Cells ◽  
Human Thyroid Peroxidase

Stable high level expression of human thyroid peroxidase in cultured Chinese hamster ovary cells

1989 ◽  
Vol 164 (3) ◽  
pp. 1268-1273 ◽  
Author(s):  
Jun-ichiro Hata ◽  
Shinya Yamashita ◽  
Satoru Yagihashi ◽  
Hideo Kato ◽  
Shoko Kabeno ◽  
...  
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
High Level Expression ◽  
Ovary Cells ◽  
Human Thyroid Peroxidase ◽  
High Level

Production of human thyroid-stimulating hormone in Chinese hamster ovary cells

1987 ◽  
Vol 149 (3) ◽  
pp. 1149-1155 ◽  
Author(s):  
Sachihiko Watanabe ◽  
Yoshihide Hayashizaki ◽  
Yuichi Endo ◽  
Machiko Hirono ◽  
Noriko Takimoto ◽  
...  
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Thyroid Stimulating Hormone ◽  
Human Thyroid ◽  
Ovary Cells ◽  
Stimulating Hormone

scholarly journals Recombinant Thyroid Peroxidase-Specific Fab Converted to Immunoglobulin G (IgG) Molecules: Evidence for Thyroid Cell Damage by IgG1, but Not IgG4, Autoantibodies1

1997 ◽  
Vol 82 (3) ◽  
pp. 925-931 ◽  
Author(s):  
Jin Guo ◽  
Juan Carlos Jaume ◽  
Basil Rapoport ◽  
Sandra M. McLachlan
Keyword(s):  
Cell Surface ◽  
B Cell ◽  
Cell Line ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Thyroid Peroxidase ◽  
51Cr Release ◽  
Thyroid Cells ◽  
Ovary Cells

Abstract A recombinant autoantibody Fab (SP1.4) to thyroid peroxidase (TPO), cloned from intrathyroidal B cell immunoglobulin genes, interacts with an epitope on TPO recognized by all patients with autoimmune thyroid disease. To compare the biological properties of IgG1 and IgG4 TPO autoantibodies, we converted Fab SP1.4 to full-length immunoglobulins. The SP1.4 heavy and κ light chain variable region genes, spliced by overlap PCR to a mammalian signal peptide, were transferred to expression vectors for human IgG1, IgG4, and κ L chains. Plasmids containing the IgG1 (or IgG4) heavy chain and the κ L chain were cotransfected into SP2/0 mouse myeloma cells. Cells secreting TPO autoantibodies were cloned, and IgG1-SP and IgG4-SP were affinity purified from medium using protein G. Their subclass specificities were confirmed by enzyme-linked immunosorbent assay and fluorometry after binding to Chinese hamster ovary cells expressing cell surface TPO. Further confirmation of SP1.4 Fab conversion to full-length molecules was the ability of protein A to precipitate IgG1-SP and IgG4-SP complexed to [125I]TPO. IgG1-SP1.4, IgG4-SP1.4, and Fab SP1.4 had similar high affinities for TPO (Kd = ∼2× 10−10 mol/L). Complexes of [125I]TPO and IgG1-SP (but not IgG4-SP) bound to peripheral blood mononuclear cells (PBMC), but not to a B cell line. Flow cytometry demonstrated Fc receptors FcγRI, FcγRII, and FcγRIII on PBMC, but only FcγRII on the B cell line. Together, these data indicate that IgG1-SP/TPO complexes bind to either FcγRI on monocytes or RIII on natural killer cells. In assays for antibody-dependent cytotoxicity using PBMC, 51Cr release was higher for thyroid cells preincubated with IgG1-SP (13.4%) than with IgG4-SP (2.5%) or with culture medium alone (−0.7%). No specific 51Cr release was observed when either fibroblasts or Chinese hamster ovary cells expressing cell surface TPO were used as target cells. In conclusion, a human TPO-specific Fab converted to IgG1, but not IgG4, can mediate cytotoxic effects on human thyroid cells in vitro. These observations support the clinical relevance of TPO autoantibody subclass distribution and emphasize the likelihood that, as opposed to being simple markers of thyroid damage, TPO autoantibodies may play a role in the induction of thyroid dysfunction in vivo.

Malignancy-related characteristics of wild type and drug-resistant chinese hamster ovary cells

Pathology ◽  
1993 ◽  
Vol 25 (3) ◽  
pp. 268-276 ◽  
Author(s):  
Wanda B. Mackinnon ◽  
Marlen Dyne ◽  
Rebecca Hancock ◽  
Carolyn E. Mountford ◽  
Adrienne J. Grant ◽  
...  
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Drug Resistant ◽  
Wild Type ◽  
Ovary Cells

Review of the current methods of Chinese Hamster Ovary (CHO) cells cultivation for production of therapeutic protein

2020 ◽  
Vol 17 ◽  
Author(s):  
Shazid Md. Sharker ◽  
Md. Atiqur Rahman
Keyword(s):  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Mass Production ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Therapeutic Protein ◽  
Specific Productivity ◽  
Ovary Cells ◽  
Further Development ◽  
Interesting Area

Most of clinical approved protein-based drugs or under in clinical trial have a profound impact in the treatment of critical diseases. The mammalian eukaryotic cells culture approaches, particularly the CHO (Chinese Hamster Ovary) cells are mainly used in the biopharmaceutical industry for the mass-production of therapeutic protein. Recent advances in CHO cell bioprocessing to yield recombinant proteins and monoclonal antibodies have enabled the expression of quality protein. The developments of cell lines are possible to upgrade specific productivity. As a result, it holds an interesting area for academic as well as industrial researchers around the world. This review will concentrate on the recent progress of the mammalian CHO cells culture technology and the future scope of further development for the mass-production of protein therapeutics.

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