Biological strategy for high quality and productivity of recombinant proteins in animal cells by the use of metal transporters
| Project/Area Number |
21780309
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Kyoto University |
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Principal Investigator |
KAMBE Taiho Kyoto University, 大学院・生命科学研究科, 准教授 (90303875)
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| Project Period (FY) |
2009 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2009: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | 細胞工学 / 物質生産 / 糖鎖 / マンガン / トランスポーター / 組換え型タンパク質 / 動物細胞 / 微量金属 / 組み換え型タンパク質 |
|---|
| Research Abstract |
Mammalian cells are used for producing recombinant proteins whose post-translational modifications are important for their therapeutic efficacy. The manufacture of recombinant proteins is complicated by the need for both high levels of expression and appropriate processing of the nascent polypeptide, especially in glycoproteins, because the capacity of glycosylation in the secretory pathway is limited in the cells. In this study, we tried to improve the strategy for producing recombinant glycoproteins by identify metal transporters that supply metal such as zinc and manganese to glycosyltransferases in the secretory pathway because these metals are functional as cofactors of the enzymes. We found a homologue of Pmr1 that is a functional as calcium cannel in yeast is important for manganese transport and likely functional in glycosylation reaction in the secretory pathway, which may lead to the improvement of the secretion capacities of recombinant cells.
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Report
(3 results)
Research Products
(45 results)
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[Journal Article] Tissue non-specific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway,2011
Author(s)
Fukunaka A, Kurokawa Y, Teranishi F, Sekler I, Oda K, Ackland M. L, Faundez V, Hiromura M, Masuda S, Nagao M, Enomoto S, Kambe T
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Journal Title
J.Biol.Chem. 286
Pages: 16363-16373
Related Report
Peer Reviewed
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[Journal Article] Demonstration and characterization of the hetero-dimerization of ZnT5 and ZnT6 in the early secretory pathway2009
Author(s)
Fukunaka A, Suzuki T, Kurokawa Y, Yamazaki T, Fujiwara N, Ishihara K, Migaki H, Okumura K, Masuda S, Yamaguchi-Iwai Y, Nagao M, Kambe T
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Journal Title
J.Biol.Chem. 284
Pages: 30798-30806
Related Report
Peer Reviewed
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[Journal Article] Demonstration and characterization of the hetero-dimerization of ZnT5 and ZnT6 in the early secretory pathway2009
Author(s)
Fukunaka A, Suzuki T, Kurokawa Y, Yamazaki T, Fujiwara N, Ishihara K, Migaki H, Okumura K, Masuda S, Yamaguchi-Iwai Y, Nagao M, Kambe T
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Journal Title
The Journal of Biological Chemistry 284
Pages: 30798-30806
Related Report
Peer Reviewed
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[Journal Article] Tissue non-specific alkaline phosphatase is activated via a two-step mechanism by zinc transport complexes in the early secretory pathway
Author(s)
Fukunaka A, Kurokawa Y, Teranishi F, Sekler I, Oda K, Ackland M.L, Faundez V, Hiromura M, Masuda S, Nagao M, Enomoto S, Kambe T
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Journal Title
The Journal of Biological Chemistry
Volume: (in press)
Related Report
Peer Reviewed
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