Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells
Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells
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DOI:
10.1016/j.bbrc.2009.02.101
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发表时间:
2009-04-17
影响因子:
3.1
通讯作者:
Saito, Saburo
中科院分区:
文献类型:
--
作者:
Akiyama, Nobutake;Ohno, Yuji;Saito, Saburo
Several fusion proteins of mouse Interleukins (mILs) and the enhanced green fluorescent protein (EGFP) were expressed in fibroblast and epithelial cells. Among these proteins, the mIL-31 derivative was the most efficiently secreted into the medium in a N-glycosylation-dependent manner. From the analysis of deletion mutants, the minimal structure for constitutive secretions consisted of a signal peptide and N-glycosylation. Introduction of the signal sequence from mIL-31 to human p53 protein failed to secrete the products, but further addition of the N-glycosylation site resulted in constitutive secretion of biologically active p53 protein into the medium in the N-glycosylated form. In this report, we showed the importance of N-glycosylation for constitutive protein secretions, especially using non-polarized cells. (C) 2009 Elsevier Inc. All rights reserved