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Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Akiyama N,Ohno Y,Fukuda T,Manome Y,Saito S

doi

10.1016/j.bbrc.2009.02.101

subject

Has Abstract

pub_date

2009-04-17 00:00:00

pages

612-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00378-7

journal_volume

381

pub_type

杂志文章

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