Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells.
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.
Akiyama
Nobutake
N
Department of Molecular Immunology, Institute of DNA medicine, Jikei University, Minato-ku, Tokyo, Japan. nakiyama@jikei.ac.jp
Ohno
Yuji
Y
Fukuda
Takahiro
T
Manome
Yosinobu
Y
Saito
Saburo
S
D000818:Animals; D016764:Cell Polarity; D005347:Fibroblasts / Q000378:metabolism; D006031:Glycosylation; D049452:Green Fluorescent Proteins / Q000378:metabolism; D006801:Humans; D007378:Interleukins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D007378:Interleukins; D011993:Recombinant Fusion Proteins; C485184:enhanced green fluorescent protein; C502588:interleukin-31, mouse; D049452:Green Fluorescent Proteins