Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells
- Department of Molecular Immunology, Institute of DNA medicine, Jikei University, 3-25-8 Nishi-Shinbashi, Minato-ku, Tokyo 105-8461 (Japan)
- Department of Pharmacology, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, Tokyo 105-8461 (Japan)
- Division of Neuropathology, Dept. of Neuroscience, Research Center of Medical Science, The Jikei Univ. Schl. Med., 3-25-8 Nishi-Shimbashi, Minato-ku, Tokyo 105-8461 (Japan)
- Department of Molecular Cell Biology, Institute of DNA medicine, Jikei University, 3-25-8 Nishi-Shinbashi, Minato-ku, Tokyo 105-8461 (Japan)
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.
- OSTI ID:
- 22199656
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 381, Issue 4; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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