Cloning, recombinant expression and biochemical characterization of the murine CD83 molecule which is specifically upregulated during dendritic cell maturation

被引：73
作者：
Berchtold, S
Mühl-Zürbes, P
Heufler, C
Winklehner, P
Schuler, G
Steinkasserer, A
机构：
[1] Univ Erlangen Nurnberg, Dept Dermatol, D-91052 Erlangen, Germany
[2] Univ Innsbruck, Dept Dermatol, A-6020 Innsbruck, Austria
来源：
FEBS LETTERS | 1999年 / 461卷 / 03期
关键词：
CD83; dendritic cell; cDNA; recombinant protein;
D O I：
10.1016/S0014-5793(99)01465-9
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Human CD83 (hCD83) is a glycoprotein expressed predominantly on the surface of dendritic cells (DC) and represents the best marker for mature DC. Here, we report the cloning of the cDNA encoding mouse CD83 (mCD83) from a murine bone marrow-derived DC (BM-DC) cDNA library, DNA sequence analysis revealed a 196 amino acid protein including a signal peptide of 21 amino acids which shares 63% amino acid identity with hCD83, Using Northern blot analyses, mCD83 mRNA was found to be strongly expressed in mouse BM-DC and its expression was upregulated following stimulation with LPS or TNF-alpha. Transfection experiments using COS-7 cells revealed that mCD83 is glycosylated. Furthermore, the extracellular CD83 domain was recombinantly expressed in Escherichia coli and one-dimensional NMR data strongly support that the protein is structurally folded. (C) 1999 Federation of European Biochemical Societies.
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收藏
页码：211 / 216
页数：6
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