The dendritic cell-derived protein DC-STAMP is highly conserved and localizes to the endoplasmic reticulum.
Article Details
- CitationCopy to clipboard
Eleveld-Trancikova D, Triantis V, Moulin V, Looman MW, Wijers M, Fransen JA, Lemckert AA, Havenga MJ, Figdor CG, Janssen RA, Adema GJ
The dendritic cell-derived protein DC-STAMP is highly conserved and localizes to the endoplasmic reticulum.
J Leukoc Biol. 2005 Mar;77(3):337-43. doi: 10.1189/jlb.0804441. Epub 2004 Dec 15.
- PubMed ID
- 15601667 [ View in PubMed]
- Abstract
Recently, we described the molecular identification of dendritic cell-specific TrAnsMembrane protein (DC-STAMP), a multimembrane-spanning protein preferentially expressed by human DC (hDC). In this report, we describe the identification and expression profile of the murine homologue of DC-STAMP (mDC-STAMP) as well as the characterization of the DC-STAMP protein. The results demonstrate that mDC-STAMP is over 90% homologous to hDC-STAMP and is also preferentially expressed by DC in vitro and ex vivo. mDC-STAMP expression is enhanced by interleukin-4 and down-regulated upon DC maturation. Analysis of differently tagged DC-STAMP proteins further demonstrates that hDC-STAMP and mDC-STAMP are glycosylated and primarily localize to an intracellular compartment. Applying confocal microscopy and electron microscopy, we demonstrate that hDC-STAMP localizes to the endoplasmic reticulum (ER) in human embryonic kidney 293 cells as well as hDC transduced with an adenovirus encoding hDC-STAMP-green fluorescent protein fusion protein. These data imply that DC-STAMP may exert its effect in the ER.