Objective. To examine whether T cell reactivity toward heat-shock proteins (HSP) contributes to cartilage destruction in rheumatoid arthritis (RA). Methods. An in vitro system was used, in which human cartilage explants were cocultured with hsp60activated synovial fluid mononuclear cells (SFMC) fro
Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60
✍ Scribed by Angela Wand-Württenberger; Bernd Schoel; Juraj Ivanyi; Stefan H. E. Kaufmann
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 412 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0014-2980
No coin nor oath required. For personal study only.
✦ Synopsis
Surface expression by mononuclear phagocytes of an epitope shared with mycobacterial heat shock protein 60*
Bone marrow-derived macrophages were stained with a variety of monoclonal antibodies (mAb) with specificity for the mycobacterial heat shock protein (hsp) 60 or with specific rabbit antiserum raised against mycobacterial hsp 60.The mAb h4L30 as well as the specific antiserum brightly stained bone marrowderived macrophages whereas all the other mAb as well as normal rabbit antiserum gave no or negligible reactivity. Surface expression of the shared epitope is observed by day 3 of in vitro cultivation and markedly increased by interferon-y stimulation on day 9. Although hsp 60 is thought to be restricted to the mitochondria1 compartment, antibody responses to this molecule have been implicated in autoimmunity. Our finding that bone marrow-derived macrophages express a cross-reactive epitope recognized by an mAb with specificity for amino acids 275 to 295 of the mycobacterial hsp60 is consistent with such a role.
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