|
|
Previous Article | Table of Contents | Next Article 
Blood, 15 October 2000, Vol. 96, No. 8, pp. 2822-2827
IMMUNOBIOLOGY
Induction of neutrophil responsiveness to myeloperoxidase
antibodies by their exposure to supernatant of degranulated
autologous neutrophils
Christoph Hess,
Salima Sadallah, and
Jürg-Alfred Schifferli
From the Department of Research, University Hospital
Basel, Hebelstrasse 20, Basel, Switzerland.
Antibodies against myeloperoxidase (MPO) and proteinase 3 (PR3) are
the predominant autoantibodies present in antineutrophil cytoplasmic
antibody (ANCA)-associated vasculitis. Their binding to the
corresponding antigen on the surface of polymorphonuclear neutrophils
(PMNs) is believed to trigger the disease process. Cytokines released
during an inflammatory reaction are thought to prime resting PMNs,
making them responsive to autoantibodies. In the present study we found
that MPO but not PR3 could be detected on the cell surface of
unstimulated PMNs after incubation with the supernatants of activated
autologous PMNs. MPO was shown to be acquired from these supernatants,
because PMNs did not express MPO when the supernatants were
specifically MPO-depleted. In addition, purified soluble MPO bound to
unstimulated PMNs. Unstimulated PMNs that had passively acquired MPO
released oxygen radicals when incubated with monoclonal antibody
anti-MPO or the immunoglobulin G fraction of a patient with MPO-ANCA.
The data presented here suggest that, in ANCA-associated vasculitis,
soluble MPO released by activated PMNs may bind to unstimulated PMNs,
thereby making them reactive to anti-MPO antibodies. This mechanism of
dispersing PMN activation would be specific for MPO-ANCA and may
explain differences in the pathologic and clinical expression of
MPO-ANCA versus PR3-ANCA vasculitis.

CiteULike Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
D. Reumaux, P. L. Hordijk, P. Duthilleul, and D. Roos
Priming by tumor necrosis factor-{alpha} of human neutrophil NADPH-oxidase activity induced by anti-proteinase-3 or anti-myeloperoxidase antibodies
J. Leukoc. Biol.,
December 1, 2006;
80(6):
1424 - 1433.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Huugen, J. W. Cohen Tervaert, and P. Heeringa
TNF-{alpha} Bioactivity-Inhibiting Therapy in ANCA-Associated Vasculitis: Clinical and Experimental Considerations
Clin. J. Am. Soc. Nephrol.,
September 1, 2006;
1(5):
1100 - 1107.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
O. Gasser, A. Missiou, C. Eken, and C. Hess
Human CD8+ T cells store CXCR1 in a distinct intracellular compartment and up-regulate it rapidly to the cell surface upon activation
Blood,
December 1, 2005;
106(12):
3718 - 3724.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Huugen, H. Xiao, A. van Esch, R. J. Falk, C. J. Peutz-Kootstra, W. A. Buurman, J. W. C. Tervaert, J. C. Jennette, and P. Heeringa
Aggravation of Anti-Myeloperoxidase Antibody-Induced Glomerulonephritis by Bacterial Lipopolysaccharide: Role of Tumor Necrosis Factor-{alpha}
Am. J. Pathol.,
July 1, 2005;
167(1):
47 - 58.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
D. Reumaux, M. de Boer, A. B. Meijer, P. Duthilleul, and D. Roos
Expression of myeloperoxidase (MPO) by neutrophils is necessary for their activation by anti-neutrophil cytoplasm autoantibodies (ANCA) against MPO
J. Leukoc. Biol.,
June 1, 2003;
73(6):
841 - 849.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|