Individual cathepsins degrade immune complexes internalized by antigen-presenting cells via Fcgamma receptors.
Publication year
2001Source
European Journal of Immunology, 31, 5, (2001), pp. 1592-1601ISSN
Publication type
Article / Letter to editor

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Organization
Ophthalmology
Journal title
European Journal of Immunology
Volume
vol. 31
Issue
iss. 5
Page start
p. 1592
Page end
p. 1601
Subject
Hereditary and acquired vitreo-retinal disorders: experimental and clinical research and treatment.; Erfelijke en verworven vitreo-retinale aandoeningen: experimenteel en klinisch onderzoek en behandeling.Abstract
We have analyzed the intracellular degradation of an immune complex after its FcgammaR-mediated uptake in antigen-presenting cells (APC). Mice that lack the cathepsins (Cat) S, L, B and D allowed us to assess the direct contribution of these individual proteases to the processing events observed. CatS and CatB mediate the bulk of degradation of the Ig-125I-labeled F(ab')2 immune complex delivered via FcgammaR, while CatL and CatD are dispensable. CatS and CatB are involved in independent processing pathways and can substitute in part for each other's absence. The combined ablation of both proteases reduces the rate of degradation observed by > 80 %. CatB is required for the generation of F(ab')23, a predominant degradation intermediate smaller by approximately 3 kDa than the 125I-labeled F(ab')2 itself. In addition, absence of CatB in vivo significantly affects the activity pattern of the remaining cysteine proteases. Thus, we conclude that CatB is a key enzyme for the proper degradation of an immune complex taken up by FcgammaR and for the control of protease activity in the endocytic pathway of APC.
This item appears in the following Collection(s)
- Academic publications [202606]
- Faculty of Medical Sciences [79948]
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