ArticleImmunology2000
Lysosomal cathepsin B plays an important role in antigen processing, while cathepsin D is involved in degradation of the invariant chain inovalbumin-immunized mice.
Article in Immunology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 79 citations in OpenAlex.
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- Identification of the protease inhibitory domain of Trichinella spiralis novel cystatin (TsCstN).Parasites, hosts and diseases · 2024Article
- Cathepsin W restrains peripheral regulatory T cells for mucosal immune quiescence.Science advances · 2023Article
- Cysteine Cathepsins as Therapeutic Targets in Immune Regulation and Immune Disorders.Biomedicines · 2023Review
- The aging immune system in Alzheimer's and Parkinson's diseases.Seminars in immunopathology · 2022Review
- The Role of Cysteine Peptidases in Hematopoietic Stem Cell Differentiation and Modulation of Immune System Function.Frontiers in immunology · 2021Review
- Misfolded amyloid-β-42 impairs the endosomal-lysosomal pathway.Cellular and molecular life sciences : CMLS · 2020Article
- Rational Design of a Humanized Antibody Inhibitor of Cathepsin B.Biochemistry · 2020Article
- Cathepsins in Bacteria-Macrophage Interaction: Defenders or Victims of Circumstance?Frontiers in cellular and infection microbiology · 2020Review
- Quantitative Temporal in Vivo Proteomics Deciphers the Transition of Virus-Driven Myeloid Cells into M2 Macrophages.Journal of proteome research · 2017Article
- Cathepsin B-Deficient Mice Resolve Leishmania major Inflammation Faster in a T Cell-Dependent Manner.PLoS neglected tropical diseases · 2016Article
- Induction of an antitumor response using dendritic cells transfected with DNA constructs encoding the HLA-A*02:01-restricted epitopes of tumor-associated antigens in culture of mononuclear cells of breast cancer patients.Immunologic research · 2016Article
- Lysosome-Dependent Activation of Human Dendritic Cells by the Vaccine Adjuvant QS-21.Frontiers in immunology · 2016Article
- A Microbial Feed Additive Abates Intestinal Inflammation in Atlantic Salmon.Frontiers in immunology · 2015Article
- β2-microglobulin amyloid fibrils are nanoparticles that disrupt lysosomal membrane protein trafficking and inhibit protein degradation by lysosomes.The Journal of biological chemistry · 2014Article
- Cathepsin B in antigen-presenting cells controls mediators of the Th1 immune response during Leishmania major infection.PLoS neglected tropical diseases · 2014Article
- Antifungal Treatments Delineate a Correlation between Cathepsins and Cytokines in Murine Model of Invasive Aspergillosis.Indian journal of pharmaceutical sciences · 2013Article
- Enhancement of HLA class II-restricted CD4+ T cell recognition of human melanoma cells following treatment with bryostatin-1.Cellular immunology · 2011Article
- Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We previously reported that CA074, a specific inhibitor of cathepsin B, modulates specific immune responses from the T helper 2 (Th2) type to Th1 type in BALB/c mice infected with Leishmania major. In the present study, we found that a similar type of immune deviation was also induced in mice immunized with ovalbumin (OVA). However, treatment of mice with pepstatin A, a specific cathepsin D inhibitor, suppressed the OVA-specific proliferation of lymphocytes and blocked the development of both Th1 and Th2 cellular responses. These inhibitors did not appear to have any direct influence in vitro on functions of naive lymphocytes. OVA antigen (47 000 MW) was digested mainly into 40 000 MW protein in vitro by lysosomal proteases from naive BALB/c mice, and its digestion was markedly inhibited by the addition of CA074, but not by addition of pepstatin A, during incubation. However, pepstatin A strongly suppressed the degradation of the major histocompatibility complex class II-associated invariant chain (Ii) molecule in vivo and in vitro. Thus, cathepsin B appears to process antigens directed to preferential activation of Th2 cells, while cathepsin D may be responsible for the degradation of Ii, the processing of which is essential in initiating the antigen-specific activation of Th1 and Th2 CD4+ T cells. These lysosomal proteases may have different functions in regulating immune responses.
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