Lysosomal Peptidases and Glycosidases in Rheumatoid Arthritis
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Nicolette Sohar
Abstract
Lysosomal serine and cysteine proteases are reported to play a role in collagen degradation. In this study, the activities of the lysosomal cysteine proteases cathepsin B and H, dipeptidyl peptidase I, and the serine protease tripeptidyl peptidase I and dipeptidyl peptidase II, all ascribed a role in collagen digestion, were compared with those of the aspartate protease cathepsin D, and lysosomal glycosidases in leukocytes from rheumatoid arthritis patients at different stages of the disease. In all patients the activities of cysteine protease cathepsin B, dipeptidyl peptidase I, aspartate protease cathepsin D, and two glycosidases were elevated, but the activities of the serine proteases tripeptidyl peptidase I, dipeptidyl peptidase II, and the cysteine protease cathepsin H was unchanged. The magnitude of the increased activity was correlated with the duration of the disease. Patients with longstanding RA (10 years or more) had higher cysteine protease activity in their leukocytes than did those with disease of shorter duration. This tendency suggests that elevated lysosomal cysteine protease activities, together with aspartate protease cathepsin D and lysosomal glycosidases (but not serine proteases), are associated with progression of rheumatoid arthritis.
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Nobuhiko Katunuma: An Outstanding Scientific and Professional Career of a Warm-Hearted Person. Reflections on the Occasion of his 75th Birthday
- Structural and Functional Diversity of Connexin Genes in the Mouse and Human Genome
- Congopain from Trypanosoma congolense: Drug Target and Vaccine Candidate
- Biosynthesis of Lysosomal Proteinases in Health and Disease
- Calpain Function in the Differentiation of Mesenchymal Stem Cells
- Ku Antigen Supports Termination of Mammalian rDNA Replication by Transcription Termination Factor TTF-I
- Thyroid Stimulating Hormone Upregulates Secretion of Cathepsin B from Thyroid Epithelial Cells
- Selective Release of Calpain Produced αII-Spectrin (α-Fodrin) Breakdown Products by Acute Neuronal Cell Death
- Altered Storage of Proteases in Mast Cells from Mice Lacking Heparin: A Possible Role for Heparin Carboxypeptidase A Processing
- Clustering-Induced Signaling of CEACAM1 in PC12 Cells
- Spin Adducts of Superoxide, Alkoxyl, and Lipid-Derived Radicals with EMPO and Its Derivatives
- Glutathione S-Transferase of the Malarial Parasite Plasmodium falciparum: Characterization of a Potential Drug Target
- Analysis of the Structural Determinants for RNA Binding of the Human Protein AUF1/hnRNP D
- Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro
- Stage-Specific Antimalarial Activity of Cysteine Protease Inhibitors
- Epoxysuccinyl Peptide-Derived Cathepsin B Inhibitors: Modulating Membrane Permeability by Conjugation with the C-Terminal Heptapeptide Segment of Penetratin
- Design of Inhibitors for Human Tissue Kallikrein Using Non-Natural Aromatic and Basic Amino Acids
- Amyloid Fibril Formation by Human Stefin B in vitro: Immunogold Labelling and Comparison to Stefin A
- Lysosomal Peptidases and Glycosidases in Rheumatoid Arthritis