Endosomal proteolysis and MHC class II function
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Cited by (138)
Transcriptome analysis in the spleen of Northern Snakehead (Channa argus) challenged with Nocardia seriolae
2022, GenomicsCitation Excerpt :Cathepsin S (CTSS) was reported as key enzymes involved in the MHC class II-restricted antigens, which are presented by processing class II-associated invariant chains and loaded antigen peptides into class II molecules [53,54]. In vitro studies have shown that most cathepsins are involved in the processing of the invariant chain (Ii) and antigenic peptides [55]. Many studies have demonstrated that CTSS and CTSL are the most effective enzymes in regulating the gradual cleavage of Ii chains and maturation of MHC class II molecules [54,56,57].
Selective inhibition of peripheral cathepsin S reverses tactile allodynia following peripheral nerve injury in mouse
2020, European Journal of PharmacologyCitation Excerpt :One of the known substrates of CatS is the invariant chain (Ii). CatS plays a major role in the degradation of an intermediate Ii fragment, p10Ii (Chapman, 1998; Nakagawa and Rudensky, 1999; Villadangos et al., 1999; Villadangos and Ploegh, 2000). Thus, addition of CatS inhibitors to cultured cells or knockout of the CatS gene in mice results in the accumulation of the p10Ii fragment, and importantly, an impaired ability to present exogenous proteins by APC with a resulting reduced susceptibility to induction of autoimmune pathologies such as collagen-induced arthritis.
Genome-wide identification and transcript profile of the whole cathepsin superfamily in the intertidal copepod Tigriopus japonicus
2015, Developmental and Comparative ImmunologyIdentification of putative cathepsin S in mangrove red snapper Lutjanus argentimaculatus and its role in antigen presentation
2012, Developmental and Comparative ImmunologyCitation Excerpt :Before MHC class II molecules become expressed on the cell surface, the CLIP is removed and exchanged with the antigenic determinant peptides generated in the endosomes and lysosomes by the MHC-like molecule HLA-DM. The antigen peptide is then displayed on the cell surface (Chapman, 1998; Riese and Chapman, 2000). Proteolysis is required in this process; both for the degradation of the Ii chain from class II–Ii complexes to allow subsequent binding of peptides and for the generation of antigenic peptides (Riese et al., 1998).
Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells
2012, European Journal of Cell BiologyCitation Excerpt :A prerequisite for peptide loading to MHC II molecules is a proteolytic cleavage of Ii that occurs in sequential steps. The initiation of Ii processing results in the Iip22 and Iip10 intermediates and finally in CLIP (class II-associated invariant chain peptide), still attached to the MHC II molecule (Chapman, 1998). CLIP is exchanged for antigenic peptides in a reaction catalysed by another chaperone molecule, followed by translocation of MHC II–peptide complexes to the cell surface for recognition by CD4+ T cells (Denzin and Cresswell, 1995; Sherman et al., 1995).
Shark class II invariant chain reveals ancient conserved relationships with cathepsins and MHC class II
2012, Developmental and Comparative Immunology