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Proteases involved in MHC dass II antigen presentation (1999)

Villadangos, José A. ; Bryant, Rebecca A. R. ; Deussing, Jan ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Immunological reviews 172 (1999), S. 0

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ISSN: 1600-065X

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Summary: Major histocompatibility complex class II antigen presentation requires the participation of lysosomal proteases in two convergent processes. First, the antigens endocytosed by the antigen-presenting cells must be broken down into antigenic peptides. Second, class II tnolecules are synthesized with their peptide-binding site blocked by invariant chain (li), and they acquire the capacity to bind antigens only after Ii has been degraded in the compartments where peptides reside. The study of genetically modified tnice deficietit in single lysosomal proteases has allowed us to determine their role in these processes, Cathepsins (Cat) B and D. previously considered major players in MHC class II antigen presentation, are dispensable for degradation of Ii and for generation of several antigenic determinants. By contrast, Cat S plays an essential role in removal of Ii in B cells and dendritic cells, whereas Cat L apparently does so in thymic epithelial cells. Accordingly, the absence of Cat S and L have major consequences for the onset of humoral immtine responses and for T-cell selection, respectively. It is likely that other as yet uncharacterized lysosomal enzymes also play a role in Ii degradation and in generation of antigenic determinants. Experiments involving drugs that interfere with protein traffic suggest that more than one mechanism for Ii removal, probably involving different proteases, can co-exist in the same antigen-presenting cell. These findings may allow the development of protease inhibitors with possible therapeutic applications.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1600-065X.1999.tb01360.x

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The genes of the lysosomal cysteine proteinases cathepsin B, H, L, and S map to different mouse chromosomes (1997)

Deussing, Jan ; Roth, Wera ; Rommerskirch, Winfried ; [et al.]

Springer

Mammalian genome 8 (1997), S. 241 -245

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ISSN: 1432-1777

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract. The mouse genes for the lysosomal cysteine proteinases cathepsin B, H, L, and S were mapped to Chromosomes (Chrs) 14, 9, 13, and 3, respectively. Two of the DNA probes used in this study detected an additional, independently segregating locus. The cathepsin B-specific probe hybridized to a locus on Chr 2, and the cathepsin H probe to a locus on the X Chr. These loci either correspond to pseudogenes or to cathepsin B- and cathepsin H-related genes. The four cysteine proteinases mapped in this study lie within known regions of conserved synteny between mouse and human chromosomes, when compared with the corresponding positions of their human homologs. Assuming that the genes of the cysteine proteinase gene family arose from a common ancestral gene, our results suggest that these four cysteine proteinases had been dispersed over different chromosomes before separation of mouse and human in evolution.