| http://purl.uniprot.org/citations/10748235 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10748235 | http://www.w3.org/2000/01/rdf-schema#comment | "The major histocompatibility complex (MHC) class II-associated invariant chain (Ii) regulates intracellular trafficking and peptide loading of MHC class II molecules. Such loading occurs after endosomal degradation of the invariant chain to a approximately 3-kD peptide termed CLIP (class II-associated invariant chain peptide). Cathepsins L and S have both been implicated in degradation of Ii to CLIP in thymus and peripheral lymphoid organs, respectively. However, macrophages from mice deficient in both cathepsins S and L can process Ii and load peptides onto MHC class II dimers normally. Both processes are blocked by a cysteine protease inhibitor, indicating the involvement of an additional Ii-processing enzyme(s). Comparison of cysteine proteases expressed by macrophages with those found in splenocytes and dendritic cells revealed two enzymes expressed exclusively in macrophages, cathepsins Z and F. Recombinant cathepsin Z did not generate CLIP from Ii-MHC class II complexes, whereas cathepsin F was as efficient as cathepsin S in CLIP generation. Inhibition of cathepsin F activity and MHC class II peptide loading by macrophages exhibited similar specificity and activity profiles. These experiments show that cathepsin F, in a subset of antigen presenting cells (APCs), can efficiently degrade Ii. Different APCs can thus use distinct proteases to mediate MHC class II maturation and peptide loading."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.org/dc/terms/identifier | "doi:10.1084/jem.191.7.1177"xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Li Z."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Ploegh H.L."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Bromme D."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Verhelst S."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Chapman H.A."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Driessen C."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Bryant R.A."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Shi G.P."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/author | "Riese R."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/name | "J Exp Med"xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/pages | "1177-1186"xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/title | "Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages."xsd:string |
| http://purl.uniprot.org/citations/10748235 | http://purl.uniprot.org/core/volume | "191"xsd:string |
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