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  • Title: Potential sites for processing of the human invariant chain by cathepsins D and E.
    Author: Kageyama T, Yonezawa S, Ichinose M, Miki K, Moriyama A.
    Journal: Biochem Biophys Res Commun; 1996 Jun 25; 223(3):549-53. PubMed ID: 8687433.
    Abstract:
    Seven peptides of 15-30 amino acid residues were synthesized that covered almost the entire sequence of the lumenal domain of the human invariant chain (Ii), and their hydrolysis by cathepsins D and E was investigated. Two sites were identified that were very susceptible to such cleavage. One site, the Leu174-Phe175 bond, was cleaved by both cathepsins, and the other site, the Met99-Gln100 bond, was specifically cleaved by cathepsin E. These two sites could be the sites at which native Ii is cleaved by aspartic proteinases. The cleavage of the Met99-Gln100 bond by cathepsin E might be important in the inactivation of Ii and its functional derivatives.
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