DM exchange mechanism

Article Abstract:

DM products contribute to the liberation of class II antigen binding sites and allow loading with antigenic peptides as revealed by the studies of binding of peptides. Class II molecules not contacted by DM products become part of complexes containing class II-associated invariant-chain peptides, but these can be recovered by later contact with DM products. A transient interaction between an anti-class II-associated invariant-chain peptides blocks DM-mediated peptide loading of alphabeta-CLIP complexes. The structure of alphabeta-Ii complexes at atomic resolution must be determined to understand the process better.

Major histocompatibility complex, MHC antibodies

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A protease draws first blood

Article Abstract:

Manoury and colleagues have shown that asparaginyl endopeptidase (AEP), a protease is involved in major histocompatibility complex (MHC)-restricted antigen presentation. AEP may be identical to the legumain homologue recently cloned from mammalian tissue, and it is believed it draws first blood, executing initial digestion of tetanus toxin. High concentrations of natural peptide substrates were use to prevent the activity of AEP in vitro and in vivo, and little or no effect was seen by inhibitors on other cysteine proteases of the family, cathepsin.

Observations, Proteases, Antigens

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A proteolytic system that compensates for loss of proteasome function

Article Abstract:

Inactivation of the proteasome in mammalian cells by covalent inhibitors has been shown to permit the outgrowth of inhibitor-resistant cells. The growth of these cells seems to be maintained by the induction of other proteolytic systems that balance out the loss of proteasomal activity. The reduced proteasomal activity in adapted cells was found to be caused by covalent modification of beta-subunits by NIPL3-VS, an amino-terminally modified tri-leucine vinyl sulphone.

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