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Related Experiment Videos

Endosomal aspartic proteinases are required for invariant-chain processing

M A Marić1, M D Taylor, J S Blum

  • 1Immunology Program, Virginia Mason Research Center, Seattle, WA 98101.

Proceedings of the National Academy of Sciences of the United States of America
|March 15, 1994
PubMed
Summary

Acidic proteinases, including aspartic and cysteine types, are essential for processing the invariant chain (I-chain) and enabling the surface expression of functional Class II MHC complexes on antigen-presenting cells.

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Class II Major Histocompatibility Complex (MHC) molecules present peptides on antigen-presenting cells.
  • The invariant chain (I-chain) binds to Class II MHC alpha and beta subunits, preventing premature peptide binding.
  • I-chain dissociation must occur in an acidic compartment before Class II MHC can present peptides.

Purpose of the Study:

  • To investigate the proteolytic mechanisms involved in invariant chain (I-chain) dissociation.
  • To identify the specific proteinases responsible for I-chain processing.
  • To determine the cellular compartment where Class II MHC-I-chain interaction is resolved.

Main Methods:

  • Utilized B-lymphoblastoid cell lines.
  • Enzymatic inactivation of specific proteinases (aspartic and cysteine).

Related Experiment Videos

  • Analysis of Class II MHC alpha beta surface expression and I-chain processing.

    • Main Results:

    • Two distinct proteinases, an aspartic and a cysteine proteinase, sequentially process the I-chain.
    • Inactivation of these acidic proteinases prevents Class II MHC maturation and surface expression.
    • I-chain processing and subsequent Class II MHC complex formation occur in a dense endosomal compartment.

    Conclusions:

    • Acidic proteinases are critical for generating functional Class II MHC complexes.
    • Dense endosomes serve as the primary site for Class II MHC-peptide loading.
    • Cytoplasmic tail signals in I-chain fragments may retain Class II MHC in endosomes until processing is complete.