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Peptide binding to active class II MHC protein on the cell surface.

J F Vacchino1, H M McConnell

  • 1Department of Chemistry, Stanford University, Stanford, CA 94305, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|May 22, 2001
PubMed
Summary

Two isomers of empty class II MHC exist: active and inactive. Cell surface I-Ek (MHC class II) is mostly inactive, with active forms originating from intracellular pools or reactivation.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Empty class II MHC molecules exist in active (peptide-binding) and inactive forms.
  • Antigen-presenting cells (APCs) can load peptides onto surface MHC molecules from the extracellular environment.
  • This process is crucial for generating diverse peptide repertoires for T cell presentation.

Purpose of the Study:

  • To investigate the active and inactive isomers of I-Ek (a class II MHC molecule) on the surface of Chinese hamster ovary cells.
  • To understand the stability and origin of active I-Ek on the cell surface.

Main Methods:

  • Utilized Chinese hamster ovary cells expressing I-Ek.
  • Examined the functional states (active vs. inactive) of cell surface I-Ek.
  • Assessed the stability and decay kinetics of active I-Ek.

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Main Results:

  • Active cell surface I-Ek is unstable, with a half-life of approximately 14 minutes before decaying to the inactive form.
  • At steady state, less than 1% of total cell surface I-Ek is in the active isomer.
  • Active I-Ek molecules originate from both intracellular pools and the reactivation of inactive cell surface I-Ek.

Conclusions:

  • Cell surface I-Ek exists in both active and inactive forms, with the active form being transient.
  • The majority of cell surface I-Ek is in an inactive state, necessitating mechanisms for its replenishment and reactivation.
  • Understanding these dynamics is key to comprehending antigen presentation by MHC class II molecules.