CD8 and β2-microglobulin-free MHC class I molecules in T cell immunoregulationMHC class I molecules in T cell immunoregulation

Sandra Demaria, Yuri Bushkin

Research output: Contribution to journalReview article

20 Citations (Scopus)

Abstract

Intracellular assembly of MHC class I heavy chains with β2-microglobulin occurs prior to the expression of the antigen-presenting complex on the cell surface. The association of β2-microglobulin with newly synthesized class I heavy chains is thought to be a strict prerequisite for their transport to the cell surface. However, MHC class I molecules not associated with β2-microglobulin (β2-microglobulin-free class I heavy chains) have been detected on the surface of activated lymphoid cells. These molecules have different conformations. Therefore, their interactions with other membrane proteins and biological functions may be different from those assigned to β2-microglobulin-associated MHC class I molecules. The two forms of MHC class I molecules on the surface of activated cells can self-associated and also form complexes with distinct proteins. Upon interaction with the appropriate ligands these molecular complexes transduce signals regulating cell activation. The ligand for β2-microglobulin-free class I heavy chains appears to be soluble CD8. A model is presented describing a novel mechanism of immunoregulation mediated by both soluble and membrane-bound forms of CD8 and β2-microglobulin-free class I heavy chains.

Original languageEnglish (US)
Pages (from-to)61-69
Number of pages9
JournalInternational Journal of Clinical & Laboratory Research
Volume23
Issue number1-4
DOIs
StatePublished - Dec 1 1993

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T-cells
T-Lymphocytes
Molecules
Ligands
Conformations
Membrane Proteins
Chemical activation
Association reactions
Lymphocytes
Membranes
Antigens
Proteins

All Science Journal Classification (ASJC) codes

  • Clinical Biochemistry

Cite this

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abstract = "Intracellular assembly of MHC class I heavy chains with β2-microglobulin occurs prior to the expression of the antigen-presenting complex on the cell surface. The association of β2-microglobulin with newly synthesized class I heavy chains is thought to be a strict prerequisite for their transport to the cell surface. However, MHC class I molecules not associated with β2-microglobulin (β2-microglobulin-free class I heavy chains) have been detected on the surface of activated lymphoid cells. These molecules have different conformations. Therefore, their interactions with other membrane proteins and biological functions may be different from those assigned to β2-microglobulin-associated MHC class I molecules. The two forms of MHC class I molecules on the surface of activated cells can self-associated and also form complexes with distinct proteins. Upon interaction with the appropriate ligands these molecular complexes transduce signals regulating cell activation. The ligand for β2-microglobulin-free class I heavy chains appears to be soluble CD8. A model is presented describing a novel mechanism of immunoregulation mediated by both soluble and membrane-bound forms of CD8 and β2-microglobulin-free class I heavy chains.",
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AU - Bushkin, Yuri

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N2 - Intracellular assembly of MHC class I heavy chains with β2-microglobulin occurs prior to the expression of the antigen-presenting complex on the cell surface. The association of β2-microglobulin with newly synthesized class I heavy chains is thought to be a strict prerequisite for their transport to the cell surface. However, MHC class I molecules not associated with β2-microglobulin (β2-microglobulin-free class I heavy chains) have been detected on the surface of activated lymphoid cells. These molecules have different conformations. Therefore, their interactions with other membrane proteins and biological functions may be different from those assigned to β2-microglobulin-associated MHC class I molecules. The two forms of MHC class I molecules on the surface of activated cells can self-associated and also form complexes with distinct proteins. Upon interaction with the appropriate ligands these molecular complexes transduce signals regulating cell activation. The ligand for β2-microglobulin-free class I heavy chains appears to be soluble CD8. A model is presented describing a novel mechanism of immunoregulation mediated by both soluble and membrane-bound forms of CD8 and β2-microglobulin-free class I heavy chains.

AB - Intracellular assembly of MHC class I heavy chains with β2-microglobulin occurs prior to the expression of the antigen-presenting complex on the cell surface. The association of β2-microglobulin with newly synthesized class I heavy chains is thought to be a strict prerequisite for their transport to the cell surface. However, MHC class I molecules not associated with β2-microglobulin (β2-microglobulin-free class I heavy chains) have been detected on the surface of activated lymphoid cells. These molecules have different conformations. Therefore, their interactions with other membrane proteins and biological functions may be different from those assigned to β2-microglobulin-associated MHC class I molecules. The two forms of MHC class I molecules on the surface of activated cells can self-associated and also form complexes with distinct proteins. Upon interaction with the appropriate ligands these molecular complexes transduce signals regulating cell activation. The ligand for β2-microglobulin-free class I heavy chains appears to be soluble CD8. A model is presented describing a novel mechanism of immunoregulation mediated by both soluble and membrane-bound forms of CD8 and β2-microglobulin-free class I heavy chains.

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