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CXCL12γ isoform is expressed on endothelial and dendritic cells in rheumatoid arthritis synovium and regulates T cell

Begoña Santiago1, Elena Izquierdo, Patricia Rueda

  • 1Hospital 12 de Octubre and Universidad Complutense de Madrid, Madrid, Spain.

Arthritis and Rheumatism
|September 29, 2011
PubMed

Insights

CXCL12γ, an alternative form of CXCL12, is increased in rheumatoid arthritis synovium and lymphoid tissues. Immobilized CXCL12γ on dendritic cells inhibits T cell activation, suggesting a distinct regulatory role in immune responses.

Area of Science:

  • Immunology
  • Molecular Biology
  • Rheumatology

Background:

  • CXCL12γ is an alternative splicing isoform of CXCL12 with higher affinity for heparan sulfate (HS) proteoglycans.
  • Its immobilization to HS may influence immune cell migration and activation in pathological and homeostatic settings.

Purpose of the Study:

  • Investigate the distribution and function of CXCL12γ in rheumatoid arthritis (RA) synovium and normal lymphoid tissue.
  • Determine the role of HS binding in CXCL12γ's interaction with dendritic cells (DCs) and its effect on T cell activation.

Main Methods:

  • Immunodetection of CXCL12 and CXCL12γ in synovial and lymphoid tissues.
  • Quantitative reverse transcription-polymerase chain reaction for mRNA expression analysis.
  • Flow cytometry to analyze HS-dependent binding of CXCL12 isoforms to DCs and their effect on T cell activation.

Main Results:

  • CXCL12γ expression is elevated in RA synovium compared to normal synovium, found in endothelia and DC-SIGN-positive cells.
  • Monocyte-derived DCs exhibit high HS-dependent binding of CXCL12γ.
  • Surface-bound CXCL12γ on DCs potently inhibits allogeneic T cell activation, unlike soluble forms.

Conclusions:

  • CXCL12γ exhibits a specific distribution in RA synovium and lymphoid tissue, correlating with its HS binding affinity.
  • Membrane-bound CXCL12γ on DCs plays a distinct regulatory role in T cell activation via HS interactions.
Abstract

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