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Convergence between CD98 and integrin-mediated T-lymphocyte co-stimulation

A P Warren1, K Patel, Y Miyamoto

  • 1Department of Biochemistry, St George's Hospital Medical School, London, UK.

Immunology
|January 29, 2000
PubMed

Insights

The cell surface molecule CD98 (also known as solute carrier 3A2) plays a key role in T lymphocyte activation. Blocking beta1 integrin signaling inhibits CD98 co-stimulatory activity, suggesting convergent signaling pathways.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • CD98 is a heterodimeric glycoprotein expressed on the cell surface.
  • It is rapidly upregulated upon T lymphocyte activation.
  • Monoclonal antibody (mAb) 80A10 recognizes an epitope on CD98.

Purpose of the Study:

  • To investigate the co-stimulatory activity of CD98.
  • To determine the effect of beta1 integrin-blocking antibodies on CD98 co-stimulation.
  • To explore potential convergent signaling mechanisms between CD98 and integrins.

Main Methods:

  • Using monoclonal antibodies (mAbs) 80A10 and 4F2 to target CD98.
  • Employing CD3 antibody to induce T lymphocyte proliferation.
  • Utilizing soluble beta1 integrin antibody 18D3 to block integrin function.
  • Comparing the effects of 18D3 on CD98 and other non-integrin co-stimulatory molecules.

Main Results:

  • mAb 80A10 in combination with CD3 antibody induced proliferation of peripheral blood T lymphocytes.
  • CD98 co-stimulatory activity (mediated by mAb 80A10 or 4F2) was blocked by the soluble beta1 integrin antibody 18D3.
  • Previously, 18D3 was shown to inhibit co-stimulatory activity of specific integrins (alpha4beta1, alpha5beta1, alphaLbeta2, alpha4beta7) but not other non-integrins.
  • CD98 demonstrated unique sensitivity to beta1 integrin-blocking antibodies.

Conclusions:

  • CD98 is uniquely sensitive to inhibitory effects of beta1 integrin-blocking antibodies.
  • This sensitivity suggests convergent signaling mechanisms between integrins and CD98.
  • CD98 may play a role in regulating integrin-mediated adhesive events.

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