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Related Experiment Video

Updated: Jun 20, 2026

Detection of CD40 Protein-Umbelliferone Interaction via Differential Scanning Fluorescence
05:30

Detection of CD40 Protein-Umbelliferone Interaction via Differential Scanning Fluorescence

Published on: March 1, 2024

OX40 (CD134) and OX40L.

Michael J Gough1, Andrew D Weinberg

  • 1Robert W. Franz Cancer Center, Earle A. Chiles Research Institute, Providence Portland Medical Center, Portland, OR, 97213, USA.

Advances in Experimental Medicine and Biology
|September 18, 2009
PubMed
Summary
This summary is machine-generated.

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The OX40-OX40L interaction enhances T-cell survival and immune responses. Blocking or mimicking this interaction offers therapeutic potential for autoimmune diseases and cancer immunotherapy.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The OX40-OX40L pathway is crucial for T-cell immune responses.
  • OX40 is primarily on activated T-cells, while OX40L is on antigen-presenting cells and endothelial cells.
  • This interaction influences T-cell survival and inflammatory processes.

Purpose of the Study:

  • To explore the role of OX40-OX40L ligation in T-cell responses.
  • To discuss the implications of this interaction in health and disease.
  • To highlight therapeutic strategies targeting the OX40-OX40L pathway.

Main Methods:

  • Review of existing literature on OX40-OX40L interactions.
  • Analysis of the molecular mechanisms underlying T-cell activation and survival.

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Generation of Human CD40-activated B cells
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  • Discussion of preclinical and clinical data on therapeutic interventions.

    • Main Results:

    • OX40 ligation by OX40L promotes T-cell survival and expansion.
    • The interaction modulates local inflammatory responses, impacting immunity and pathology.
    • Targeting this pathway can enhance anti-tumor immunity and treat autoimmune conditions.

    Conclusions:

    • The OX40-OX40L interaction is a key regulator of adaptive immunity.
    • Modulating this pathway holds significant therapeutic promise for immune-related diseases.
    • Understanding this TNFSF-TNFSF interaction is vital for developing novel immunotherapies.