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Studies on the interaction between TWEAK and the death receptor WSL-1/TRAMP (DR3)

A Kaptein1, M Jansen, G Dilaver

  • 1Cell Biology Department, GlaxoWellcome Medicines Research Centre, Stevenage, UK.

FEBS Letters
|November 30, 2000
PubMed

Insights

Tumor Necrosis Factor (TNF) receptor superfamily member WSL-1/TRAMP (DR3) does not bind TWEAK. These findings indicate WSL-1/TRAMP is not the primary receptor for the novel TNF-related molecule TWEAK.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • WSL-1/TRAMP (DR3) is a TNF receptor superfamily member involved in NF-kappaB activation and apoptosis.
  • TWEAK, a novel TNF-related molecule, has been hypothesized as the ligand for WSL-1/TRAMP.

Purpose of the Study:

  • To investigate the interaction between TWEAK and its putative receptor WSL-1/TRAMP.
  • To determine if WSL-1/TRAMP is the major receptor for TWEAK.

Main Methods:

  • In vitro binding assays using human and murine TWEAK ligands.
  • Cell-based assays to assess TWEAK binding and biological activity on cells with and without WSL-1/TRAMP expression.
  • Analysis of TWEAK interaction with cells from WSL-1/TRAMP knockout mice.

Main Results:

  • TWEAK did not interact with WSL-1/TRAMP in in vitro binding assays.
  • TWEAK bound strongly to cells lacking WSL-1/TRAMP surface expression, with observed biological activity.
  • Cells from WSL-1/TRAMP knockout mice retained the ability to interact with TWEAK.

Conclusions:

  • WSL-1/TRAMP is not the major receptor for TWEAK.
  • The findings challenge the proposed ligand-receptor relationship between TWEAK and WSL-1/TRAMP.

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