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Related Experiment Video

Updated: Jul 7, 2026

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin
07:56

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin

Published on: January 17, 2012

HMGB1 develops enhanced proinflammatory activity by binding to cytokines.

Yonggang Sha1, Jaroslaw Zmijewski, Zhiwei Xu

  • 1Department of Medicine, University of Alabama, 1530 3rd Avenue South, Birmingham, AL 35294, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|February 6, 2008
PubMed
Summary

High mobility group box 1 protein (HMGB1) gains proinflammatory activity by binding to mediators like IL-1beta. This binding enhances cytokine production, influencing cellular activation and inflammatory responses.

Related Experiment Videos

Last Updated: Jul 7, 2026

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin
07:56

Modified Yeast-Two-Hybrid System to Identify Proteins Interacting with the Growth Factor Progranulin

Published on: January 17, 2012

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • High mobility group box 1 protein (HMGB1) is a nuclear protein with known extracellular roles in inflammation.
  • HMGB1's extracellular functions involve cellular activation and proinflammatory responses.

Purpose of the Study:

  • To investigate how HMGB1 acquires proinflammatory activity.
  • To determine the role of inflammatory mediators in modulating HMGB1's function.

Main Methods:

  • Inducible expression of FLAG-tagged HMGB1 in cell cultures with or without IL-1beta, IFN-gamma, or TNF-alpha.
  • Purification of HMGB1 and assessment of its effect on cytokine production by macrophages and neutrophils.
  • Investigating the binding of IL-1beta to HMGB1 and the impact of IL-1 receptor antagonism.

Main Results:

  • HMGB1 purified from cells cultured with IL-1beta, IFN-gamma, and TNF-alpha exhibited enhanced proinflammatory activity.
  • This enhanced activity included increased production of MIP-2 and TNF-alpha by exposed cells.
  • HMGB1 acquired proinflammatory activity upon binding to IL-1beta, and this activity was IL-1 receptor-dependent.

Conclusions:

  • HMGB1 acquires its proinflammatory activity through binding to specific proinflammatory mediators, exemplified by IL-1beta.
  • The interaction of HMGB1 with IL-1beta is crucial for its enhanced inflammatory function.
  • These findings highlight a mechanism by which HMGB1 contributes to inflammatory processes.