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Related Experiment Videos

Pentraxin binding to isolated rat liver nuclei.

E G Shephard1, P J Smith, S Coetzee

  • 1MRC/UCT Liver Research Centre, Department of Medicine, Observatory, South Africa.

The Biochemical Journal
|October 1, 1991
PubMed
Summary

Human C-reactive protein (CRP) and serum amyloid P-component (SAP) bind to rat liver nuclei, including nuclear envelopes and histones. This study identified specific nuclear targets for these pentraxins using cross-linking techniques.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • C-reactive protein (CRP) and serum amyloid P-component (SAP) are pentraxins involved in innate immunity.
  • The interaction of pentraxins with nuclear components is not fully understood.
  • Identifying nuclear ligands for CRP and SAP is crucial for understanding their cellular functions.

Purpose of the Study:

  • To investigate the binding of human CRP and SAP to isolated rat liver nuclei.
  • To identify specific nuclear ligands for CRP and SAP using a cross-linking approach.
  • To differentiate between chromatin and nuclear envelope binding of these pentraxins.

Main Methods:

  • Utilized iodinatable heterobifunctional cross-linking reagent (SASD) for studying protein interactions.

Related Experiment Videos

  • Quantified binding of 125I-labelled CRP and SAP to isolated rat liver nuclei and nuclear envelopes.
  • Employed photocross-linking to identify specific protein targets within the nucleus.

    • Main Results:

    • Nuclei bound significantly more CRP (21 pmol) than SAP (2.7 pmol) at saturation.
    • Both pentraxins bound to nuclear envelopes, with SAP showing higher affinity.
    • Photocross-linking identified nuclear envelope proteins (43, 46, 52, 70 kDa) and histones (H2A, H2B, H3, H4 for SAP; H4 for CRP) as binding partners.

    Conclusions:

    • CRP and SAP interact with distinct nuclear components, including nuclear envelope proteins and histones.
    • SAP exhibits broader histone binding compared to CRP.
    • These findings elucidate specific nuclear targets for CRP and SAP, contributing to their functional understanding.