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Functional effects of CRP binding to nuclei.

E G Shephard, P D van Helden, M Strauss

|July 1, 1986

Summary

Human C-reactive protein (CRP) binds to liver nuclei via calcium-dependent and independent mechanisms, affecting chromatin structure and DNA transcription. This interaction influences chromatin accessibility and may limit aberrant DNA transcription.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

C-reactive protein (CRP) is a key acute-phase protein involved in innate immunity.
CRP's interaction with cellular components, particularly chromatin, is not fully understood.
Liver nuclei are a potential site for CRP interaction due to their role in cellular processes.

Purpose of the Study:

To investigate the binding characteristics of human and rat CRP to liver nuclei.
To elucidate the role of calcium in CRP-chromatin interactions.
To determine the functional consequences of CRP binding on chromatin structure and DNA transcription.

Main Methods:

Isolation of autologous liver nuclei from human and rat subjects.
Biochemical assays to assess CRP binding to nuclei, including calcium-dependent and independent components.
Co-precipitation studies with histones to identify binding mediators.
Micrococcal nuclease digestion assays to evaluate chromatin accessibility.
Analysis of DNA transcription following saturated CRP binding.

Main Results:

Demonstrated calcium-dependent and independent binding of human and rat CRP to liver nuclei.
Identified CRP-polycation site interaction as a mediator for calcium-independent chromatin binding.
Observed complement-dependent solubilization of intact chromatin by bound CRP.
Showed enhanced micrococcal nuclease digestion, indicating increased linker DNA exposure.
Confirmed suppression of DNA transcription upon saturated CRP binding to nuclei.

Conclusions:

CRP binding to liver nuclei involves both calcium-dependent and independent mechanisms.
CRP binding alters chromatin structure by increasing linker DNA exposure, potentially affecting gene accessibility.
Suppressed DNA transcription following CRP binding may serve a protective role against aberrant transcription of damaged chromatin.

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