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Immunoradiometric assay for human serum amyloid P component
David J Millar1, Winston L Hutchinson, Mark B Pepys
1Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, Rowland Hill Street, London NW3 2PF, UK.
Journal of Immunological Methods
|June 29, 2011
Summary
A new immunoradiometric assay (IRMA) accurately measures human serum amyloid P component (SAP) in various biological fluids. This assay is stable and crucial for amyloidosis and Alzheimer's disease research, especially when accounting for drug interference.
Area of Science:
- Biochemistry
- Immunology
- Neuroscience
Background:
- Human serum amyloid P component (SAP) is implicated in amyloidosis and Alzheimer's disease.
- SAP is a potential therapeutic target for these neurodegenerative conditions.
Purpose of the Study:
- To develop and validate a robust immunoradiometric assay (IRMA) for quantifying human SAP.
- To assess SAP stability in biological samples and identify potential interferences.
Main Methods:
- Development and validation of a human SAP-specific immunoradiometric assay (IRMA).
- Assessment of SAP immunoreactivity stability under various storage conditions (temperature, freeze-thaw).
- Evaluation of assay performance across a 100-fold dynamic range (0.5-50 microg/L) in serum, plasma, and cerebrospinal fluid.
Main Results:
- The IRMA demonstrated robust and reproducible quantification of human SAP.
- Human SAP immunoreactivity remained stable during prolonged storage and repeated freeze-thaw cycles.
- Assay interference from CPHPC binding to SAP was identified, particularly in heparinized plasma, and was abrogated by omitting calcium.
Conclusions:
- A validated IRMA provides a reliable method for measuring human SAP in clinical samples.
- Understanding and mitigating CPHPC interference is essential for accurate SAP quantification in patients undergoing treatment.
- The assay's stability and dynamic range support its utility in amyloidosis and Alzheimer's disease research.
