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Biosynthesis and postsynthetic processing of human C-reactive protein
Journal of Immunology (Baltimore, Md. : 1950)
|November 1, 1983
Summary
Human C-reactive protein (CRP) gene expression was studied to understand the acute phase response. Researchers found a larger primary translation product and a significantly larger mRNA, providing insights into eukaryotic gene control.
Area of Science:
- Molecular Biology
- Immunology
- Genetics
Background:
- Human C-reactive protein (CRP) is a key plasma protein marker elevated during inflammation and tissue injury.
- The significant (100-1000 fold) increase in CRP levels makes it a valuable model for studying eukaryotic gene regulation.
Purpose of the Study:
- To investigate the biosynthesis and post-translational processing of human CRP.
- To elucidate the molecular mechanisms controlling CRP gene expression during the acute phase response.
Main Methods:
- Cell-free protein synthesis systems.
- Xenopus oocyte microinjection with human liver mRNA.
- Nucleotide sequencing of a CRP-specific cDNA clone.
- Northern blot analysis to determine mRNA size.
Main Results:
- The primary translation product of human CRP is larger than mature serum CRP due to an 18-amino acid N-terminal signal peptide.
- Nucleotide sequencing identified the signal peptide sequence.
- Northern blot analysis revealed a CRP mRNA of approximately 2.2 Kb, substantially larger than the coding sequence requires.
Conclusions:
- The findings provide a foundation for studying the molecular regulation of the acute phase response.
- The presence of an extended signal peptide and a large mRNA suggest complex post-transcriptional or translational regulatory mechanisms for CRP production.