Abstract
C reactive protein (CRP) increases up to 100 or 1000 fold during acute tissue injury, hence serum CRP measurements have been useful in clinical evaluation of inflammatory diseases. Since the molecular mechanisms that regulate the acute phase response are unknown, we undertook a study of the CRP gene and biosynthesis and postsynthetic processing of CRP protein. We have isolated a CRP specific human cDNA probe and used it to localize the gene to chromosome 1 (Science 221:69). CRP cDNA hybridized with poly A+ mRNA (2.2 Kb) that directs cell free translation of monomeric preCRP (26,000 Mr). PreCRP expressed antigenic determinants not detectable in the native plasma protein. When mRNA is translated in the presence of microsomes or in Xenopus oocytes, the 18 amino acid signal peptide of preCRP was cleaved, the monomer assembled to the pentameric form, characteristic of native serum CRP, and lost the antigenic determinant associated with the cell free translation product. Induction with turpentine of a acute phase response in rabbits demonstrated a dose dependent specific rise in CRP mRNA detected by Northern blot analysis and an increase in cell free pre-CRP synthesis. These data provide a model of molecular control of the acute phase response and regulation of other plasma proteins.
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Mantzouranis, E., Goldberger, G., Potempa, L. et al. BIOSYNTHESIS AND POSTSYNTHETIC ASSEMBLY OF HUMAN C REACTIVE PROTEIN (CRP). Pediatr Res 18 (Suppl 4), 260 (1984). https://doi.org/10.1203/00006450-198404001-01003
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DOI: https://doi.org/10.1203/00006450-198404001-01003