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. 1990 Feb 15;266(1):283–290. doi: 10.1042/bj2660283

Mouse C-reactive protein. Generation of cDNA clones, structural analysis, and induction of mRNA during inflammation.

A S Whitehead 1, K Zahedi 1, M Rits 1, R F Mortensen 1, J M Lelias 1
PMCID: PMC1131125  PMID: 2310378

Abstract

A full-length C-reactive protein (CRP) cDNA clone has been isolated from a CBA/J-strain-mouse acute-phase liver library. The 1614-nucleotide cDNA specifies mRNA 5' and 3' untranslated regions of 81 and 858 bases respectively that flank 675 bases encoding mouse pre-CRP. The derived amino acid sequence predicts a 19-residue leader peptide followed by a 206-residue mature mouse CRP that shows considerable sequence identity with both human and rabbit CRP. Northern-blot analysis of mouse liver CRP mRNA concentrations after inflammatory stimuli and comparison with hepatic induction of mRNA for the major mouse acute-phase protein serum amyloid P component established that CRP, a major acute-phase reactant in human and rabbit, is a minor acute-phase reactant in mouse. The size and organization of the mouse CRP mRNA 5' and 3' untranslated regions are significantly different from those of human and rabbit CRP mRNA and may have implications for its anomalous minimal induction during acute inflammation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Auffray C., Rougeon F. Purification of mouse immunoglobulin heavy-chain messenger RNAs from total myeloma tumor RNA. Eur J Biochem. 1980 Jun;107(2):303–314. doi: 10.1111/j.1432-1033.1980.tb06030.x. [DOI] [PubMed] [Google Scholar]
  2. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Azorin F., Rich A. Isolation of Z-DNA binding proteins from SV40 minichromosomes: evidence for binding to the viral control region. Cell. 1985 Jun;41(2):365–374. doi: 10.1016/s0092-8674(85)80009-x. [DOI] [PubMed] [Google Scholar]
  4. Bodmer B., Siboo R. Isolation of mouse C-reactive protein from liver and serum. J Immunol. 1977 Mar;118(3):1086–1089. [PubMed] [Google Scholar]
  5. Caput D., Beutler B., Hartog K., Thayer R., Brown-Shimer S., Cerami A. Identification of a common nucleotide sequence in the 3'-untranslated region of mRNA molecules specifying inflammatory mediators. Proc Natl Acad Sci U S A. 1986 Mar;83(6):1670–1674. doi: 10.1073/pnas.83.6.1670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ciliberto G., Arcone R., Wagner E. F., Rüther U. Inducible and tissue-specific expression of human C-reactive protein in transgenic mice. EMBO J. 1987 Dec 20;6(13):4017–4022. doi: 10.1002/j.1460-2075.1987.tb02745.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Clewell D. B., Helinski D. R. Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an opern circular DNA form. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1159–1166. doi: 10.1073/pnas.62.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dowton S. B., Woods D. E., Mantzouranis E. C., Colten H. R. Syrian hamster female protein: analysis of female protein primary structure and gene expression. Science. 1985 Jun 7;228(4704):1206–1208. doi: 10.1126/science.2408337. [DOI] [PubMed] [Google Scholar]
  9. Floyd-Smith G., Whitehead A. S., Colten H. R., Francke U. The human C-reactive protein gene (CRP) and serum amyloid P component gene (APCS) are located on the proximal long arm of chromosome 1. Immunogenetics. 1986;24(3):171–176. doi: 10.1007/BF00364745. [DOI] [PubMed] [Google Scholar]
  10. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hu S. I., Miller S. M., Samols D. Cloning and characterization of the gene for rabbit C-reactive protein. Biochemistry. 1986 Dec 2;25(24):7834–7839. doi: 10.1021/bi00372a008. [DOI] [PubMed] [Google Scholar]
  12. Ishikawa N., Shigemoto K., Maruyama N. The complete nucleotide and deduced amino acid sequence of mouse serum amyloid P component. Nucleic Acids Res. 1987 Sep 11;15(17):7186–7186. doi: 10.1093/nar/15.17.7186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lei K. J., Liu T., Zon G., Soravia E., Liu T. Y., Goldman N. D. Genomic DNA sequence for human C-reactive protein. J Biol Chem. 1985 Oct 25;260(24):13377–13383. [PubMed] [Google Scholar]
  14. Mantzouranis E. C., Dowton S. B., Whitehead A. S., Edge M. D., Bruns G. A., Colten H. R. Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1. J Biol Chem. 1985 Jun 25;260(12):7752–7756. [PubMed] [Google Scholar]
  15. Mole J. E., Beaulieu B. L., Geheran C. A., Carnazza J. A., Anderson J. K. Isolation and analysis of murine serum amyloid P component cDNA clones. J Immunol. 1988 Nov 15;141(10):3642–3646. [PubMed] [Google Scholar]
  16. Mortensen R. F., Beisel K., Zeleznik N. J., Le P. T. Acute-phase reactants of mice. II. Strain dependence of serum amyloid P-component (SAP) levels and response to inflammation. J Immunol. 1983 Feb;130(2):885–889. [PubMed] [Google Scholar]
  17. Mortensen R. F., Le P. T., Taylor B. A. Mouse serum amyloid P-component (SAP) levels controlled by a locus on chromosome 1. Immunogenetics. 1985;22(4):367–375. doi: 10.1007/BF00430920. [DOI] [PubMed] [Google Scholar]
  18. Ohnishi S., Maeda S., Nishiguchi S., Arao T., Shimada K. Structure of the mouse C-reactive protein gene. Biochem Biophys Res Commun. 1988 Oct 31;156(2):814–822. doi: 10.1016/s0006-291x(88)80917-3. [DOI] [PubMed] [Google Scholar]
  19. Oliveira E. B., Gotschlich C., Liu T. Y. Primary structure of human C-reactive protein. J Biol Chem. 1979 Jan 25;254(2):489–502. [PubMed] [Google Scholar]
  20. Osmand A. P., Friedenson B., Gewurz H., Painter R. H., Hofmann T., Shelton E. Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins). Proc Natl Acad Sci U S A. 1977 Feb;74(2):739–743. doi: 10.1073/pnas.74.2.739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pelham H. R. A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell. 1982 Sep;30(2):517–528. doi: 10.1016/0092-8674(82)90249-5. [DOI] [PubMed] [Google Scholar]
  23. Pepys M. B., Baltz M., Gomer K., Davies A. J., Doenhoff M. Serum amyloid P-component is an acute-phase reactant in the mouse. Nature. 1979 Mar 15;278(5701):259–261. doi: 10.1038/278259a0. [DOI] [PubMed] [Google Scholar]
  24. Pinteric L., Assimeh S. N., Kells D. I., Painter R. H. The ultrastructure of C1t, a subcomponent of the first component of complement: an E.M. and ultracentrifuge study. J Immunol. 1976 Jul;117(1):79–83. [PubMed] [Google Scholar]
  25. Prelli F., Pras M., Frangione B. The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis. J Biol Chem. 1985 Oct 25;260(24):12895–12898. [PubMed] [Google Scholar]
  26. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Siboo R., Kulisek E. A fluorescent immunoassay for the quantification of C-reactive protein. J Immunol Methods. 1978;23(1-2):59–67. doi: 10.1016/0022-1759(78)90109-6. [DOI] [PubMed] [Google Scholar]
  28. Simon J. A., Sutton C. A., Lobell R. B., Glaser R. L., Lis J. T. Determinants of heat shock-induced chromosome puffing. Cell. 1985 Apr;40(4):805–817. doi: 10.1016/0092-8674(85)90340-x. [DOI] [PubMed] [Google Scholar]
  29. Tucci A., Goldberger G., Whitehead A. S., Kay R. M., Woods D. E., Colten H. R. Biosynthesis and postsynthetic processing of human C-reactive protein. J Immunol. 1983 Nov;131(5):2416–2419. [PubMed] [Google Scholar]
  30. Whitehead A. S., Rits M. Characterization of the gene encoding mouse serum amyloid P component. Comparison with genes encoding other pentraxins. Biochem J. 1989 Oct 1;263(1):25–31. doi: 10.1042/bj2630025. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Whitehead A. S., Rits M., Michaelson J. Molecular genetics of mouse serum amyloid P component (SAP): cloning and gene mapping. Immunogenetics. 1988;28(5):388–390. doi: 10.1007/BF00364241. [DOI] [PubMed] [Google Scholar]
  32. Woo P., Korenberg J. R., Whitehead A. S. Characterization of genomic and complementary DNA sequence of human C-reactive protein, and comparison with the complementary DNA sequence of serum amyloid P component. J Biol Chem. 1985 Oct 25;260(24):13384–13388. [PubMed] [Google Scholar]
  33. Zahedi K., Whitehead A. S. Acute phase induction of mouse serum amyloid P component. Correlation with other parameters of inflammation. J Immunol. 1989 Nov 1;143(9):2880–2886. [PubMed] [Google Scholar]

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