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. 1991 Feb 1;173(2):495–498. doi: 10.1084/jem.173.2.495

Extrahepatic transcription of human C-reactive protein

PMCID: PMC2118780  PMID: 1988544

Abstract

We synthesized and cloned cDNA from human peripheral blood mononuclear cell (PBMC) transcripts that were hybrid selected by pCRP5, a liver C- reactive protein (CRP)-specific cDNA (Woo, P.,J.R. Korenberg, and A.S. Whitehead. 1985. J.Biol. Chem. 260:13384). Three hybrid-selected cDNA clones, HScDNA1, HScDNA3, and HScDNA8, were isolated and characterized. Nucleotide sequence analysis of the 5' end of the smaller clones, HScDNA1 and HScDNA8, demonstrated that these two PBMC clones are homologous to the 3' and 5' ends, respectively, of pCRP5. Our largest clone, HScDNA3, is larger than pCRP5, extending beyond both the 5' and 3' limits of pCRP5. Therefore, HScDNA3 was coded by human PBMC and not by the hybrid selection vehicle, pCRP5. HScDNA3 lacks the intervening sequence verifying that this clone is DNA made from a PBMC mRNA and not genomic DNA. The complete nucleotide sequence revealed that HScDNA3 is greater than 99% homologous to the CRP gene. These results demonstrate that PBMC express the CRP gene. Based on our previous report, which shows that peripheral blood cells synthesize a peptide recognized by anti-CRP (Kuta, A.E., and L.L. Baum. 1986. J. Exp. Med. 164:321), in conjunction with the data presented here, we conclude that human PBMC can synthesize CRP.

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Selected References

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  1. Baum L. L., James K. K., Glaviano R. R., Gewurz H. Possible role for C-reactive protein in the human natural killer cell response. J Exp Med. 1983 Jan 1;157(1):301–311. doi: 10.1084/jem.157.1.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  3. Goldman N. D., Liu T., Lei K. J. Structural analysis of the locus containing the human C-reactive protein gene and its related pseudogene. J Biol Chem. 1987 May 25;262(15):7001–7005. [PubMed] [Google Scholar]
  4. Ikuta T., Okubo H., Ishibashi H., Okumura Y., Hayashida K. Human lymphocytes synthesize C-reactive protein. Inflammation. 1986 Sep;10(3):223–232. doi: 10.1007/BF00916118. [DOI] [PubMed] [Google Scholar]
  5. Kushner I., Feldmann G. Control of the acute phase response. Demonstration of C-reactive protein synthesis and secretion by hepatocytes during acute inflammation in the rabbit. J Exp Med. 1978 Aug 1;148(2):466–477. doi: 10.1084/jem.148.2.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kuta A. E., Baum L. L. C-reactive protein is produced by a small number of normal human peripheral blood lymphocytes. J Exp Med. 1986 Jul 1;164(1):321–326. doi: 10.1084/jem.164.1.321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Samberg N. L., Bray R. A., Gewurz H., Landay A. L., Potempa L. A. Preferential expression of neo-CRP epitopes on the surface of human peripheral blood lymphocytes. Cell Immunol. 1988 Oct 1;116(1):86–98. doi: 10.1016/0008-8749(88)90212-2. [DOI] [PubMed] [Google Scholar]

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