Abstract
Clearance from the plasma of 125I-labelled rabbit C-reactive protein (CRP) was significantly slower in animals undergoing an acute phase response (T1/2, mean +/- s.d., 6.48 +/- 1.4 h, n = 4) than in normal rabbits (3.17 +/- 0.4 h, n = 4), P less than 0.01. In contrast there was no difference between the rates of clearance of CRP in rabbits on a normal diet and hypercholesterolaemic rabbits, the plasma of which contained high levels of beta-VLDL with which CRP is known to form circulating complexes. Furthermore the apparent rates of clearance of 125I-labelled beta-VLDL, VLDL and LDL did not differ between normal rabbits and rabbits undergoing an acute phase response. The significance of these findings is discussed.
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Selected References
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- ANDERSON H. C., McCARTY M. The occurrence in the rabbit of an acute phase protein analogous to human C reactive protein. J Exp Med. 1951 Jan;93(1):25–36. doi: 10.1084/jem.93.1.25. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bilheimer D. W., Goldstein J. L., Grundy S. M., Brown M. S. Reduction in cholesterol and low density lipoprotein synthesis after portacaval shunt surgery in a patient with homozygous familial hypercholesterolemia. J Clin Invest. 1975 Dec;56(6):1420–1430. doi: 10.1172/JCI108223. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chelladurai M., Macintyre S. S., Kushner I. In vivo studies of serum C-reactive protein turnover in rabbits. J Clin Invest. 1983 Mar;71(3):604–610. doi: 10.1172/JCI110806. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coe J. E., Ross M. J. Hamster female protein. A divergent acute phase protein in male and female Syrian hamsters. J Exp Med. 1983 May 1;157(5):1421–1433. doi: 10.1084/jem.157.5.1421. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Beer F. C., Shine B., Pepys M. B. Radiometric ligand binding assay for C-reactive protein. Complexed C-reactive protein is not detectable in acute phase serum. Clin Exp Immunol. 1982 Oct;50(1):231–237. [PMC free article] [PubMed] [Google Scholar]
- Gotschlich E. C., Liu T. Y., Oliveira E. Binding of C-reactive protein to C-carbohydrate and PC-substituted protein. Ann N Y Acad Sci. 1982;389:163–171. doi: 10.1111/j.1749-6632.1982.tb22134.x. [DOI] [PubMed] [Google Scholar]
- HAVEL R. J., EDER H. A., BRAGDON J. H. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J Clin Invest. 1955 Sep;34(9):1345–1353. doi: 10.1172/JCI103182. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KUSHNER I., KAPLAN M. H. Studies of acute phase protein. I. An immunohistochemical method for the localization of Cx-reactive protein in rabbits. Association with necrosis in local inflammatory lesions. J Exp Med. 1961 Dec 1;114:961–974. doi: 10.1084/jem.114.6.961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KUSHNER I., RAKITA L., KAPLAN M. H. Studies of acute-phase protein. II. Localization of Cx-reactive protein in heart in induced myocardial infarction in rabbits. J Clin Invest. 1963 Feb;42:286–292. doi: 10.1172/JCI104715. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McFARLANE A. S. Efficient trace-labelling of proteins with iodine. Nature. 1958 Jul 5;182(4627):53–53. doi: 10.1038/182053a0. [DOI] [PubMed] [Google Scholar]
- Narkates A. J., Volanakis J. E. C-reactive protein binding specificities: artificial and natural phospholipid bilayers. Ann N Y Acad Sci. 1982;389:172–182. doi: 10.1111/j.1749-6632.1982.tb22135.x. [DOI] [PubMed] [Google Scholar]
- Pepys M. B., Baltz M. L. Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein. Adv Immunol. 1983;34:141–212. doi: 10.1016/s0065-2776(08)60379-x. [DOI] [PubMed] [Google Scholar]
- Rowe I. F., Soutar A. K., Trayner I. M., Baltz M. L., de Beer F. C., Walker L., Bowyer D., Herbert J., Feinstein A., Pepys M. B. Rabbit and rat C-reactive proteins bind apolipoprotein B-containing lipoproteins. J Exp Med. 1984 Feb 1;159(2):604–616. doi: 10.1084/jem.159.2.604. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Salacinski P. R., McLean C., Sykes J. E., Clement-Jones V. V., Lowry P. J. Iodination of proteins, glycoproteins, and peptides using a solid-phase oxidizing agent, 1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenyl glycoluril (Iodogen). Anal Biochem. 1981 Oct;117(1):136–146. doi: 10.1016/0003-2697(81)90703-x. [DOI] [PubMed] [Google Scholar]
- Volanakis J. E., Kaplan M. H. Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccharide. Proc Soc Exp Biol Med. 1971 Feb;136(2):612–614. doi: 10.3181/00379727-136-35323. [DOI] [PubMed] [Google Scholar]
- de Beer F. C., Soutar A. K., Baltz M. L., Trayner I. M., Feinstein A., Pepys M. B. Low density lipoprotein and very low density lipoprotein are selectively bound by aggregated C-reactive protein. J Exp Med. 1982 Jul 1;156(1):230–242. doi: 10.1084/jem.156.1.230. [DOI] [PMC free article] [PubMed] [Google Scholar]