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. 1988 Jan;85(2):637–640. doi: 10.1073/pnas.85.2.637

Transferrin receptors in rat plasma.

Y Beguin 1, H A Huebers 1, B Josephson 1, C A Finch 1
PMCID: PMC279606  PMID: 3422446

Abstract

Antigenic material in rat plasma reacting with rat transferrin receptor antibodies was identified as an intact receptor molecule complexed with transferrin. Plasma transferrin receptors were measured by ELISA in rats of different age and sex, of different iron status, with different degrees of erythropoiesis, and with inflammation. An inverse relationship between iron status and receptor number was found, whereas a direct relationship existed between erythropoiesis and receptors. These changes in receptor number can be explained by assuming that the number of tissue receptors determined the number of plasma receptors and that the erythroid cells possessed most of the body's receptors. Increases in plasma receptors lagged behind the appearance of circulating reticulocytes, suggesting that receptors were released to the plasma during the terminal phase of erythrocyte maturation.

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Selected References

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

  1. Bauer W., Stray S., Huebers H., Finch C. The relationship between plasma iron and plasma iron turnover in the rat. Blood. 1981 Feb;57(2):239–242. [PubMed] [Google Scholar]
  2. Bergamaschi G., Eng M. J., Huebers H. A., Finch C. A. The effect of transferrin saturation on internal iron exchange. Proc Soc Exp Biol Med. 1986 Oct;183(1):66–73. doi: 10.3181/00379727-183-42387. [DOI] [PubMed] [Google Scholar]
  3. Conradie J. D., Mbhele B. E. Quantitation of serum ferritin by enzyme-linked immunosorbent assay (ELISA). S Afr Med J. 1980 Feb 23;57(8):282–287. [PubMed] [Google Scholar]
  4. Dautry-Varsat A., Ciechanover A., Lodish H. F. pH and the recycling of transferrin during receptor-mediated endocytosis. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2258–2262. doi: 10.1073/pnas.80.8.2258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Engvall E., Perlmann P. Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry. 1971 Sep;8(9):871–874. doi: 10.1016/0019-2791(71)90454-x. [DOI] [PubMed] [Google Scholar]
  6. Flowers C. A., Kuizon M., Beard J. L., Skikne B. S., Covell A. M., Cook J. D. A serum ferritin assay for prevalence studies of iron deficiency. Am J Hematol. 1986 Oct;23(2):141–151. doi: 10.1002/ajh.2830230209. [DOI] [PubMed] [Google Scholar]
  7. Hu H. Y., Aisen P. Molecular characteristics of the transferrin-receptor complex of the rabbit reticulocyte. J Supramol Struct. 1978;8(3):349–360. doi: 10.1002/jss.400080312. [DOI] [PubMed] [Google Scholar]
  8. Huebers H. A., Brittenham G. M., Csiba E., Finch C. A. Absorption of carbonyl iron. J Lab Clin Med. 1986 Nov;108(5):473–478. [PubMed] [Google Scholar]
  9. Huebers H. A., Csiba E., Huebers E., Finch C. A. Competitive advantage of diferric transferrin in delivering iron to reticulocytes. Proc Natl Acad Sci U S A. 1983 Jan;80(1):300–304. doi: 10.1073/pnas.80.1.300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Huebers H. A., Finch C. A. The physiology of transferrin and transferrin receptors. Physiol Rev. 1987 Apr;67(2):520–582. doi: 10.1152/physrev.1987.67.2.520. [DOI] [PubMed] [Google Scholar]
  11. Huebers H., Josephson B., Huebers E., Csiba E., Finch C. Uptake and release of iron from human transferrin. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2572–2576. doi: 10.1073/pnas.78.4.2572. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kohgo Y., Nishisato T., Kondo H., Tsushima N., Niitsu Y., Urushizaki I. Circulating transferrin receptor in human serum. Br J Haematol. 1986 Oct;64(2):277–281. doi: 10.1111/j.1365-2141.1986.tb04120.x. [DOI] [PubMed] [Google Scholar]
  13. Kohgo Y. Structure of transferrin and transferrin receptor. Nihon Ketsueki Gakkai Zasshi. 1986 Dec;49(8):1627–1634. [PubMed] [Google Scholar]
  14. Rao K. K., Shapiro D., Mattia E., Bridges K., Klausner R. Effects of alterations in cellular iron on biosynthesis of the transferrin receptor in K562 cells. Mol Cell Biol. 1985 Apr;5(4):595–600. doi: 10.1128/mcb.5.4.595. [DOI] [PMC free article] [PubMed] [Google Scholar]

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