Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1991 Sep 1;88(17):7505–7508. doi: 10.1073/pnas.88.17.7505

Differential tissue localization of oviduct and erythroid transferrin receptors.

H A Fuernkranz 1, J E Schwob 1, J J Lucas 1
PMCID: PMC52329  PMID: 1881888

Abstract

The tissue distributions of the estrogen-inducible hen oviduct transferrin receptor and the chicken embryonic erythrocyte transferrin receptor were studied. Tissue sections were investigated by immunofluorescence microscopy using specific polyclonal antisera against each receptor. The receptor originally identified and characterized in the oviduct strongly stained liver and ovary; localized staining was observed in the brain (especially endothelial cells). Staining of breast muscle and heart tissue occurred only in occasional interstitial cells. Antiserum against oviduct transferrin receptor did not stain erythrocytes, either from embryos or from mature animals. On the other hand, the antiserum directed against the embryonic erythrocyte receptor stained embryonic erythrocytes; it did not stain any other tissues. The fluorescence microscopy observations were confirmed by Western blot analysis. The strong staining of oviduct, liver, and ovary suggests a major role for the oviduct transferrin receptor in oogenesis.

Full text

PDF
7505

Images in this article

7506Image
on p.7506
7507Image
on p.7507
7507Image
on p.7507

Selected References

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

  1. DeRosa P. A., Lucas J. J. Estrogen-induced changes in chick oviduct membrane glycoproteins. J Biol Chem. 1982 Jan 25;257(2):1017–1024. [PubMed] [Google Scholar]
  2. Enns C. A., Sussman H. H. Similarities between the transferrin receptor proteins on human reticulocytes and human placentae. J Biol Chem. 1981 Dec 25;256(24):12620–12623. [PubMed] [Google Scholar]
  3. Espinosa de los Monteros A., Peña L. A., de Vellis J. Does transferrin have a special role in the nervous system? J Neurosci Res. 1989 Oct;24(2):125–136. doi: 10.1002/jnr.490240202. [DOI] [PubMed] [Google Scholar]
  4. Fishman J. B., Rubin J. B., Handrahan J. V., Connor J. R., Fine R. E. Receptor-mediated transcytosis of transferrin across the blood-brain barrier. J Neurosci Res. 1987;18(2):299–304. doi: 10.1002/jnr.490180206. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Jefferies W. A., Brandon M. R., Hunt S. V., Williams A. F., Gatter K. C., Mason D. Y. Transferrin receptor on endothelium of brain capillaries. Nature. 1984 Nov 8;312(5990):162–163. doi: 10.1038/312162a0. [DOI] [PubMed] [Google Scholar]
  7. Klausner R. D., Harford J. B. cis-trans models for post-transcriptional gene regulation. Science. 1989 Nov 17;246(4932):870–872. doi: 10.1126/science.2683086. [DOI] [PubMed] [Google Scholar]
  8. Kline K., Plante L. A., Morgan T. J., Jr, Sanders B. G. Chicken transferrin receptor expression during erythroid differentiation and by retrovirus transformed cells. Dev Comp Immunol. 1989 Summer;13(3):231–252. doi: 10.1016/0145-305x(89)90004-9. [DOI] [PubMed] [Google Scholar]
  9. Kühn L. C., McClelland A., Ruddle F. H. Gene transfer, expression, and molecular cloning of the human transferrin receptor gene. Cell. 1984 May;37(1):95–103. doi: 10.1016/0092-8674(84)90304-0. [DOI] [PubMed] [Google Scholar]
  10. Kühn L. C. The transferrin receptor: a key function in iron metabolism. Schweiz Med Wochenschr. 1989 Sep 30;119(39):1319–1326. [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Lee D. C., McKnight G. S., Palmiter R. D. The action of estrogen and progesterone on the expression of the transferrin gene. A comparison of the response in chick liver and oviduct. J Biol Chem. 1978 May 25;253(10):3494–3503. [PubMed] [Google Scholar]
  13. Lopez-Berjes M. A., Recio J. M., Planas J. Plasma variation of transferrin-iron and phosvitin-iron during the laying period in chicken hens. Poult Sci. 1981 Aug;60(8):1951–1956. doi: 10.3382/ps.0601951. [DOI] [PubMed] [Google Scholar]
  14. Mattia E., Rao K., Shapiro D. S., Sussman H. H., Klausner R. D. Biosynthetic regulation of the human transferrin receptor by desferrioxamine in K562 cells. J Biol Chem. 1984 Mar 10;259(5):2689–2692. [PubMed] [Google Scholar]
  15. May W. S., Jr, Cuatrecasas P. Transferrin receptor: its biological significance. J Membr Biol. 1985;88(3):205–215. doi: 10.1007/BF01871086. [DOI] [PubMed] [Google Scholar]
  16. Müllner E. W., Kühn L. C. A stem-loop in the 3' untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell. 1988 Jun 3;53(5):815–825. doi: 10.1016/0092-8674(88)90098-0. [DOI] [PubMed] [Google Scholar]
  17. Oh T. H., Markelonis G. J., Royal G. M., Bregman B. S. Immunocytochemical distribution of transferrin and its receptor in the developing chicken nervous system. Brain Res. 1986 Dec;395(2):207–220. doi: 10.1016/s0006-8993(86)80199-8. [DOI] [PubMed] [Google Scholar]
  18. Pardridge W. M., Eisenberg J., Yang J. Human blood-brain barrier transferrin receptor. Metabolism. 1987 Sep;36(9):892–895. doi: 10.1016/0026-0495(87)90099-0. [DOI] [PubMed] [Google Scholar]
  19. Poola I., Lucas J. J. Purification and characterization of an estrogen-inducible membrane glycoprotein. Evidence that it is a transferrin receptor. J Biol Chem. 1988 Dec 15;263(35):19137–19146. [PubMed] [Google Scholar]
  20. Poola I., Mason A. B., Lucas J. J. The chicken oviduct and embryonic red blood cell transferrin receptors are distinct molecules. Biochem Biophys Res Commun. 1990 Aug 31;171(1):26–32. doi: 10.1016/0006-291x(90)91351-r. [DOI] [PubMed] [Google Scholar]
  21. Roberts K. P., Griswold M. D. Characterization of rat transferrin receptor cDNA: the regulation of transferrin receptor mRNA in testes and in Sertoli cells in culture. Mol Endocrinol. 1990 Apr;4(4):531–542. doi: 10.1210/mend-4-4-531. [DOI] [PubMed] [Google Scholar]
  22. Schmidt J. A., Marshall J., Hayman M. J., Beug H. Primitive series embryonic chick erythrocytes express the transferrin receptor. Exp Cell Res. 1986 May;164(1):71–78. doi: 10.1016/0014-4827(86)90455-6. [DOI] [PubMed] [Google Scholar]
  23. Schmidt J. A., Marshall J., Hayman M. J. Identification and characterization of the chicken transferrin receptor. Biochem J. 1985 Dec 15;232(3):735–741. doi: 10.1042/bj2320735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Schneider C., Owen M. J., Banville D., Williams J. G. Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature. 1984 Oct 18;311(5987):675–678. doi: 10.1038/311675b0. [DOI] [PubMed] [Google Scholar]
  25. Schneider C., Williams J. G. Molecular dissection of the human transferrin receptor. J Cell Sci Suppl. 1985;3:139–149. doi: 10.1242/jcs.1985.supplement_3.14. [DOI] [PubMed] [Google Scholar]
  26. Stearne P. A., Pietersz G. A., Goding J. W. cDNA cloning of the murine transferrin receptor: sequence of trans-membrane and adjacent regions. J Immunol. 1985 May;134(5):3474–3479. [PubMed] [Google Scholar]
  27. Stein B. S., Sussman H. H. Peptide mapping of the human transferrin receptor in normal and transformed cells. J Biol Chem. 1983 Feb 25;258(4):2668–2673. [PubMed] [Google Scholar]
  28. Trowbridge I. S., Lesley J., Schulte R. Murine cell surface transferrin receptor: studies with an anti-receptor monoclonal antibody. J Cell Physiol. 1982 Sep;112(3):403–410. doi: 10.1002/jcp.1041120314. [DOI] [PubMed] [Google Scholar]
  29. Trowbridge I. S., Shackelford D. A. Structure and function of transferrin receptors and their relationship to cell growth. Biochem Soc Symp. 1986;51:117–129. [PubMed] [Google Scholar]
  30. Williams S. C., Woodworth R. C. The interaction of iron-conalbumin (anion) complexes with chick embryo red blood ccells. J Biol Chem. 1973 Aug 25;248(16):5848–5853. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES