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. 1991 Mar;11(3):1448–1453. doi: 10.1128/mcb.11.3.1448

A transferrinlike (hemiferrin) mRNA is expressed in the germ cells of rat testis.

B J Stallard 1, M W Collard 1, M D Griswold 1
PMCID: PMC369422  PMID: 1996102

Abstract

In the testis, germ cells which are separated from the serum by the blood-testis barrier rely primarily on the Sertoli cell to obtain nutrients. For example, transferrin synthesized by the Sertoli cell is important in delivering iron from the serum to the developing germ cells. Because of its role in the testis, Sertoli cell transferrin protein and mRNA have been extensively studied. By using RNA blot analysis of rat testicular tissue, we detected a transcript of 2.6 kb which is attributed to transferrin. In addition, we detected a novel mRNA of 0.9 kb which had sequence similarity to the 3' end of transferrin. This 0.9-kb mRNA was present in germ cells, but not Sertoli cells, liver, or brain. The primary source of this mRNA in the testis was round spermatids. Sequence analysis of a cDNA clone showed that this mRNA encoded a protein with sequence similarity to the carboxy terminus of transferrin. Polysome analysis indicated that this transcript was translated and may therefore have importance in the iron metabolism of germ cells. The evolutionary implications between the transferrinlike mRNA germ cells and the gene duplication event which resulted in the diferric binding of transferrin are discussed.

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Selected References

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

  1. Aisen P., Listowsky I. Iron transport and storage proteins. Annu Rev Biochem. 1980;49:357–393. doi: 10.1146/annurev.bi.49.070180.002041. [DOI] [PubMed] [Google Scholar]
  2. Baldwin G. S., Weinstock J. Nucleotide sequence of porcine liver transferrin. Nucleic Acids Res. 1988 Sep 12;16(17):8720–8720. doi: 10.1093/nar/16.17.8720. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bellvé A. R., Cavicchia J. C., Millette C. F., O'Brien D. A., Bhatnagar Y. M., Dym M. Spermatogenic cells of the prepuberal mouse. Isolation and morphological characterization. J Cell Biol. 1977 Jul;74(1):68–85. doi: 10.1083/jcb.74.1.68. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cathala G., Savouret J. F., Mendez B., West B. L., Karin M., Martial J. A., Baxter J. D. A method for isolation of intact, translationally active ribonucleic acid. DNA. 1983;2(4):329–335. doi: 10.1089/dna.1983.2.329. [DOI] [PubMed] [Google Scholar]
  5. Chen L. H., Bissell M. J. Transferrin mRNA level in the mouse mammary gland is regulated by pregnancy and extracellular matrix. J Biol Chem. 1987 Dec 25;262(36):17247–17250. [PubMed] [Google Scholar]
  6. Cochet M., Gannon F., Hen R., Maroteaux L., Perrin F., Chambon P. Organization and sequence studies of the 17-piece chicken conalbumin gene. Nature. 1979 Dec 6;282(5739):567–574. doi: 10.1038/282567a0. [DOI] [PubMed] [Google Scholar]
  7. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dorrington J. H., Roller N. F., Fritz I. B. Effects of follicle-stimulating hormone on cultures of Sertoli cell preparations. Mol Cell Endocrinol. 1975 Jul;3(1):57–70. doi: 10.1016/0303-7207(75)90031-3. [DOI] [PubMed] [Google Scholar]
  9. Ehlers M. R., Fox E. A., Strydom D. J., Riordan J. F. Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7741–7745. doi: 10.1073/pnas.86.20.7741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Garrett J. E., Collard M. W., Douglass J. O. Translational control of germ cell-expressed mRNA imposed by alternative splicing: opioid peptide gene expression in rat testis. Mol Cell Biol. 1989 Oct;9(10):4381–4389. doi: 10.1128/mcb.9.10.4381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  12. Huggenvik J. I., Idzerda R. L., Haywood L., Lee D. C., McKnight G. S., Griswold M. D. Transferrin messenger ribonucleic acid: molecular cloning and hormonal regulation in rat Sertoli cells. Endocrinology. 1987 Jan;120(1):332–340. doi: 10.1210/endo-120-1-332. [DOI] [PubMed] [Google Scholar]
  13. Hugly S., Griswold M. Regulation of levels of specific Sertoli cell mRNAs by vitamin A. Dev Biol. 1987 Jun;121(2):316–324. doi: 10.1016/0012-1606(87)90167-9. [DOI] [PubMed] [Google Scholar]
  14. Kleene K. C., Distel R. J., Hecht N. B. Translational regulation and deadenylation of a protamine mRNA during spermiogenesis in the mouse. Dev Biol. 1984 Sep;105(1):71–79. doi: 10.1016/0012-1606(84)90262-8. [DOI] [PubMed] [Google Scholar]
  15. Kumar R. S., Kusari J., Roy S. N., Soffer R. L., Sen G. C. Structure of testicular angiotensin-converting enzyme. A segmental mosaic isozyme. J Biol Chem. 1989 Oct 5;264(28):16754–16758. [PubMed] [Google Scholar]
  16. Legrand D., Mazurier J., Montreuil J., Spik G. Structure and spatial conformation of the iron-binding sites of transferrins. Biochimie. 1988 Sep;70(9):1185–1195. doi: 10.1016/0300-9084(88)90184-8. [DOI] [PubMed] [Google Scholar]
  17. Russell L. D., Alger L. E., Nequin L. G. Hormonal control of pubertal spermatogenesis. Endocrinology. 1987 Apr;120(4):1615–1632. doi: 10.1210/endo-120-4-1615. [DOI] [PubMed] [Google Scholar]
  18. Skinner M. K., Griswold M. D. Sertoli cells synthesize and secrete transferrin-like protein. J Biol Chem. 1980 Oct 25;255(20):9523–9525. [PubMed] [Google Scholar]
  19. Uzan G., Frain M., Park I., Besmond C., Maessen G., Trépat J. S., Zakin M. M., Kahn A. Molecular cloning and sequence analysis of cDNA for human transferrin. Biochem Biophys Res Commun. 1984 Feb 29;119(1):273–281. doi: 10.1016/0006-291x(84)91648-6. [DOI] [PubMed] [Google Scholar]
  20. Wilson R. M., Griswold M. D. Secreted proteins from rat Sertoli cells. Exp Cell Res. 1979 Oct 1;123(1):127–135. doi: 10.1016/0014-4827(79)90429-4. [DOI] [PubMed] [Google Scholar]
  21. Yang F., Lum J. B., McGill J. R., Moore C. M., Naylor S. L., van Bragt P. H., Baldwin W. D., Bowman B. H. Human transferrin: cDNA characterization and chromosomal localization. Proc Natl Acad Sci U S A. 1984 May;81(9):2752–2756. doi: 10.1073/pnas.81.9.2752. [DOI] [PMC free article] [PubMed] [Google Scholar]

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