Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
권호 표지
DOI QR코드

DOI QR Code

Cloning and Characterization of the Putative Transferrin Receptor cDNA from the Olive Flounder (Paralichthys olivaceus)

  • Won Kyoung-Mi (Department of Aquatic Life Medicine, Pukyong National University) ;
  • Park Soo-Il (Department of Aquatic Life Medicine, Pukyong National University)
  • Published : 2003.06.01
Download PDF
⟨ Previous Next ⟩

Abstract

A cDNA clone for the olive flounder (Paralichthys olivaceus) transferrin receptor (fTfR) was isolated from a leukocytes cDNA library. The fTfR gene consisted of 2,319 bp encoding 773 amino acid residues. The amino acid sequence alignment of the fTfR showed that their size and hydrophobic profile are similar. In addition, the Tyr-Thr-Arg-Phe (YTRF) motif that is the recognition signal for high-efficiency endocytosis, is conserved very well. This motif is important for functional properties of TfR. The deduced amino acid sequence had $42.4-42.9\%$ identities with the previously reported TfRs of vertebrates. The fTfR was expressed in the blood, kidney, spleen, and liver of healthy olive flounder by the Northern blot hybridization.

Keywords

References

  1. Collawn, J.F., A. Lai, A. Domino, M. Fitch, S. Haton and I.S. Trowbridge. 1993. YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at postion 31-34 enhances endocytosis. J. Biol. Chem., 268, 21686-21692
  2. Gerhardt, E.M., L-N.L. Chan, S. Jing, M. Qi and I.S. Trowbridge. 1991. The cDNA sequence and primary structure of the chicken transferrin receptor. Gene 102, 249-254 https://doi.org/10.1016/0378-1119(91)90085-P
  3. Girones, N., E. Alvarez, A. Seth, I.M. Lin, D.A. Latour and R.J. Davis. 1991. Mutational analysis of the cytoplasmic tail of the human transferrin receptor. J. BioI. Chem. 266(28), 19006-19012
  4. Grego, B., I.R. Van Driel, P.A. Stearne, J.W. Goding, E.C. Nice and R.J. Simpson. 1985. A microbore high-performance liquid chromatography strategy for the purification of polypeptides for gas-phase sequence analysis. Structural studies on the murine transferrin receptor. Eur. J. Biochem. 148(3), 485-91 https://doi.org/10.1111/j.1432-1033.1985.tb08865.x
  5. Hirono, I., T. Uchiyama and T. Aoki. 1995. Cloning, nucleotide sequence analysis, and characterization of cDNA for medaka (Oryzias latipes) transferrin. J. Mar. Biotechnol, 2, 193-198
  6. Hoe, M.H. and R.C. Hunt. 1992. Loss of one asparaginelinked oligosaccharide from human transferrin receptors results in specific cleavage and association with the endoplasmic reticulum. J. BioI. Chem. 267, 4916-4929
  7. Iacopetta, B.J. and E.H. Morgan. 1983. The kinetics of transferrin endocytosis and iron uptake from transferrin in rabbit reticulocytes. J. BioI. Chem. 258, 9108-9115
  8. Jing, S. and I.S. Trowbridge. 1987. Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid attachment site. EMBO J. 6, 327-331
  9. Kenneth, P.R., D.G. Michael. 1990. Characterization of rat transferrin receptor cDNA: The regulation of transferrin receptor mRNA in testes and in sertoli cells in culture. Mol. Endo. 4(4), 531-542 https://doi.org/10.1210/mend-4-4-531
  10. Kim, Y.D., J.Y. Lee, Y.K. Hong, J. Hikima, I. Hirono and T. Aoki. 1997. Molecular cloning and sequence analysis of transferrin cDNA from Japanese flounder Paralichtys olivaceus. Fish. Sci. 63, 582-586 https://doi.org/10.2331/fishsci.63.582
  11. Lee, J.Y., T. Tada, I. Hirono and T. Aoki. 1998. Molecular coloning and evolution of transferrin cDNAs in salmonids. Mol. Mar. BioI. Biotechnol. 7(4), 287-293
  12. McClelland, A., L.C. Kuhn and F.H. Ruddle. 1984. The human transferring receptor gene: genomic organization and the complete primary structure of the receptor deduced from a cDNA sequence. Cell 39, 267-274 https://doi.org/10.1016/0092-8674(84)90004-7
  13. Nam B.H. , E. Yamamoto, I. Hirono and T. Aoki. 2000. A survey of expressed genes in the leukocytes of Japanese flounder, Paralichthys olivaceus, infected with Hirame rhadovirus. Dev. Comp. Immunol. 24(1), 13-24 https://doi.org/10.1016/S0145-305X(99)00058-0
  14. Sambrook, J., E.F. Fritsch and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
  15. Tadashi, S.O., H. Yasuko and O. Eijiro. 1986. Class specificity of transferring as a muscle trophic factor. J. Cell. Physiol. 126, 341-351 https://doi.org/10.1002/jcp.1041260304
  16. Testa, U., E. Pelosi and C. Peschle. 1993. The transferrin receptor. Crit. Rev. Oncogen. 4, 241-276
  17. Yang, B., M.H. Hoe, P. Black and R.C. Hunt. 1993. Role of oligosaccharides in the processing and function of human transferrin receptors: Effect of the loss of the three N-glycosyl oligo saccharides individually or together. J. BioI. Chem. 286, 7435-7441
  18. Young, S.P. and Aisen, P. 1981. Transferrin receptors and the uptake and release of iron by isolated hepatocytes. Hepatology 1, 114 https://doi.org/10.1002/hep.1840010205