Manduca sexta hemolymph ferritin: CDNA sequence and mRNA expression

Gene

Volumn 172, Issue 2, 1996, Pages 255-259

  Pham, Daphne Q D ^a   Zhang, Dianzheng ^a   Hufnagel, David H ^a   Winzerling, Joy J ^a  

^a University of Arizona   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; FERRITIN; MESSENGER RNA; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ARTICLE; HEMOLYMPH; IRON RESPONSIVE ELEMENT; LEPIDOPTERA; MIDGUT; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SYNTHESIS;

EID: 0029951578     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(96)00012-1     Document Type: Article

References (33)

1. Andrews, S.C., Arosio, P., Bottke, W., Briat, J.-F., von Darl, M., Harrison, P.M., Laulhere, H.-P., Levi, S., Lobreaux, S. and Yewdall, S.J.: Structure, function and evolution of ferritin. J. Inorg. Biochem. 47 (1992) 161-174.
2. Arosio, P., Pozone, A., Ferrero, R., Renoldi, I. and Levi, S.: Characteristics of ferritins in human milk secretions: similarities to serum and tissue isoferritins. Clin. Chim. Acta 161 (1986) 201-208.
3. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. Current Protocols in Molecular Biology. Greene Publishing Associates and Wiley-Interscience, John Wiley and Sons, New York, NY, 1987.
4. Barton, H.A., Eisenstein, R.S., Bonford, A. and Munro, H.N.: Determinants of the interaction between the iron-responsive element-binding protein and its binding site in rat L -ferritin mRNA. J. Biol. Chem. 265 (1990) 7000-7008.
5. Beattany, A.J.E., Eisenstein, R.S. and Munro, H.N.: Mutagenesis of the iron-regulatory element further defines a role for RNA secondary structure in the regulation of ferritin and transferrin receptor expression. J. Biol. Chem. 267 (1992) 16531-16537.
6. Benning, M.M., Smith, A.F., Wells, M.A. and Holden, H.M.: Crystallization, structure determination and least-squares refinement to 1.75 Å resolution of the fatty-acid-binding protein isolated from Manduca sexta L. J. Mol. Biol. 228 (1992) 208-219.
7. Cecil, R.L., Wyngarden, J.B. and Smith, L.H. Textbook of Medicine, 17th ed. Saunders, Philadelphia, PA, 1985.
8. Collin, O., Thomas, D., Flifla, M., Quintan, C. and Gouranton, J.: Characterization of a ferritin isolated from the midgut epithelial cell of a homopteran insect, Philaenus spumarius L. Biol. Cell 63 (1988) 297-305.
9. Cragg, S.J., Wagstaff, M. and Worwood, M.: Sialic acid and the microheterogeneity of human serum ferritin. Clin. Sci. 58 (1980) 259-262.
10. Drysdale, J.W.: Human ferritin gene expression. Prog. Nucleic Acid Res. Mol. Biol. 35 (1988) 127-155.
11. Dunkov, B.C., Zhang, D., Choumarov, K., Winzerling, J.J. and Law, J.H.: Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit. Arch. Insect Biochem. Physiol. 29 (1995) 293-307.
12. Harford, J.B. and Klausner, R.D.: Coordinate post-transcriptional regulation of ferritin and transferrin receptor expression: the role of regulated RNA-protein interaction. Enzyme 44 (1990) 28-41.
13. Huebers, H.A., Huebers, E., Finch, C.A., Webb, B.A., Truman, J.W. and Riddiford, L.M.: Iron binding proteins and their roles in the tobacco hornworm, Manduca sexta (L.). J. Comp. Physiol. B 158 (1988) 291-300.
14. Jaffrey, S.R., Haile, D.J., Klausner, R.D. and Harford, J.B.: The interaction between the iron-responsive element binding protein and its cognate RNA is highly dependent upon both RNA sequence and structure. Nucleic Acids Res. 21 (1993) 4627-4631.
15. Laemmli, U.K.: Most commonly used discontinuous buffer system for SDS electrophoresis. Nature 227 (1970) 680-685.
16. Law, J.H., Ribeiro, J.M.C. and Wells, M.A.: Biochemical insights derived from insect diversity. Annu. Rev. Biochem, 61 (1992) 87-111.
17. Lawson, D.M., Artymiuk, P.J., Yewdall, S.J., Smith, J.M.A., Livingstone, J.C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., Thomas, C.D., Shaw, W.V. and Harrison, P.M.: Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 349 (1991) 541-544.
18. Locke, M.: Apoferritin in the vacuolar system of insect hemocytes. Tissue Cell 23 (1991) 367-375.
19. Locke, M. and Leung, H.: The induction and distribution of an insect ferritin - a new function for the endoplasmic reticulum. Tissue Cell 16 (1984) 739-766.
20. Locke, M. and Nichols, H.: Iron economy in insects: transport, metabolism, and storage. Annu. Rev. Entomol. 37 (1992) 195-215.
21. Locke, M., Ketola-Pirie, C., Leung, H. and Nichol, H.: Vacuolar apoferritin synthesis by the fat body of an insect. J. Insect Physiol. 37 (1991) 297-309.
22. Mullner, E.W., Rothenberge, S., Muller, A.M. and Kühn, L.C.: In vivo and in vitro modulation of the mRNA-binding activity of iron-regulatory factor. Eur. J. Biochem. 208 (1992) 597-605.
23. Nichol, H. and Locke, M.: The characterization of ferritin in an insect. Insect Biochem. 19 (1989) 587-602.
24. Nichol, H. and Locke, M.: The localization of ferritin in insects. Tissue Cell 22 (1990) 767-777.
25. Pham, D.Q.-D. and Sivasubramanian, N.: In vivo transcriptional analysis of three baculovirus genes: evidence of homology between viral and host transcripts. Virology 190 (1992) 288-297.
26. Ponka, P., Schulman, H.M. and Woodworth, R.C.: Iron Transport and Storage. CRC Press, Boca Raton, FL, 1990.
27. Rothenberger, D., Mullner, E.W. and Kuhn, L.C.: The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution. Nucleic Acids Res. 18 (1990) 1175-1179.
28. Sussman, H.H.: Iron in cancer. Pathobiology 60 (1992) 2-9.
29. von Heijne, G.: Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133 (1983) 17-21.
30. von Heijne, G.: SIGPEP: a sequence database for secretory signal peptides. Protein Seq. Data Anal. 1 (1987) 41-42.
31. Waldo, G.S. and Theil, E.C.: Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin. Biochemistry 32 (1993) 13262-13269.
32. Waldo, G.S., Ling, J., Sanders-Loehr, J. and Theil, E.C.: Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin. Science 259 (1993) 796-798.
33. Winzerling, J.J., Nez, P., Porath, J. and Law, J.H.: Rapid and efficient isolation of transferrin and ferritin from Manduca sexta. Insect Biochem. Mol. Biol. 25 (1995) 217-224.