Rat muscle fructose-1,6-bisphosphatase: Cloning of the cDNA, expression of the recombinant enzyme, and expression analysis in different tissues

Biological Chemistry

Volumn 380, Issue 9, 1999, Pages 1079-1085

  Al Robaiy, Samiya ^a   Eschrich, Klaus ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

Gluconeogenesis; Isoenzyme; Quantitative PCR

Indexed keywords

COMPLEMENTARY DNA; FRUCTOSE BISPHOSPHATASE; LIVER ENZYME; MESSENGER RNA; RECOMBINANT ENZYME;

ANIMAL TISSUE; ARTICLE; EXPRESSION VECTOR; MOLECULAR CLONING; MUSCLE; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; WESTERN BLOTTING;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ESCHERICHIA COLI; FRUCTOSE-BISPHOSPHATASE; MOLECULAR SEQUENCE DATA; MUSCLES; PHYLOGENY; RATS; RECOMBINANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA; EUKARYOTA; RODENTIA;

EID: 0032842869     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.134     Document Type: Article

References (35)

1. Becker-André, M., and Hahlbrock, K. (1989). Absolute mRNA quantification using the polymerase chain reaction (PCR). A novel approach by a PCR aided transcript titration assay (PATTY). Nucleic Acids Res. 17, 9437-9446.
2. Black, W.J., Van Tol, A., Fernando, J., and Horecker, B.L. (1972). Isolation of highly active fructose diphosphatase from rabbit muscle: its subunit structure and activation by monovalent cations. Arch. Biochem. Biophys. 151, 576-590.
3. Bradford, M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
4. Challiss, R.A., Arch, J.R., and Newsholme, E.A. (1984). The rate of substrate cycling between fructose 6-phosphate and fructose 1,6-bisphosphate in skeletal muscle. Biochem. J. 221, 153-161.
5. Chatterjee, T., Rittenhouse, J., and Marcus, F. (1984). Identification of the in vivo and in vitro phosphorylation sites of rat liver fructose-1,6-bisphosphatase. J. Biol. Chem. 259, 3831-3833.
6. Cloix, J.-F., Beaulieu, E., and Hevor, T. (1997). Various fructose-1,6-bisphosphatase mRNAs in mouse brain, liver, kidney and heart. Neuroreport 8, 617-622.
7. El-Maghrabi, M.R., Pilkis, J., Marker, A.J., Colosia, A.D., D'Angelo, G., Fraser, B.A., and Pilkis, S.J. (1988). cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin. Proc. Natl. Acad. Sci. USA 85, 8430-8434.
8. El-Maghrabi, M.R., Lange, A.J., Kümmel, L., and Pilkis, S.J. (1991). The rat fructose-1,6-bisphosphatase gene. Structure and regulation of expression. J. Biol. Chem. 266, 2115-2120.
9. El-Maghrabi, M.R., Gidh-Jain, M., Austin, L.R., and Pilkis, S.J. (1993). Isolation of human fructose-1,6-bisphosphatase cDNA and expression of the protein in Escherichia coli. J. Biol. Chem. 668, 9466-9472.
10. Enser, M., Shapiro, S., and Horecker, B.L. (1969). Immunological studies of liver, kidney, and muscle fructose-1,6-diphosphatases. Arch. Biochem. Biophys. 129, 377-383.
11. Felsenstein, J. (1988). Phylogenies from molecular sequences: inference and reliability. Ann. Rev. Genet. 22, 521-565.
12. Fernando, J., Enser, M., Pontremoli, S., and Horecker, B.L. (1968). Purification and properties of rabbit muscle fructose-1,6-diphosphatase. Arch. Biochem. Biophys. 126, 599-606.
13. Gaesser, G.A., and Brooks, G.A. (1984). Metabolic basis of excess post-exercise oxygen consumption: a review. Med. Sci Sports Exerc. 16, 29-43.
14. Gleeson, T.T. (1996). Post-exercise lactate metabolism: a comparative review of sites, pathways, and regulation. Annu. Rev. Physiol. 58, 565-581.
15. Gidh-Jain, M., Zhang, Y., van Poelje, P.D., Liang, J.-Y., Huang, S., Kim, J., Elliott, J.T., Erion, M.D., Pilkis, S.J., El-Maghrabi, M.R., and Lipscomb, W.N. (1994). The allosteric site of human liver fructose-1,6-bisphosphatase. J. Biol. Chem. 269, 27732-27738.
16. Giroux, E., Williams, M.K., and Kantrowitz, E.R. (1994). Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition. J. Biol. Chem. 269, 31404-31409.
17. Ke, H., Zhang, Y., and Lipscomb, W.N. (1990). Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. Proc. Natl. Acad. Sci. USA 87, 5243-5247.
18. Kikawa, Y., Inuzuka, M., Takano, T., Shigematsu, Y., Nakai, A., Yamamoto, Y., Jin, B.Y., Koga, J., Taketo, A., and Sudo, M. (1994). cDNA sequences encoding human fructose-1,6-bisphosphatase from monocytes, liver and kidney: application of monocytes to molecular analysis of human fructose-1,6-bisphosphatase deficiency. Biochem. Biophys. Res. Commun. 199, 687-693.
19. Kimura, M. (1983). The neutral theory of molecular evolution (Cambridge, U.K.: Cambridge University Press).
20. Liu, F., and Fromm, H.J. (1988). Purification and characterization of fructose-1,6-bisphosphatase from bovine brain. Arch. Biochem. Biophys. 260, 609-615.
21. Majumder, A.L., and Eisenberg, F. (1977). Unequivocal demonstration of fructose-1,6-bisphosphatase in mammalian brain. Proc. Natl. Acad. Sci. USA 74, 3222-3225.
22. Meek, D.W., and Nimmo, H.G. (1983). The interaction of fructose 2,6-bisphosphate with an allosteric site of rat liver fructose-1,6-bisphosphatase. FEBS Lett. 160, 105-109.
23. 2+ on fructose 2,6-bisphosphate inhibition of mouse liver, intestinal, and muscle fructose-1,6-bisphosphatase. Arch. Biochem. Biophys. 226, 257-264.
24. Mizunuma, H., and Tashima, Y. (1986). Characterization of rat muscle fructose-1,6-bisphosphatase. J. Biochem. 99, 1781-1788.
25. Mizunuma, H., and Tashima, Y. (1990). Survey of fructose-1,6-bisphosphatase isoenzyme in rat organs and ontogenic expression of the enzyme in rat fetus. Int. J. Biochem. 22, 883-887.
26. Nikolovski, S., Faulkner, D.L., Palmer, T.N., and Fournier, P.A. (1996). Muscle glycogen repletion from endogenous carbon sources during recovery from high intensity exercise in the fasted rat. Acta Physiol. Scand. 157, 427-434.
27. Rittenhouse, J., Chatterjee, T., and Marcus, F. (1983). Amino acid sequence of the COOH-terminal region of fructose-1,6-bisphosphatase in relation to cyclic AMP-dependent phosphorylation. J. Biol. Chem. 258, 7648-7652.
28. Saitou, N., and Nei, M. (1987). The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425.
29. Sanger, F., Nicklen, S., and Coulson, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
30. Serth, J., Panitz, F., Hermann, H., and Alves, J. (1998). Single tube nested competitive PCR with homologous competitor for quantitation of DNA target sequences: theoretical description of heteroduplex formation, evaluation of sensitivity, precision and linear range of the method. Nucleic Acids Res. 26, 4401-4408.
31. Skalecki, K., Mularczyk, W., and Dzugaj, A. (1995). Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle. Biochem. J. 310, 1029-1035.
32. Tejwani, G.A., Pedrosa, F.O., Pontremoli, S., and Horecker, B.L. (1976). The purification and properties of rat liver fructose-1,6-bisphosphatase. Arch. Biochem. Biophys. 177, 255-264.
33. Tillmann, H., and Eschrich, K. (1998). Isolation and characterization of an allelic cDNA for human muscle fructose-1,6-bisphosphatase, Gene 212, 295-304.
34. Tonder, A.V., Terblanche, S.E., and Oelofsen, W. (1985). Isolation and partial characterization of rat muscle fructose bisposphatase. Biochim. Biophys. Acta 831, 186-191.
35. Van de Peer, Y., and De Wachter, R. (1994). TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment. Comput. Applic. Biosci. 10, 569-570.