The human glutaredoxin gene: Determination of its organization, transcription start point, and promoter analysis

Gene

Volumn 197, Issue 1-2, 1997, Pages 189-193

  Park, Jae B ^a   Levine, Mark ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Ascorbic acid; Dehydroascorbic acid; Thioltransferase

Indexed keywords

COMPLEMENTARY DNA; LUCIFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; NUCLEASE S1; TRANSCRIPTION FACTOR AP 2;

ARTICLE; CONTROLLED STUDY; FIBROBLAST; GENETIC ORGANIZATION; HUMAN; HUMAN CELL; INTRON; PRIORITY JOURNAL; PROMOTER REGION; START CODON; STOP CODON; TATA BOX;

EID: 0030799313     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00262-X     Document Type: Article

References (17)

1. Abate, C., Patel, L., Rauscher, F.J., Curran, T., 1990. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 249, 1157-1161.
2. Bjornsted, M., Xue, J., Huang, W., Akesson, B., Holmgren, A., 1994. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269, 29382-29384.
3. Bolle, P.A., Gilliquet, V., Berben, G., Dumont, J., Hilger, F., 1992. The complete sequence of K3B, a 7.9 kb fragment between PGK1 and CRY1 on chromosome III reveals the presence of seven open reading frames. Yeast 8, 205-213.
4. Buettner, G.R., Moseley, P.L., 1993. EPR spin trapping of free radicals produced by bleomycin and ascorbate . Free Radic. Res. Commun. (Suppl. 1) 19, 89-93.
5. Goswami, A., Rosenberg, I.N., 1985. Purification and characterization of a cytosolic protein enhancing glutathione-dependent microsomal iodothyronine 5′-monodeiodination. J. Biol. Chem. 260, 6012-6019.
6. Holmgren, A., 1976. Hydrogen donor system for E. coli ribonucleotide diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. USA 73, 2275-2279.
7. Holmgren, A., 1978. A thiol-dependent transhydrogenase from yeast. J. Biol. Chem. 253, 7424-7430.
8. Holmgren, A., 1989. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-13966.
9. Johnson, P.F., McKnight, S.L., 1989. Eukaryotic transcriptional regulatory proteins. Ann. Rev. Biochem. 58, 799-839.
10. Luthman, M., Eriksson, S., Holmgren, A., Thelander, L., 1979. Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase. Proc. Natl. Acad. Sci. USA 76, 2158-2162.
11. Park, J.B., Levine, M., 1996. Purification, cloning, and expression of dehydroascorbic acid reduction activity from human neutrophils: identification as glutaredoxin. Biochem. J. 315, 931-938.
12. Racker, E., 1955. Glutathione-homocystine transhydrogenase. J. Biol. Chem. 217, 867-874.
13. Rozell, B., Barcena, J.A., Martinez-Galistes, E., Padilla, C.A., Holmgren, A., 1993. Immunochemical characterization and tissue distribution of glutaredoxin (thioltransferase) from calf. Eur. J. Cell. Biol. 62, 314-324.
14. Washko, P.W., Wang, Y., Levine, M., 1993. Ascorbic acid recycling in human neutrophils. J. Biol. Chem. 268, 15531-15535.
15. Wells, W.W., Xu, D.P., Yang, Y., Rocque, P.A., 1990. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265, 15361-15364.
16. Wells, W.W., Yang, Y., Deits, T.L., Gan, Z., 1993. Thioltransferases. Adv. Enzymol. Relat. Areas. Mol. Biol. 66, 149-201.
17. Winkler, B.S., Orselli, S.M., Rex, T.S., 1994. The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective. Free Radic. Biol. Med. 17, 333-349.