Entry - *600443 - GLUTAREDOXIN; GLRX - OMIM
 
* 600443

GLUTAREDOXIN; GLRX


Alternative titles; symbols

GRX
THIOLTRANSFERASE


HGNC Approved Gene Symbol: GLRX

Cytogenetic location: 5q15     Genomic coordinates (GRCh38): 5:95,813,849-95,822,726 (from NCBI)


TEXT

Cloning and Expression

Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. Padilla et al. (1995) purified a human placental glutaredoxin to homogeneity and showed that its amino acid sequence was similar to that of other known mammalian glutaredoxins (about 80% identity), with some important differences. A cDNA that encodes the entire GRX open reading frame (ORF) and flanking sequences was isolated from a human spleen cDNA library. Glutaredoxin is a small protein of 12 kD.


Mapping

Using a genomic clone for fluorescence in situ hybridization, Padilla et al. (1996) mapped the GLRX gene to 5q14. This localization was in agreement with that arrived at by somatic cell hybrid analysis.


Gene Function

Raghavachari et al. (2001) investigated how the expression of thioltransferase (TTase), a critical thiol repair and dethiolating enzyme, is regulated in human lens epithelial cells under oxidative stress. They also examined whether depleting the primary cellular antioxidant glutathione in these cells has any influence on TTase expression under the same conditions. They found a transient increase in TTase mRNA after 5 minutes of H(2)O(2) treatment. Upregulation reached a maximum of 80% above normal by 10 minutes and gradually decreased as the cells detoxified the oxidant. They found that manipulation of cellular GSH resulted in minimal changes in TTase expression. When cells depleted of GSH were subjected to oxidative stress, TTase expression was also strongly upregulated. Raghavachari et al. (2001) concluded that the upregulation of TTase expression in lens epithelial cells could be an adaptive response of the cells to combat oxidative stress and restore the vital functions of lens proteins and enzymes. They found that such regulation was independent of cellular GSH concentration.


REFERENCES

  1. Padilla, C. A., Bajalica, S., Lagercrantz, J., Holmgren, A. The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14. Genomics 32: 455-457, 1996. [PubMed: 8838810, related citations] [Full Text]

  2. Padilla, C. A., Martinez-Galisteo, E., Barcena, J. A., Spyrou, G., Holmgren, A. Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Europ. J. Biochem. 227: 27-34, 1995. [PubMed: 7851394, related citations] [Full Text]

  3. Raghavachari, N., Krysan, K., Xing K., Lou, M. F. Regulation of thioltransferase expression in human lens epithelial cells. Invest. Ophthal. Vis. Sci. 42: 1002-1008, 2001. [PubMed: 11274078, related citations]


Contributors:
Jane Kelly - updated : 6/14/2001
Creation Date:
Victor A. McKusick : 3/7/1995
carol : 09/24/2008
mcapotos : 6/19/2001
mcapotos : 6/14/2001
jamie : 2/5/1997
mark : 3/28/1996
terry : 3/27/1996
carol : 3/8/1995
carol : 3/7/1995

* 600443

GLUTAREDOXIN; GLRX


Alternative titles; symbols

GRX
THIOLTRANSFERASE


HGNC Approved Gene Symbol: GLRX

Cytogenetic location: 5q15     Genomic coordinates (GRCh38): 5:95,813,849-95,822,726 (from NCBI)


TEXT

Cloning and Expression

Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. Padilla et al. (1995) purified a human placental glutaredoxin to homogeneity and showed that its amino acid sequence was similar to that of other known mammalian glutaredoxins (about 80% identity), with some important differences. A cDNA that encodes the entire GRX open reading frame (ORF) and flanking sequences was isolated from a human spleen cDNA library. Glutaredoxin is a small protein of 12 kD.


Mapping

Using a genomic clone for fluorescence in situ hybridization, Padilla et al. (1996) mapped the GLRX gene to 5q14. This localization was in agreement with that arrived at by somatic cell hybrid analysis.


Gene Function

Raghavachari et al. (2001) investigated how the expression of thioltransferase (TTase), a critical thiol repair and dethiolating enzyme, is regulated in human lens epithelial cells under oxidative stress. They also examined whether depleting the primary cellular antioxidant glutathione in these cells has any influence on TTase expression under the same conditions. They found a transient increase in TTase mRNA after 5 minutes of H(2)O(2) treatment. Upregulation reached a maximum of 80% above normal by 10 minutes and gradually decreased as the cells detoxified the oxidant. They found that manipulation of cellular GSH resulted in minimal changes in TTase expression. When cells depleted of GSH were subjected to oxidative stress, TTase expression was also strongly upregulated. Raghavachari et al. (2001) concluded that the upregulation of TTase expression in lens epithelial cells could be an adaptive response of the cells to combat oxidative stress and restore the vital functions of lens proteins and enzymes. They found that such regulation was independent of cellular GSH concentration.


REFERENCES

  1. Padilla, C. A., Bajalica, S., Lagercrantz, J., Holmgren, A. The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14. Genomics 32: 455-457, 1996. [PubMed: 8838810] [Full Text: https://doi.org/10.1006/geno.1996.0141]

  2. Padilla, C. A., Martinez-Galisteo, E., Barcena, J. A., Spyrou, G., Holmgren, A. Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Europ. J. Biochem. 227: 27-34, 1995. [PubMed: 7851394] [Full Text: https://doi.org/10.1111/j.1432-1033.1995.tb20356.x]

  3. Raghavachari, N., Krysan, K., Xing K., Lou, M. F. Regulation of thioltransferase expression in human lens epithelial cells. Invest. Ophthal. Vis. Sci. 42: 1002-1008, 2001. [PubMed: 11274078]


Contributors:
Jane Kelly - updated : 6/14/2001

Creation Date:
Victor A. McKusick : 3/7/1995

Edit History:
carol : 09/24/2008
mcapotos : 6/19/2001
mcapotos : 6/14/2001
jamie : 2/5/1997
mark : 3/28/1996
terry : 3/27/1996
carol : 3/8/1995
carol : 3/7/1995