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GLO1  -  glyoxalase I

Homo sapiens

Synonyms: Aldoketomutase, GLOD1, GLYI, Glx I, Glyoxalase I, ...
 
 
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Disease relevance of GLO1

  • Human lung cancer NCI-H522 and DMS114 cells, expressing higher GLO1 activity, underwent apoptosis when treated with BBGC, whereas A549 cells, expressing lower activity, did not [1].
  • Spinocerebellar ataxia (SCA1) in two large Italian kindreds: evidence in favour of a locus position distal to GLO1 and the HLA cluster [2].
  • The crystal structure of L. major GLO1 reveals differences in active site architecture to both human GLO1 and the nickel-dependent Escherichia coli GLO1, including increased negative charge and hydrophobic character and truncation of a loop that may regulate catalysis in the human enzyme [3].
  • Human myeloid leukemia cells become resistant to doxorubicin (DOX) treatment and this resistance is correlated with an increased glyoxalase 1 (GLO1) expression [4].
  • Glyoxalase I (GLO1) is a putative drug target for trypanosomatids, which are pathogenic protozoa that include the causative agents of leishmaniasis [5].
 

Psychiatry related information on GLO1

 

High impact information on GLO1

 

Chemical compound and disease context of GLO1

 

Biological context of GLO1

 

Anatomical context of GLO1

  • When overexpressed in human Jurkat cells, GLO1 inhibited etoposide- and adriamycin-induced caspase activation and apoptosis, indicating the involvement of GLO1 in apoptosis suppression caused by these drugs [13].
  • RESULTS: We found that GLO1 enzyme activity was higher in all of the 38 human cancer cell lines that we examined than in the normal tissue samples [1].
  • The results suggest possible linkage of red blood cell magnesium with the HLA locus and of red blood cell zinc with the GLO1 locus [17].
  • Transfection of COS-1 cells with the 622-base pair cDNA containing the entire coding region cloned into a pMT2 vector produced an immunoreactive protein and an approximate 180-fold increase in glyoxalase-I enzyme activity as determined with methylglyoxal as a substrate [18].
  • One hundred and ten pairs of blood and semen samples and their stains were studied to type glyoxalase 1 (GLO 1) isoenzymes using agarose-starch medium [19].
 

Associations of GLO1 with chemical compounds

  • The Gypsies deviate in the systems of GLO1, ACP1, ADA, C3, BF and HP from the Hungarians [20].
  • We found that glyoxalase I (GLO1), an enzyme that detoxifies methylglyoxal, is selectively overexpressed in the apoptosis-resistant UK711 cells [13].
  • The GLO1 enzyme activity was significantly elevated in UK711 and UK110 cells, another drug-resistant mutant, as well as in K562/ADM, adriamycin-resistant leukemia cells, compared with their parental cells [13].
  • The overall gene frequencies were as follows: Hp1, 0.21; Gc1F, 0.34; Gc1S, 0.36; Gc2, 0.30; TfC1, 0.66; TfC2, 0.26; TfC3, 0.001; TfD, 0.06; GLO1, 0.21; PGI2, 0.04; AK2, 0.01; PGM1+, 0.80; PGM1-, 0.06; PGM2+, 0.11 and PGM2-, 0.02 [21].
  • These differences correlate with the differential binding of glutathione and trypanothione-based substrates, and thus offer a route to the rational design of L. major-specific GLO1 inhibitors [3].
 

Other interactions of GLO1

  • The distribution of red cell enzymes showed Mongoloid characteristics with low PGDC, AK2, ESD1, GLO1, and higher pa [22].
  • The results also agree with those of most researchers in the importance of G6PD, FY, and MN as geographic markers and in the role of HP, GLO1, and Rh as indicators the Middle Eastern origin of the Jews but differ with respect to the geographic pattern of ABO [23].
  • Negative lodscores significantly excluded linkage with F13A at less than 5% and with GLO1 at less than 10% [2].
  • Blood and serum samples from random individuals of three populations in south India, the first being an endogamous group from the Nilgiri hills (Tamil Nadu), the second from the Shevroy hills (Tamil Nadu), and the third from a semi-urban area of Tamil Nadu, were screened for ESD, GLO1 and Hp polymorphisms [24].
  • The GLO1 gene was mapped further centromeric in the 6p21.2-6p21.1 region toward TCTE-1 [25].
 

Analytical, diagnostic and therapeutic context of GLO1

References

  1. Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells. Sakamoto, H., Mashima, T., Sato, S., Hashimoto, Y., Yamori, T., Tsuruo, T. Clin. Cancer Res. (2001) [Pubmed]
  2. Spinocerebellar ataxia (SCA1) in two large Italian kindreds: evidence in favour of a locus position distal to GLO1 and the HLA cluster. Frontali, M., Iodice, C., Lulli, P., Spadaro, M., Cappellacci, S., Giunti, P., Malaspina, P., Morellini, M., Morocutti, C., Novelletto, A. Ann. Hum. Genet. (1991) [Pubmed]
  3. Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme. Ariza, A., Vickers, T.J., Greig, N., Armour, K.A., Dixon, M.J., Eggleston, I.M., Fairlamb, A.H., Bond, C.S. Mol. Microbiol. (2006) [Pubmed]
  4. Troglitazone overcomes doxorubicin-resistance in resistant K562 leukemia cells. Davies, G.F., Roesler, W.J., Juurlink, B.H., Harkness, T.A. Leuk. Lymphoma (2005) [Pubmed]
  5. Crystallization and preliminary X-ray analysis of Leishmania major glyoxalase I. Ariza, A., Vickers, T.J., Greig, N., Fairlamb, A.H., Bond, C.S. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
  6. Association analysis of the functional Ala111Glu polymorphism of the glyoxalase I gene in panic disorder. Politi, P., Minoretti, P., Falcone, C., Martinelli, V., Emanuele, E. Neurosci. Lett. (2006) [Pubmed]
  7. Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. Shinohara, M., Thornalley, P.J., Giardino, I., Beisswenger, P., Thorpe, S.R., Onorato, J., Brownlee, M. J. Clin. Invest. (1998) [Pubmed]
  8. Extended MHC haplotypes in 21-hydroxylase-deficiency congenital adrenal hyperplasia: shared genotypes in unrelated patients. Fleischnick, E., Awdeh, Z.L., Raum, D., Granados, J., Alosco, S.M., Crigler, J.F., Gerald, P.S., Giles, C.M., Yunis, E.J., Alper, C.A. Lancet (1983) [Pubmed]
  9. Twenty-seven protein polymorphisms by two-dimensional electrophoresis of serum, erythrocytes, and fibroblasts in two pedigrees. Goldman, D., Goldin, L.R., Rathnagiri, P., O'Brien, S.J., Egeland, J.A., Merril, C.R. Am. J. Hum. Genet. (1985) [Pubmed]
  10. Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications. Vander Jagt, D.L., Hassebrook, R.K., Hunsaker, L.A., Brown, W.M., Royer, R.E. Chem. Biol. Interact. (2001) [Pubmed]
  11. Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase. Vander Jagt, D.L., Hunsaker, L.A. Chem. Biol. Interact. (2003) [Pubmed]
  12. Chromosomal assignments of 23 biochemical loci of the rat by using rat x mouse somatic cell hybrids. Yasue, M., Serikawa, T., Yamada, J. Cytogenet. Cell Genet. (1991) [Pubmed]
  13. Glyoxalase I is involved in resistance of human leukemia cells to antitumor agent-induced apoptosis. Sakamoto, H., Mashima, T., Kizaki, A., Dan, S., Hashimoto, Y., Naito, M., Tsuruo, T. Blood (2000) [Pubmed]
  14. Investigations on the polymorphism of glyoxalase I (EC 4.4.1.5) in the population of Hessen, Germany. Kühnl, P., Schwabenland, R., Spielmann, W. Hum. Genet. (1977) [Pubmed]
  15. An MHC (HLA-A, -B, C2, BF, HLA-DR, GLO1) haplotype study of 497 Danish normal families with 1970 children including 97 twin pairs. Nielsen, L.S., Eiberg, H., Fenger, K., Mohr, J. Tissue Antigens (1990) [Pubmed]
  16. Mapping SB in relation to HLA and GLO1 using cells from first-cousin marriage offspring. Termijtelen, A., Meera Khan, P., Shaw, S., van Rood, J.J. Immunogenetics (1983) [Pubmed]
  17. Possible linkage relationship between genetic markers and blood magnesium and zinc. A twin study. Darlu, P., Defrise-Gussenhoven, E., Michotte, Y., Susanne, C., Henrotte, J.G. Acta geneticae medicae et gemellologiae. (1985) [Pubmed]
  18. Cloning and characterization of human colon glyoxalase-I. Ranganathan, S., Walsh, E.S., Godwin, A.K., Tew, K.D. J. Biol. Chem. (1993) [Pubmed]
  19. Studies on glyoxalase 1 isoenzymes in semen stains: polymorphism in Himachal (India) population. Sharma, A., Arora, V.K., Bhalla, V. Forensic Sci. Int. (1988) [Pubmed]
  20. Genetic markers among three population groups of Hungary. Goedde, H.W., Benkmann, H.G., Kriese, L., Bogdanski, P., Czeizel, A., Bères, J. Gene geography : a computerized bulletin on human gene frequencies. (1987) [Pubmed]
  21. The distribution of some serum protein and red cell enzyme polymorphisms in the Koch ethnic group of West Bengal, India. Saha, N., Tay, J.S., Das, M.K., Das, K., Roy, M., Dey, B., Banerjee, S., Mukherjee, B.N. Jinrui Idengaku Zasshi (1990) [Pubmed]
  22. Blood genetic markers in the Chinese of two eastern provinces. Saha, N. Am. J. Phys. Anthropol. (1989) [Pubmed]
  23. Genetics of the Chuetas (Majorcan Jews): a comparative study. Picornell, A., Castro, J.A., Misericórdia Ramon, M. Hum. Biol. (1997) [Pubmed]
  24. Red cell enzymes and serum protein polymorphisms in three population groups of south India. Subramanian, V.S., Balakrishnan, K., Pitchappan, R.M., Sekharan, P.C., Damodaran, C. Gene geography : a computerized bulletin on human gene frequencies. (1994) [Pubmed]
  25. Physical map of human 6p21.2-6p21.3: region flanking the centromeric end of the major histocompatibility complex. Tripodis, N., Mason, R., Humphray, S.J., Davies, A.F., Herberg, J.A., Trowsdale, J., Nizetic, D., Senger, G., Ragoussis, J. Genome Res. (1998) [Pubmed]
  26. Extended haplotypes in rheumatoid arthritis and preliminary evidence for an interaction with immunoglobulin genes. Puttick, A., Briggs, D., Welsh, K., Jacoby, R., Williamson, E., Jones, V. Dis. Markers (1986) [Pubmed]
  27. Localization of the Chinese hamster MHC locus to chromosome 1q17-->q18 by fluorescence in situ hybridization. Rassool, F.V., Neilly, M.E., McGuire, K.L., McKeithan, T.W., Le Beau, M.M. Cytogenet. Cell Genet. (1995) [Pubmed]
  28. Identification of phosphoproteins regulated by gibberellin in rice leaf sheath. Khan, M.M., Jan, A., Karibe, H., Komatsu, S. Plant Mol. Biol. (2005) [Pubmed]
  29. Proteomic studies identified a single nucleotide polymorphism in glyoxalase I as autism susceptibility factor. Junaid, M.A., Kowal, D., Barua, M., Pullarkat, P.S., Sklower Brooks, S., Pullarkat, R.K. Am. J. Med. Genet. A (2004) [Pubmed]
 
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