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

• The zinc metalloenzyme glyoxalase I (GLO1) is thought to play a role in anxiety disorders because a reduced brain expression of GLO1 has been associated with increased anxiety-behaviours in mice [6].

High impact information on GLO1

• Glyoxalase-I catalyzes the conversion of MG to S-D-lactoylglutathione, which in turn is converted to D-lactate by glyoxalase-II [7].
• Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis [7].
• Overexpression of glyoxalase-I completely prevented both hyperglycemia-induced AGE formation and increased macromolecular endocytosis [7].
• The haplotype containing this rare set of complement alleles always carried the rare HLA allele, HLA-Bw47, usually carried HLA-A3, and almost always had the alleles HLA-Cw6, HLA-DR7, and the glyoxalase I (GLO) allele GLO1 [8].
• Two allozyme polymorphisms, glyoxalase-1 (GLO1) and phosphoglucomutase-3 (PGM3) were specifically identified here based on genotypic concordance and molecular mass [9].

Chemical compound and disease context of GLO1

• Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications [10].
• Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase [11].

Biological context of GLO1

• In addition, ACP1 and GLO1 were reassigned to rat chromosomes 6 and 20, respectively [12].
• Moreover, cotreatment with S-p-bromobenzylglutathione cyclopentyl diester (BBGC), a cell-permeable inhibitor of GLO1, enhanced etoposide-induced apoptosis in resistant UK711 cells but not in parental U937 cells [13].
• The gene frequencies in 1150 unrelated individuals were 0.4391 for GLO1 and 0.5609 fro GLO2 [14].
• An MHC (HLA-A, -B, C2, BF, HLA-DR, GLO1) haplotype study of 497 Danish normal families with 1970 children including 97 twin pairs [15].
• Recombinations were identified which mapped SB between HLA-B and GLO1 [16].

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

• One haplotype only, HLA-Bw62 BfS C4A*3 C4B*3 DR4 GLO2, was significantly increased in the patient group, whereas HLA-B7 BfS C4A*3 C4B*1 DR2 GLO1, which was the most common haplotype in the control groups, was absent [26].
• Comparative gene mapping analysis in mammals suggests that the major histocompatibility complex (MHC) genes map syntenic with genes, such as glyoxylase 1 (GLO1) [27].
• Examination of colon carcinomas for the amplification of the glyoxalase-I gene by Southern blot analysis revealed no change in gene copy number [18].
• The abundance of glyoxalase-I and cytoplasmic malate dehydrogenase remained unchanged by GA3 treatment as detected on 2D-gel by silver staining, unlike for glyceraldehydes-3-phosphate dehydrogenase [28].
• In four of eight autism brains, we have found an increase in polarity (more acidic) of glyoxalase I (Glo1) by two-dimensional gel electrophoresis [29].

References