Lactoylglutathione lyase (GLO1)
The protein contains 184 amino acids for an estimated molecular weight of 20778 Da.
Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs17855424 | |
| dbSNP:rs4746 |
The reference OMIM entry for this protein is 138750
Glyoxalase i; glo1
DESCRIPTION
Glyoxalase I (EC 4.4.1.5) is a glutathione-binding protein involved in the detoxification of methylglyoxal, a byproduct of glycolysis. GLO1 and glyoxalase II (GLO2; 138760) catalyze successive steps in the pathway. GLO1 catalyzes condensation of methylglyoxal and reduced glutathione to form S-lactoyl-glutathione; GLO2 (hydroxyacyl glutathione hydrolase) converts the latter substance to D-lactic acid and reduced glutathione (Ranganathan et al., 1999).CLONING
Kim et al. (1993) isolated a cDNA corresponding to the GLO1 gene from a human monocyte cDNA library. The cDNA predicts a 184-amino acid protein with M(r) 20,719. Ranganathan et al. (1993) isolated a GLO1 cDNA from a human colon cDNA library. The human enzyme showed 42% amino acid homology with bacterial Glo1. Northern blot analysis identified a 2.2-kb mRNA transcript in colon tissue. There was a 12-fold increase of the GLO1 transcript in colon carcinoma tissue compared to normal colon tissue from the same patient, and the authors concluded that GLO1 gene expression was induced in colon carcinoma. Ranganathan et al. (1999) identified an insulin response element (IRE) and zinc metal response element (MRE) in the promoter region of the GLO1 gene.GENE STRUCTURE
Ranganathan et al. (1999) determined that the GLO1 gene contains 5 exons. Using bioinformatics, Gale and Grant (2004) found that the GLO1 gene contains 6 exons with evidence of possible alternative splicing.MAPPING
Reinsmoen et al. (1977) presented evidence from the family data that GLO is linked to HLA and that the order of loci on chromosome 6p is HLA-A, HLA-B, HLA-D, GLO, centromere. Meo et al. (1977) found that in the mouse glyoxalase I maps approximately 3 cM from the Ss locus, a component of the major histocompatibility complex, H-2. GLO1 has no known functional relationship to MHC. From study of a 3-generation family segregating for variation of the centromeric heterochromatic region of chromosome 6p11, Bakker et al. (1979) concluded that the HLA cluster and 6ph are about 6 cM apart (with peak lod score of 3.466), that GLO is on the centromeric side of HLA, that PGM3 (172100) is not on the short arm, and that HLA-B is closer to the centromere than HLA-A. Hansen and Eriksen (1979) found a maximum lod score of 14.6 at theta = 0.060 for linkage of HLA and GLO1. Goldman et al. (1991) confirmed the linkage by study of 2-dimensional electrophoresis in CEPH families. Blanche et al. (1991) presented a genetic map of 6p which involved RFLP mapping of the GLO1 locus.MOLECULAR GENETICS
Kompf et al. (1975) found that red cell GLO1 is polymorphic in man. Junaid et al. (2004) presented evidence suggesting that an ala111-to-glu polymorphism in the GLO1 gene (A111E; 138750.0001) may be a susceptibility factor for the development of autism (see 209850). This suggestion was not confirmed in studies by Rehnstrom et al. (2008) and Wu et al. (2008) in Finnish and Han Chinese populations, respectively.POPULATION GENETICS
Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988).ANIMAL MODEL
Chen et al. (2004) found that the Glo1 gene was upregulated approximately 1.6-fold in brain tissue of a transgenic mouse model of Alzheimer disease (AD; 104300) and frontotemporal dementia (600274). The transgenic mice carried the pro301-to-leu mutation in the tau gene (P301L; 157140.0001) and developed neurofibrillary tangles. GLO1 ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 138750 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed