Lactate dehydrogenase A: Difference between revisions

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* {{cite journal | vauthors = Maekawa M, Sudo K, Li SS, Kanno T | title = Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification | journal = Human Genetics | volume = 88 | issue = 1 | pages = 34–8 | date = November 1991 | pmid = 1959923 | doi = 10.1007/BF00204925 }}
* {{cite journal | vauthors = Maekawa M, Sudo K, Li SS, Kanno T | title = Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification | journal = Human Genetics | volume = 88 | issue = 1 | pages = 34–8 | date = November 1991 | pmid = 1959923 | doi = 10.1007/BF00204925 }}
* {{cite journal | vauthors = Scrable HJ, Johnson DK, Rinchik EM, Cavenee WK | title = Rhabdomyosarcoma-associated locus and MYOD1 are syntenic but separate loci on the short arm of human chromosome 11 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 6 | pages = 2182–6 | date = March 1990 | pmid = 2315312 | pmc = 53650 | doi = 10.1073/pnas.87.6.2182 | bibcode = 1990PNAS...87.2182S }}
* {{cite journal | vauthors = Scrable HJ, Johnson DK, Rinchik EM, Cavenee WK | title = Rhabdomyosarcoma-associated locus and MYOD1 are syntenic but separate loci on the short arm of human chromosome 11 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 6 | pages = 2182–6 | date = March 1990 | pmid = 2315312 | pmc = 53650 | doi = 10.1073/pnas.87.6.2182 | bibcode = 1990PNAS...87.2182S }}
* {{cite journal | vauthors = Maekawa M, Sudo K, Kanno T, Li SS | title = Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency | journal = Biochemical and Biophysical Research Communications | volume = 168 | issue = 2 | pages = 677–82 | date = April 1990 | pmid = 2334430 | doi = 10.1016/0006-291X(90)92374-9 }}
* {{cite journal | vauthors = Maekawa M, Sudo K, Kanno T, Li SS | title = Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency | journal = Biochemical and Biophysical Research Communications | volume = 168 | issue = 2 | pages = 677–82 | date = April 1990 | pmid = 2334430 | doi = 10.1016/0006-291X(90)92374-9 | url = https://zenodo.org/record/1253806 | type = Submitted manuscript }}
* {{cite journal | vauthors = Gosti F, Marty MC, Courvalin JC, Maunoury R, Bornens M | title = Centrosomal proteins and lactate dehydrogenase possess a common epitope in human cell lines | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 4 | pages = 1000–4 | date = February 1987 | pmid = 2434947 | pmc = 304349 | doi = 10.1073/pnas.84.4.1000 | bibcode = 1987PNAS...84.1000G }}
* {{cite journal | vauthors = Gosti F, Marty MC, Courvalin JC, Maunoury R, Bornens M | title = Centrosomal proteins and lactate dehydrogenase possess a common epitope in human cell lines | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 4 | pages = 1000–4 | date = February 1987 | pmid = 2434947 | pmc = 304349 | doi = 10.1073/pnas.84.4.1000 | bibcode = 1987PNAS...84.1000G }}
* {{cite journal | vauthors = Chung FZ, Tsujibo H, Bhattacharyya U, Sharief FS, Li SS | title = Genomic organization of human lactate dehydrogenase-A gene | journal = Biochemical Journal | volume = 231 | issue = 3 | pages = 537–41 | date = November 1985 | pmid = 3000353 | pmc = 1152784 | doi =  }}
* {{cite journal | vauthors = Chung FZ, Tsujibo H, Bhattacharyya U, Sharief FS, Li SS | title = Genomic organization of human lactate dehydrogenase-A gene | journal = Biochemical Journal | volume = 231 | issue = 3 | pages = 537–41 | date = November 1985 | pmid = 3000353 | pmc = 1152784 | doi =  }}
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* {{cite journal | vauthors = Vilà MR, Nicolás A, Morote J, de I, Meseguer A | title = Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction | journal = Cancer | volume = 89 | issue = 1 | pages = 152–64 | date = July 2000 | pmid = 10897012 | doi = 10.1002/1097-0142(20000701)89:1<152::AID-CNCR20>3.0.CO;2-T }}
* {{cite journal | vauthors = Vilà MR, Nicolás A, Morote J, de I, Meseguer A | title = Increased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction | journal = Cancer | volume = 89 | issue = 1 | pages = 152–64 | date = July 2000 | pmid = 10897012 | doi = 10.1002/1097-0142(20000701)89:1<152::AID-CNCR20>3.0.CO;2-T }}
* {{cite journal | vauthors = Boutet A, Altmeyer R, Héry C, Tardieu M | title = Direct role of plasma membrane-expressed gp120/41 in toxicity to human astrocytes induced by HIV-1-infected macrophages | journal = AIDS | volume = 14 | issue = 17 | pages = 2687–97 | date = December 2000 | pmid = 11125887 | doi = 10.1097/00002030-200012010-00008 }}
* {{cite journal | vauthors = Boutet A, Altmeyer R, Héry C, Tardieu M | title = Direct role of plasma membrane-expressed gp120/41 in toxicity to human astrocytes induced by HIV-1-infected macrophages | journal = AIDS | volume = 14 | issue = 17 | pages = 2687–97 | date = December 2000 | pmid = 11125887 | doi = 10.1097/00002030-200012010-00008 }}
* {{cite journal | vauthors = Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL | title = Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase | journal = Proteins | volume = 43 | issue = 2 | pages = 175–85 | date = May 2001 | pmid = 11276087 | doi = 10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-# | doi-broken-date = 2017-01-24 }}
* {{cite journal | vauthors = Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL | title = Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase | journal = Proteins | volume = 43 | issue = 2 | pages = 175–85 | date = May 2001 | pmid = 11276087 | doi = 10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-# }}
* {{cite journal | vauthors = Sung JH, Shin SA, Park HK, Montelaro RC, Chong YH | title = Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells | journal = Journal of NeuroVirology | volume = 7 | issue = 5 | pages = 454–65 | date = October 2001 | pmid = 11582518 | doi = 10.1080/135502801753170318 }}
* {{cite journal | vauthors = Sung JH, Shin SA, Park HK, Montelaro RC, Chong YH | title = Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells | journal = Journal of NeuroVirology | volume = 7 | issue = 5 | pages = 454–65 | date = October 2001 | pmid = 11582518 | doi = 10.1080/135502801753170318 }}
* {{cite journal | vauthors = Pioli PA, Hamilton BJ, Connolly JE, Brewer G, Rigby WF | title = Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1 | journal = Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35738–45 | date = September 2002 | pmid = 12107167 | doi = 10.1074/jbc.M204002200 }}
* {{cite journal | vauthors = Pioli PA, Hamilton BJ, Connolly JE, Brewer G, Rigby WF | title = Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1 | journal = Journal of Biological Chemistry | volume = 277 | issue = 38 | pages = 35738–45 | date = September 2002 | pmid = 12107167 | doi = 10.1074/jbc.M204002200 }}

Latest revision as of 12:59, 23 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
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RefSeq (mRNA)

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RefSeq (protein)

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PubMed searchn/an/a
Wikidata
View/Edit Human

Lactate dehydrogenase A (LDHA) is an enzyme which in humans is encoded by the LDHA gene.[1] It is a monomer of lactate dehydrogenase, which exists as a tetramer. The other main subunit is lactate dehydrogenase B (LDHB).

Function

Lactate dehydrogenase A catalyzes the inter-conversion of pyruvate and L-lactate with concomitant inter-conversion of NADH and NAD+. LDHA is found in most somatic tissues, though predominantly in muscle tissue and tumours, and belongs to the lactate dehydrogenase family. It has long been known that many human cancers have higher LDHA levels compared to normal tissues. It has also been shown that LDHA plays an important role in the development, invasion and metastasis of malignancies. Mutations in LDHA have been linked to exertional myoglobinuria.[2]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit]]
Glycolysis and Gluconeogenesis edit
  1. The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Model organisms

Model organisms have been used in the study of LDHA function. A conditional knockout mouse line, called Ldhatm1a(EUCOMM)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[12][13][14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty seven tests were carried out on mutant mice and five significant abnormalities were observed.[8] Few homozygous mutant embryos were identified during gestation, and none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice. Animals of both sex had abnormal plasma chemistry, males also had improved glucose tolerance and increased red blood cell distribution width.[8]

LDHA

The following compounds have been demonstrated to inhibit the LDHA enzyme:

References

  1. Chung FZ, Tsujibo H, Bhattacharyya U, Sharief FS, Li SS (November 1985). "Genomic organization of human lactate dehydrogenase-A gene". Biochemical Journal. 231 (3): 537–41. PMC 1152784. PMID 3000353.
  2. "Entrez Gene: LDHA lactate dehydrogenase A".
  3. "Glucose tolerance test data for Ldha". Wellcome Trust Sanger Institute.
  4. "Clinical chemistry data for Ldha". Wellcome Trust Sanger Institute.
  5. "Haematology data for Ldha". Wellcome Trust Sanger Institute.
  6. "Salmonella infection data for Ldha". Wellcome Trust Sanger Institute.
  7. "Citrobacter infection data for Ldha". Wellcome Trust Sanger Institute.
  8. 8.0 8.1 8.2 8.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  9. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  10. "International Knockout Mouse Consortium".
  11. "Mouse Genome Informatics".
  12. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  13. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  14. Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  15. van der Weyden L, White JK, Adams DJ, Logan DW (June 2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  16. Miskimins WK, Ahn HJ, Kim JY, Ryu S, Jung YS, Choi JY (2014). "Synergistic anti-cancer effect of phenformin and oxamate". PLoS One. 9 (1): e85576. Bibcode:2014PLoSO...985576M. doi:10.1371/journal.pone.0085576. PMC 3897486. PMID 24465604.
  17. Lu QY, Zhang L, Yee JK, Go VW, Lee WN (February 2015). "Metabolic Consequences of LDHA inhibition by Epigallocatechin Gallate and Oxamate in MIA PaCa-2 Pancreatic Cancer Cells". Metabolomics. 11 (1): 71–80. doi:10.1007/s11306-014-0672-8. PMC 4523095. PMID 26246802.
  18. Billiard J, Dennison JB, Briand J, Annan RS, Chai D, Colón M, Dodson CS, Gilbert SA, Greshock J, Jing J, Lu H, McSurdy-Freed JE, Orband-Miller LA, Mills GB, Quinn CJ, Schneck JL, Scott GF, Shaw AN, Waitt GM, Wooster RF, Duffy KJ (September 2013). "Quinoline 3-sulfonamides inhibit lactate dehydrogenase A and reverse aerobic glycolysis in cancer cells". Cancer & Metabolism. 1 (1): 19. doi:10.1186/2049-3002-1-19. PMC 4178217. PMID 24280423.

Further reading