Lactate dehydrogenase A (LDHA) is an enzyme which in humans is encoded by the LDHAgene.[5] 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 tumors, 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.[6]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
Sudo K, Maekawa M, Shioya M, Ikeda K, Takahashi N, Isogai Y, Li SS, Kanno T, Machida K, Toriumi J (September 1992). "Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit". Biochemistry International. 27 (6): 1051–7.
PMID1445373.
Maekawa M, Sudo K, Li SS, Kanno T (October 1991). "Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining". Biochemical and Biophysical Research Communications. 180 (2): 1083–90.
doi:
10.1016/S0006-291X(05)81177-5.
PMID1953713.
Maekawa M, Sudo K, Li SS, Kanno T (November 1991). "Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification". Human Genetics. 88 (1): 34–8.
doi:
10.1007/BF00204925.
PMID1959923.
S2CID19321774.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Miyajima H, Takahashi Y, Suzuki M, Shimizu T, Kaneko E (July 1993). "Molecular characterization of gene expression in human lactate dehydrogenase-A deficiency". Neurology. 43 (7): 1414–9.
doi:
10.1212/wnl.43.7.1414.
PMID8327147.
S2CID41011165.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Sung JH, Shin SA, Park HK, Montelaro RC, Chong YH (October 2001). "Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells". Journal of NeuroVirology. 7 (5): 454–65.
doi:
10.1080/135502801753170318.
PMID11582518.
S2CID12958486.
Lactate dehydrogenase A (LDHA) is an enzyme which in humans is encoded by the LDHAgene.[5] 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 tumors, 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.[6]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
Sudo K, Maekawa M, Shioya M, Ikeda K, Takahashi N, Isogai Y, Li SS, Kanno T, Machida K, Toriumi J (September 1992). "Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit". Biochemistry International. 27 (6): 1051–7.
PMID1445373.
Maekawa M, Sudo K, Li SS, Kanno T (October 1991). "Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining". Biochemical and Biophysical Research Communications. 180 (2): 1083–90.
doi:
10.1016/S0006-291X(05)81177-5.
PMID1953713.
Maekawa M, Sudo K, Li SS, Kanno T (November 1991). "Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification". Human Genetics. 88 (1): 34–8.
doi:
10.1007/BF00204925.
PMID1959923.
S2CID19321774.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Miyajima H, Takahashi Y, Suzuki M, Shimizu T, Kaneko E (July 1993). "Molecular characterization of gene expression in human lactate dehydrogenase-A deficiency". Neurology. 43 (7): 1414–9.
doi:
10.1212/wnl.43.7.1414.
PMID8327147.
S2CID41011165.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Sung JH, Shin SA, Park HK, Montelaro RC, Chong YH (October 2001). "Protective effect of glutathione in HIV-1 lytic peptide 1-induced cell death in human neuronal cells". Journal of NeuroVirology. 7 (5): 454–65.
doi:
10.1080/135502801753170318.
PMID11582518.
S2CID12958486.