High impact information on LDHA

• Tumor necrosis factor-alpha stimulates lactate dehydrogenase A expression in porcine cultured sertoli cells: mechanisms of action [1].
• The regulatory actions of the cytokine and the hormone on LDH A mRNA levels and therefore on lactate production may operate in the context of the metabolic cooperation between Sertoli and postmeiotic germ cells in the seminiferous tubules [1].
• The direct effect of TNFalpha on LDH A mRNA could not be accounted for by an increase in mRNA stability (half-life = 9 h), but was probably due to an increase in LDH A gene transcription [1].
• These observations suggest that the stimulatory effect of TNFalpha on LDH A mRNA expression requires protein synthesis and may involve a protein tyrosine kinase and protein kinase C. In addition, we report that LDH A mRNA levels were increased in Sertoli cells treated with FSH [1].
• Exogenous sphingosine stimulated LDH(A4) activity and LDHA expression in a dose-dependent manner (ED(50) = 8 microM of sphingosine) [2].

Biological context of LDHA

• The LDHA, PEPB and PGM1 genes were assigned to pig chromosomes nos 2, 5 and 6 respectively [3].
• Together, the present data suggest that in primary Sertoli cell cultures, TNFalpha stimulating action on LDHA expression is partly exerted via sphingomyelin hydrolysis pathway, sphingosine being the active metabolite [2].
• Eleven single nucleotide polymorphisms (SNPs) were identified in six of these genes (PRKAB1, GAA, PYGM, LDHA, PGAM2 and PKM2) [4].
• However, although the cytokine enhances LDH A mRNA levels through increased gene transcription, the hormone exerts its stimulatory action through an increase in LDH A mRNA stability [1].

Associations of LDHA with chemical compounds

• Sphingomyelinase, C2 ceramide, sphingosine 1-phosphate, N, N-dimethylsphingosine, and phosphorylcholine had no significant effect on LDHA expression/LDH(A4) activity [2].
• Epidermal growth factor regulates glucose metabolism through lactate dehydrogenase A messenger ribonucleic acid expression in cultured porcine Sertoli cells [5].

Other interactions of LDHA

• Tumor necrosis factor-alpha-stimulated lactate production is linked to lactate dehydrogenase A expression and activity increase in porcine cultured Sertoli cells [6].

Analytical, diagnostic and therapeutic context of LDHA

• Linkage mapping assigned PYGM and LDHA to porcine chromosome (SSC) 2, PKM2 to SSC7, GAA to SSC12, PRKAB1 to SSC14 and PGAM2 to SSC18 [4].

References