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The protein encoded by LDHA catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis.
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Results show that LDHA is highly expressed in triple negative breast cancer (TNBC) and correlated with a poor outcome. Its 3'UTR is targeted by miR (show MLXIP Proteins)-34a. Also, LDHA along with PDL1 (show CD274 Proteins) seem to act as ceRNAs to promote the expression and function of each other through regulation of miR (show MLXIP Proteins)-34a in TNBC.
LDHA siRNA can inhibit cell proliferation, induce apoptosis, reduce invasion and migration in renal cell carcinoma (show MOK Proteins) cells.
JMJD2A (show KDM4A Proteins) regulated aerobic glycolysis by regulating LDHA expression. Therefore, the novel JMJD2A (show KDM4A Proteins)-LDHA signaling pathway could contribute to the Warburg effects in NPC (show NPC1 Proteins) progression.
The present study proved that HIF1 (show HIF1A Proteins)/2alpha could activate LDHA expression in human pancreatic cancer cells, and high expression of LDHA promoted the growth and migration of pancreatic cancer cells.
Pretreatment LDH levels had noticeable prognostic value in advanced pancreatic ductal adenocarcinoma (PDAC) patients who received subsequent chemotherapy. Tackling elevated LDH levels before the initiation of chemotherapy might be a promising measure for improving overall survival of patients after treatment for their advanced PDAC.
Authors demonstrated that knock down of LDHA with siRNA or inhibition of LDHA activity with a LDHA specific inhibitor (FX-11), could sensitize PC-3RR cells to radiotherapy with reduced epithelial-mesenchymal transition, hypoxia, DNA repair ability and autophagy, as well as increased DNA double strand breaks and apoptosis.
Taken together, these results indicate that miR (show MLXIP Proteins)-142-3p could act as a tumor suppressor in HCC (show FAM126A Proteins) by targeting LDHA, suggesting new therapeutic targets for HCC (show FAM126A Proteins) treatment.
Findings suggest that miR (show MLXIP Proteins)-34b-3 and miR (show MLXIP Proteins)-449a suppress the development of nasopharyngeal carcinoma (NPC (show NPC1 Proteins)) through regulation of glycolysis via targeting lactate dehydrogenase A.(LDHA) and may be potential therapeutic targets for the treatment of NPC (show NPC1 Proteins).
Results provide evidence that miR (show MLXIP Proteins)-200b acts as a tumor suppressor in glioma through the inhibition of LDHA both in vitro and in vivo.
our data demonstrate that overexpression of 14-3-3zeta (show YWHAZ Proteins) in early stage pre-cancerous breast epithelial cells may trigger an elevated glycolysis and transcriptionally up-regulating LDHA, thereby contributes to human breast cancer initiation.
Dynamic changes of LDH and HBDH activities may be useful in diagnosis of non-thermal low voltage electrical injury and in estimation of post injury intervals.
Hair follicle stem cells maintain a metabolic state that allows them to remain dormant and yet quickly respond to appropriate proliferative stimuli mediated by LDH-A signaling.
Results revealed that beta-arrestin-1 (show ARRB1 Proteins) regulates lactate metabolism to contribute to beta2-adrenergic receptor (show ADRB2 Proteins) functions in improved memory formation.
The authors identified lactate dehydrogenase (LDH) as a new functional target of AMPKalpha1.
LDHA-associated lactic acid accumulation in melanomas inhibits tumor surveillance by T and natural killer cells.
lactate dehydrogenase A (LDHA) is induced in activated T cells to support aerobic glycolysis but promotes IFN-gamma (show IFNG Proteins) expression independently of its 3'UTR.
LDHA is a direct target of miR (show MLXIP Proteins)-34a in regulating glucose metabolism and tumor growth in breast cancer.
Findings suggest that RANKL protein-induced lactate dehydrogenase (LDH) activation stimulates glycolytic and mitochondrial respiratory metabolism via transcription factor NFATc1 signaling.
We propose a profibrotic feed forward loop, in which radiation induces LDHA expression and lactate production, which can lead to further activation of TGF-beta (show TGFB1 Proteins) to drive the fibrotic process.
High LDH-A expression is associated with metastases in breast tumors.
PGC-1alpha reduces the expression of LDH A and one of its regulators, the transcription factor myelocytomatosis oncogene (show MYC Proteins).
These findings indicated that heat shock (HS)-induced autophagy regulates lactate secretion by inhibiting apoptosis and increasing mRNA transcript and protein levels of SLC2A3 (show SLC2A3 Proteins), LDHA, and SLC16A1 (show SLC16A1 Proteins), which suggests that HS-induced autophagy may enhance lactate secretion by sertoli cells.
The NADH-cofactor binding site of pig heart LDH is involved in the interaction with acidic phospholipids, in the pig skeletal muscle LDH, neither the cofactor binding site nor the subunit interfacing areas seem to be involved in the interaction.
Both LDHA and COPB1 (show COPB1 Proteins) were highly expressed in porcine skeletal muscle tissues, implying their potential regulatory function of muscle development.
Molecular characterization and expression pattern of the equine lactate dehydrogenase A genes
The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. The protein is found predominantly in muscle tissue and belongs to the lactate dehydrogenase family. Mutations in this gene have been linked to exertional myoglobinuria. Multiple transcript variants encoding different isoforms have been found for this gene. The human genome contains several non-transcribed pseudogenes of this gene.
L-lactate dehydrogenase A chain
, LDH muscle subunit
, cell proliferation-inducing gene 19 protein
, lactate dehydrogenase M
, proliferation-inducing gene 19
, renal carcinoma antigen NY-REN-59
, lactate dehydrogenase-M
, lactate dehydrogenase A
, lactate dehydrogenase 1, A chain
, lactate dehydrogenase A4
, lactate dehydrogenase-A
, lactate dehydrogenase A-like
, lactate dehydrogenase A1
, lactate dehydrogenase C
, L-lactic acid dehydrogenase
, M(A)-type lactate dehydrogenase