Disease relevance of DLD1

• The present study was carried out to evaluate the effect of phagocytosis of killed yeast on the induction of apoptosis in two human solid tumors of the gastrointestinal (GI): the squamous cell carcinomas of the tongue (SCCA) are (SCC-4 and SCC-9) and the adenocarcinomas of the colon (ADENOCA) are (Caco-2 and DLD-1) [1].
• In the murine macrophage cell line RAW 264.7, in mouse peritoneal macrophages (MPM) and in human colorectal adenocarcinoma cells (DLD-1), iNOS activity could be induced with lipopolysaccharides and cytokines [2].

High impact information on DLD1

• While SW480, NP29, NP18 and HeLa cells did not enter mitosis in the presence of caffeine after HU treatment, in CaCo2, DLD1, HCT116 and HT29 caffeine abrogated the checkpoint response [3].
• However, when DLD-1 human colon carcinoma cells were transfected with antisense SAG, monolayer growth was significantly inhibited, as shown by a decreased number of stable colonies in the plate after normalization with transfection efficiency [4].
• Sequence analysis reveals that the human and mouse transcripts encode novel proteins that display strong similarities to the yeast D-lactate dehydrogenase proteins DLD1, AIP2, and YEL071W [5].
• Immunofluorescence subcellular localization of the mouse DLD protein indicates that it resides within mitochondria, a feature shared by many dehydrogenases [5].
• This gene (DLD1) was found to be subject to several regulatory controls at the transcriptional level: synthesis of DLD1 mRNA is repressed by glucose, is derepressed in ethanol or lactate and is heme dependent [6].

Associations of DLD1 with chemical compounds

• These results are discussed together with the role of L-LCR and D-LCR in lactate metabolism of S. cerevisiae [7].
• The DLD gene was cloned by complementation for growth on D-, L-lactate in the strain WWF18-3D, carrying both a CYB2 disruption and the dld mutation [7].
• Expression of the Kluyveromyces lactis KlDLD gene, encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase (D-LCR), is subject to two metabolic controls at the transcriptional level: induction by lactate, the substrate of the D-LCR enzyme, and repression by glucose [8].
• The concentration of itraconazole, ketoconazole or miconazole needed to inhibit iNOS activity by 50% in RAW 264.7 cells, MPM and DLD-1 cells was > or = 10 mumol l-1 [2].

Other interactions of DLD1

• Using this screen, we have identified a previously uncharacterized gene, YEL071w, predicted to encode a protein of 496 amino acids that shares 80% homology and 60% sequence identity with actin interacting protein 2, encoded by the AIP2 gene; both proteins also share sequence similarity to aD-lactate dehydrogenase encoded by the DLD1 gene [9].

References