High impact information on ImpL3

• Suppression of HPH in cultured Drosophila melanogaster cells by RNA interference resulted in elevated expression of a hypoxia-inducible gene (LDH, encoding lactate dehydrogenase) under normoxic conditions [1].
• IMP-L3, A 20-hydroxyecdysone-responsive gene encodes Drosophila lactate dehydrogenase: structural characterization and developmental studies [2].
• The predicted amino acid sequence of IMP-L3 is 58-61% identical to those of human LDHs [2].
• High levels of transcript and LDH activity persist throughout embryogenesis and throughout larval development [2].
• IMP-L3, a gene isolated as a potential mediator of imaginal disc morphogenesis in Drosophila melanogaster, encodes lactate dehydrogenase (LDH) [2].

Biological context of ImpL3

• In embryos, IMP-L3 transcript and LDH activity appear in developing somatic muscles by late stage 13, well before the onset of muscular contraction [2].
• Furthermore, exposure to agonists of ZE1-1 cells expressing the epsilon1/zeta1 NMDA receptor channel resulted in the release of lactate dehydrogenase (LDH) activity in the culture medium indicating agonist-induced cell death [3].
• Analogous preparations from pupae and adults exhibit three LDH-staining bands (one major and two minor) in a similar pattern [4].
• This fact indicates that the life-cycle stage-dependent LDH isozymic distribution is possibly due to a posttranslational effect(s) [4].

Anatomical context of ImpL3

• Incubation of isolated rat hepatocytes with BCA, in the dark, does not result in increased cell death as measured by leakage of cytosolic lactate dehydrogenase [5].
• Changes in the activity of 3 enzymes--lactate dehydrogenase (LDH), soluble malate dehydrogenase (sMDH), and pyruvate kinase (PK)--in homogenates of larval salivary glands of Drosophila melanogaster were studied before and after the induction of heat sensitive puffs with trinactin [6].

Associations of ImpL3 with chemical compounds

• Out of the nine electrophoretic zones of activity observed on polyacrylamide gel (or out of the six previously observed) using crude extract, only two (one major and one minor) belong to LDH, as revealed by purified enzyme preparations [7].
• Homogeneous LDH preparations exhibit one band on neutral acrylamide gels when the substrate is either DL-lactic acid or L-(+)-lactate [8].
• A UEP of 12 is approximately half that of lactate dehydrogenase and shows that aldehyde reductase is evolving at twice the rate of glycolytic enzymes [9].
• The appearance of a band in an assay using lactic acid as a substrate is not sufficient evidence for the presence of LDH [7].
• The activities of 2 enzymes (LDH and sMDH) were enhanced after puff induction, an effect that was abolished in the presence of cycloheximide [6].

Analytical, diagnostic and therapeutic context of ImpL3

• Highly purified LDH from larvae, pupae, or adults, obtained by an affinity chromatography procedure, displays just one dispersed band, located in the area between the band 5 and the band 6 exhibited by crude extract preparations [4].

References