This gene encodes a cytosolic, NADP-dependent enzyme that generates NADPH for fatty acid biosynthesis. The activity of this enzyme, the reversible oxidative decarboxylation of malate, links the glycolytic and citric acid cycles. The regulation of expression for this gene is complex. Increased expression can result from elevated levels of thyroid hormones or by higher proportions of carbohydrates in the diet. [provided by RefSeq, Jul 2008] (from
... Rabbit polyclonal antibodies against c-Cbl, Cbl-b, EpoR, Jak2 (C-20 and M-126), and STAT5A as well as a mouse monoclonal antibody against α-tubulin were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA) ...
... the reaction was carried out for 20 minutes at room temperature.Afterwards, beads were washed with MES-T buffer using centrifugation at 600 G for 8 minutes on 3-µm Transwell inserts (Life Technologies) assembled on top of ...
Inui et al., Kyoto, Japan. In Appl Microbiol Biotechnol, 27 Apr 2015
Similarly, in phosphoenolpyruvate carboxylase gene (ppc)- or malate dehydrogenase gene (mdh)-deficient strains, overexpression of the ndh gene decreased the NADH/NAD(+) ratio from 1.66 to 0.37 and 2.20 to 0.57, respectively, whereas the glucose consumption rate increased by 57 and 330 %, respectively.
Weaver et al., Birmingham, United States. In Nat Immunol, 31 Mar 2015
By repressing expression of the negative regulator SOCS3 dependent on the transcription factor NF-κB, IL-1 increased the amplitude and duration of phosphorylation of the transcription factor STAT3 induced by TH17-polarizing cytokines, which led to an altered balance in the binding of STAT3 and STAT5 to shared consensus sequences in developing T cells.
Schraenen et al., Leuven, Belgium. In Cell Metab, Jan 2015
Locally secreted hGH binds to prolactin receptors on β cells, activates STAT5 signaling, and induces pregnancy-like changes in gene expression, thereby augmenting pancreatic β cell mass and insulin content.
Chiang et al., State College, United States. In Membranes (basel), 2013
When Saccharomyces cerevisiae is starved of glucose, the gluconeogenic enzymes fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase, isocitrate lyase, and malate dehydrogenase, as well as the non-gluconeogenic enzymes glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A, are secreted into the periplasm.