Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mammalian phospholipase D (PLD) has been implicated in the cellular signal transduction pathways leading to diverse physiological events and known to be regulated by many cellular factors. To identify the proteins that interact with PLD, we performed a protein overlay assay with fractions obtained from the sequential column chromatographic separation of rat brain cytosol using purified PLD2 as a probe. A protein of molecular mass 40 kDa, which was detected by anti-PLD antibody with overlaying of the purified PLD2, is shown to be aldolase C by peptide-mass fingerprinting with matrix-assisted laser desorption/ionization-time-of flight mass spectrometry (MALDI-TOF-MS). Aldolase A also showed similar binding properties as aldolase C and was co-immunoprecipitated with PLD2 in COS-7 cells overexpressing PLD2 and aldolase A. The PH domain corresponding to amino acids 201-310 of PLD2 was necessary for the interaction observed in vitro, and aldolase A was found to interact with the PH domain of PLD2 specifically, but not with other PH domains. PLD2 activity was inhibited by the presence of purified aldolase A in a dose-dependent manner, and the inhibition by 50% was observed by the addition of less than micromolar aldolase A. Moreover, the inclusion of the aldolase metabolites fructose 1,6-bisphosphate (F-1,6-P) or glyceraldehyde 3-phosphate (G-3-P) resulted in an enhanced interaction between PLD2 and aldolase A with a concomitant increase in the potential ability of aldolase A to inhibit PLD2, which suggests the existence of a possible regulation of the interaction by the change of intracellular concentrations of glycolytic metabolites.
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PMID:Phospholipase D2 directly interacts with aldolase via Its PH domain. 1187 50

Changes in gene expression within roots of Glycine max (soybean), cv. Kent, susceptible to infection by Heterodera glycines (the soybean cyst nematode [SCN]), at 6, 12, and 24 h, and 2, 4, 6, and 8 days post-inoculation were monitored using microarrays containing more than 6,000 cDNA inserts. Replicate, independent biological samples were examined at each time point. Gene expression was analyzed statistically using T-tests, ANOVA, clustering algorithms, and online analytical processing (OLAP). These analyses allow the user to query the data in several ways without importing the data into third-party software. RT-PCR confirmed that WRKY6 transcription factor, trehalose phosphate synthase, EIF4a, Skp1, and CLB1 were differentially induced across most time-points. Other genes induced across most timepoints included lipoxygenase, calmodulin, phospholipase C, metallothionein-like protein, and chalcone reductase. RT-PCR demonstrated enhanced expression during the first 12 h of infection for Kunitz trypsin inhibitor and sucrose synthase. The stress-related gene, SAM-22, phospholipase D and 12-oxophytodienoate reductase were also induced at the early time-points. At 6 and 8 dpi there was an abundance of transcripts expressed that encoded genes involved in transcription and protein synthesis. Some of those genes included ribosomal proteins, and initiation and elongation factors. Several genes involved in carbon metabolism and transport were also more abundant. Those genes included glyceraldehyde 3-phosphate dehydrogenase, fructose-bisphosphate aldolase and sucrose synthase. These results identified specific changes in gene transcript levels triggered by infection of susceptible soybean roots by SCN.
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PMID:Timecourse microarray analyses reveal global changes in gene expression of susceptible Glycine max (soybean) roots during infection by Heterodera glycines (soybean cyst nematode). 1657 92