Disease relevance of Aldoa

• We show that these drugs cause a detachment of the glycolytic enzymes, phosphofructokinase (ATP: D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13), from cytoskeleton of B16 melanoma cells [1].
• To determine the EBs' capability to sense low oxygen tension and to specifically respond to low ambient oxygen by modulating gene expression we quantified aldolase A and vascular endothelial growth factor (VEGF) mRNAs, since expression of these genes is upregulated by hypoxia in a variety of cells [2].
• Detachment of the glycolytic enzymes, phosphofructokinase and aldolase, from cytoskeleton of melanoma cells, induced by local anesthetics [3].
• The activities of serine protease, cathepsin B1, ornithine aminotransferase, and aldolase in skeletal muscles of mice with hereditary muscular dystrophy and their normal litter mates were studied [4].
• At 9-10 weeks after transplantation of adenocarcinoma, a negligible glycogen content and decreased phosphorylase and aldolase activities are observed in the white, intermediate and red fibre types in the three muscles [5].

Psychiatry related information on Aldoa

• Identification of aldolase as a target antigen in Alzheimer's disease [6].

High impact information on Aldoa

• This process yielded aldolase catalytic antibodies that approximated the rate acceleration of the natural enzyme used in glycolysis [7].
• 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells [8].
• Approximately 23% of the glycolytic enzyme aldolase in the perinuclear region of Swiss 3T3 cells is immobile as measured by FRAP [8].
• We have tested the effect of a key glycolytic inhibitor and an actin cytoskeletal modulator on the mobility of aldolase in living cells directly, using fluorescent analog cytochemistry and FRAP [8].
• We report here that the competitive hexokinase inhibitor 2-deoxyglucose releases the bound fraction of aldolase in 3T3 cells within 10 min, and that this process is reversible upon washout of the inhibitor [8].

Chemical compound and disease context of Aldoa

• Prolonged exposure of mice to hypoxia (7.5% O2 for up to 72 hours) also caused a decrease in liver HIF-1alpha mRNA, whereas aldolase mRNA levels increased [9].
• We report here that the local anesthetics, lidocaine and bupivacaine, induced a dose-dependent detachment of the glycolytic enzymes, phosphofructokinase (EC 2.7.1.11) and aldolase (EC 4.1.2.13), from cytoskeleton of B16 melanoma cells [3].
• Undifferentiated embryonal carcinoma cells contained only the early embryonic forms of all three enzymes, while differentiated cells formed in vivo, and in some cases in vitro, started to express the adult types of creatine phosphokinase and aldolase [10].
• Metabolism of triceps, pectoralis (in the vicinity of tumor) and gastrocnemius (away from the tumor) muscles in Swiss albino mice bearing adenocarcinoma has been studied histochemically with regard to content of glycogen, lipids, phosphorylase, aldolase, lipase, succinate dehydrogenase and cytochrome oxidase in the constituent fibres [5].

Biological context of Aldoa

• Recently, analysis of the sequence and expression of the human aldolase A gene revealed the unique arrangement of three tandem promoters and exons preceding a common coding sequence [11].
• Negative regulation of the mouse aldolase A gene. A cell cycle-dependent DNA binding activity functions as a silencer of gene transcription [12].
• The proximal promoter of the aldolase A gene remains active during myogenesis in vitro and muscle development in vivo [13].
• Structure and expression of mouse aldolase genes. Brain-specific aldolase C amino acid sequence is closely related to aldolase A [14].
• A lethal deletion on mouse chromosome 7 affects regulation of liver-cell-specific functions: posttranscriptional control of serum protein and transcriptional control of aldolase B synthesis [15].

Anatomical context of Aldoa

• In situ hybridization of mouse central nervous system using isozyme-specific probes revealed that aldolase A and C are expressed in complementary cell types [16].
• With the exception of cerebellar Purkinje cells, aldolase A mRNA is found in neurons; aldolase C message is detected in astrocytes, some cells of the pia mater, and Purkinje cells [16].
• The isozyme distribution of aldolase and enolase did not change during CFU-E in vitro differentiation into the reticulocyte [17].
• Several clones of mouse embryonic hepatocytes immortalized in serum-free MX83 medium by infection with recombinant retrovirus-expressed transcripts for connexin32, connexin26, albumin, alpha-fetoprotein, tyrosine aminotransferase, as well as aldolase A and B, at more than half of the levels found in primary mouse hepatocytes [18].
• Genomic aldolase C:LacZ fusion genes with 1.8 kb of sequence 5' to the transcription start site drive CNS expression of LacZ only in astrocytes and cells of the pia mater [19].

Associations of Aldoa with chemical compounds

• Within 2 h, C7-deficient serum plus C7, compared with C7-deficient serum alone, induced markedly decreased levels of mRNAs encoding alpha-actin, troponin I slow twitch isoform, acetylcholine receptor alpha, and muscle aldolase A, whereas the heat shock protein 83 mRNA level remained constant, by northern analysis [20].
• Developmental expression patterns of liver-specific markers that are up-regulated (e.g., phosphoenolpyruvate carboxykinase and aldolase B) and down-regulated (e.g., alpha-fetoprotein) are similar [21].
• This interaction was prevented by incubation with the aldolase substrates, fructose 1,6-bisphosphate or glyceraldehyde 3-phosphate [22].
• Aldolase mediates the association of F-actin with the insulin-responsive glucose transporter GLUT4 [22].
• We firmly establish that the endogenous aldolase B gene's first response to glucagon or cyclic AMP exposure was a transient increase in the expression in the liver, followed by a secondary decline in the transcription, as previously reported [23].

Physical interactions of Aldoa

• The combination of modeling data obtained with purified and extract systems suggests that aldolase binds to an intermediate dimer of phosphofructokinase and within this heterocomplex the kinase is completely active [24].

Co-localisations of Aldoa

• In immunocytochemical assays, aldolase was found to colocalize with V-ATPase in the renal proximal tubule [25].

Other interactions of Aldoa

• In addition, alpha-fetoprotein and aldolase A mRNA levels were also higher than in normal littermates [26].
• The glycolytic enzymes PFK, ALD, and G3PDH were distributed throughout the hypodermal tissue, somatic muscles and reproductive organs [27].
• The expression of alpha-fetoprotein and aldolase A was elevated, indicating that the liver of jvs mice is undifferentiated or dedifferentiated (FEBS Lett. 311, 63-66, 1992) [28].
• In cultures containing predominantly nerve-type cells, there was a 30-fold increase in the specific activity of acetylcholinesterase, with concomitant appearance of the aldolase isoenzyme characteristic of mouse brain [29].
• In addition to GAPDHS, ALDOA, and LDHA, this method determined that pyruvate kinase is also tightly bound to the fibrous sheath [30].

Analytical, diagnostic and therapeutic context of Aldoa

• Furthermore, microinjection of an aldolase-specific antibody also inhibited insulin-stimulated GLUT4 translocation [22].
• Immunofluorescence confocal microscopy demonstrated a significant co-localization of aldolase and GLUT4 in intact 3T3L1 adipocytes, which decreased following insulin stimulation [22].
• Aldolase was isolated associated with intact V-ATPase from bovine kidney microsomes and osteoclast-containing mouse marrow cultures in co-immunoprecipitation studies performed using an anti-E subunit monoclonal antibody [25].
• In order to determine whether this muscle-specific regulatory mechanism can be reproduced in vitro, we have examined the mRNA species of aldolase A isolated from mouse C2C12 myoblasts and myotubes on Northern blots and by primer extension [31].
• A humanized aldolase antibody for selective chemotherapy and adaptor immunotherapy [32].

References