Disease relevance of Aldoa

• Furthermore, partial nucleotide sequence analysis of the fetal liver aldolase A mRNA supports that aldolase A mRNA that reappeared in hepatoma is really a resurgence of the gene product expressed in the fetus [1].
• Aldo increased body weight through an increase in fluid volume (estimated by decreased plasma protein concentration); however, fat stores were not different from ADX [2].
• Synthesis in vitro of aldolase A by polysomes or mRNA of rat ascites hepatoma AH 7974 cells [3].
• One of them was subcloned in M 13 phage, then used as a probe to investigate the patterns and the levels of aldolase A mRNA in various human tissues [4].

High impact information on Aldoa

• The rat aldolase A gene contains two alternative promoters and two alternative first exons [5].
• Both cell lines exhibit some characteristics of fetal liver cells, such as the expression of the 2.3-kilobase alpha-fetoprotein mRNA, aldolase A, and lactate dehydrogenases 4 and 5 [6].
• Cells of biliary epithelium from normal livers also contain aldolase A and pyruvate kinase K, but not the fetal-adult isozymes present in oval cell populations [7].
• The fetal liver isozymes aldolase A and pyruvate kinase K increase in livers of adult rats fed a choline deficient-diet containing 0.1% ethionine [7].
• Consistent with previous reports, exon M is found only in skeletal muscle and exon H, the "housekeeping" exon, is utilized in every tissue where aldolase A is expressed [8].

Biological context of Aldoa

• These results allowed us to conclude that mRNA I and mRNAs II, III were generated from a single aldolase A gene by alternative usage of exon M1 or exon AH1 in addition to exons 2 to 9 [9].
• The complete nucleotide sequence of the rat aldolase A isozyme gene, including the 5' and 3' flanking sequences, was determined [9].
• Analysis of upstream regulatory regions required for the activities of two promoters of the rat aldolase A gene [10].
• Several plasmids containing aldolase A cDNA were identified by colony hybridization with 32P-labeled cDNA prepared from immunologically purified aldolase A mRNA [11].
• A rat brain cDNA library was screened at low stringency with an aldolase B cDNA probe corresponding to the coding sequence of the mRNA, then at high stringency with a 3' non-coding aldolase A cDNA probe [12].

Anatomical context of Aldoa

• The mRNAs II and III differ in the sequence between -25 and the 5' termini from the previously reported skeletal muscle aldolase A mRNA (mRNA I, 1343 nucleotides long) [1].
• Experiments using FITC-labeled enzymes and Rh-labeled phalloidin disclosed that aldolase A associated with the cytoskeleton [13].
• Similar experiments using RNAs from fetuses at later stages, however, showed that aldolase B mRNA increased during development, whereas aldolase A mRNA decreased [14].
• Specifically, when aldolase A was incubated with human fibroblast MRC-5 permeabilized with Triton X-100, aldolase A bound to the actin filaments in the stress fibers within the cell [13].
• These findings suggest that the differentiated hepatocyte maintains a differentiated state during the liver regeneration as seen in aldolase B, whereas "oncofetal" isozymes such as aldolase A resurge after partial hepatectomy under the control of post-transcriptional mechanism [15].

Associations of Aldoa with chemical compounds

• The specific binding of aldolase A to the skeletal muscle cytoskeleton was inhibited strongly by the substrates fructose 1,6-bisphosphate and fructose 1-phosphate [13].
• Aminopeptidase and alkaline phosphatase were found from 3 days before birth in proximal tubule cells, aldolase-B and aldolase-A in all the nephron and collecting duct [16].
• The accumulation of muscle-type phosphorylase and creatine kinase and muscle-specific aldolase A mRNA accumulation during muscle development seems to be a coordinate process occurring progressively from the 17th day of intrauterine life up to the 30th day after birth [17].
• Lithium regulation of aldolase A expression in the rat frontal cortex: identification by differential display [18].
• The levels of vascular endothelial growth factor, aldolase-A, and glucose transporter-1 mRNA were significantly elevated in the Co(2+)-treated myocardium [19].

Other interactions of Aldoa

• The determined sequence of rat aldolase A mRNA was compared with the published ones of rabbit aldolase A or rat aldolase B mRNAs [20].
• The relative abundance of rat aldolase A, B, C, alpha-fetoprotein, and albumin mRNAs was determined by Northern hybridization during liver regeneration after partial hepatectomy [15].
• The cellular localization of aldolase C mRNA was determined in the central nervous system along with aldolase A mRNA by in situ hybridization [21].
• 2) After a certain lag time from the activation of HIF-1, mRNAs accumulate for two glycolytic enzymes, in particular Aldolase A and Heme Oxygenase 1, which contain HIF-1 sequences in their promoters [22].
• Treatment with l-NIL, however, failed to significantly alter aldolase A, enolase-1, and VEGF mRNA levels in normoxic cytomix-treated cells [23].

Analytical, diagnostic and therapeutic context of Aldoa

• The changes of aldolase mRNA levels were analyzed further by northern blot and dot-blot hybridization experiments using cloned aldolase A and B cDNAs [14].
• The band was identified by mass spectrometry to be aldolase A. Western blotting with aldolase using patient sera demonstrated a band of identical size [24].
• Their epitopes were mapped in detail on the molecule by examining the reactivities of the MAbs to chimeric proteins between aldolases A and B [Kitajima et al. (1990) J. Biol. Chem. 265, 17493-17498] in ELISA and to the CNBr-cleaved fragments of aldolase A in immuno-blotting [25].
• RNA was isolated and mRNA levels of the HIF-1 dependent genes aldolase A and vascular endothelial growth factor (VEGF) were determined using quantitative real-time RT-PCR [26].
• Although hepatic microvascular perfusion was comparable in saline- and LPS-treated rats, hepatic microvascular blood flow and aldolase A expression were significantly inversely correlated among endotoxemic rats (r = 0.773; P = 0.003) [26].

References