Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.6.1.1 (aspartate aminotransferase)
21,665 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This is a case of decompensated chronic liver disease associated with FZ phenotype AAT deficiency. Histologic confirmation of the diagnosis was aided by immunostaining of the AAT globules. Liver transplantation was successful in reversing the disease process.
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PMID:End-stage liver disease in a 31-year-old man. 143 85

The levels of soluble, structural and total proteins, and the activities of A1AT and AAT decreased along with an increase in the levels of free amino acids and the activity of protease in the ctenidium, hepatopancreas and foot of the freshwater mussel L. marginalis after 1, 2, 3 and 4 d of exposure to a lethal concentration (115 mg.L-1) of nickel. But the activity of GDH and the level of urea decreased in the hepatopancreas and increased in the ctenidium and foot. A reverse trend was observed in the level of ammonia. In a sublethal concentration (23 mg.L-1), the levels of soluble, structural and total proteins and ammonia decreased in these three organs of the mussel after 1, 5, 10 and 15 d of exposures, with an increase in the levels of free aminoacids, urea and in the activities of protease, A1AT, AAT and GDH. The extent of these changes differed in degree depending on exposure period in the lethal and sublethal concentrations. The results are discussed in order to arrive at the degree of metal stress on the overall nitrogen metabolism of the mussel according to the period of exposure to lethal and sublethal concentrations of nickel.
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PMID:Effect of nickel on some aspects of protein metabolism in selected organs of the freshwater mussel Lamellidens marginalis. 144 56

The effect of potassium depolarization and N-methyl-D-aspartate (NMDA) on the activity of aspartate aminotransferase (AAT; EC 2.6.1.1), an enzyme suggested to be involved in neurotransmitter glutamate synthesis, was studied in cultured cerebellar granule neurons. Both KCl and NMDA increased AAT activity in a dose-dependent manner. When cells were treated 48-72 hr with 40 mM KCl or 150 microM NMDA the AAT was enhanced about 65-75%. The EC50 for NMDA and KCl were 25 microM and 17 mM, respectively. The effect of NMDA and KCl was specific for AAT without affecting the activity of other enzymes like lactate dehydrogenase or protein content and it was observed only in granule cells but not in astrocytes or cortical neurons. The effect of KCl was not mediated by an activation of excitatory amino acid receptors and was Ca(++)-dependent. The effect of NMDA was completely blocked by Mg++ and NMDA antagonists. The increase of AAT induced by AAT and KCl was blocked by cycloheximide and actinomycin D, suggesting an involvement of de novo synthesis of proteins and RNA. Kainic acid and quinolinic acid were also effective in increasing the AAT activity. The action of kainate was less effective than that of NMDA and it was observed only at relatively low concentrations (10 microM). Quinolinic acid raised the activity of AAT about 45% at a concentration of 500 microM. Other non-NMDA agonists did not modify the AAT activity. From these findings we can conclude that NMDA and KCl exert a trophic action on cerebellar granular neurons.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of potassium and N-methyl-D-aspartate on the aspartate aminotransferase activity in cultured cerebellar granule cells. 145 88

A pharmacokinetic study of alpha 1-antitrypsin (ATT) was performed in 2 groups of homozygous PiZ-deficient patients (treated and untreated) and 1 group of healthy volunteers. The distribution of the 131I-labelled protein corresponds to a 3-compartment model. The intravenously administered protein diffused quickly to the extravascular compartment where some retention occurred. No significant difference in AAT metabolism was observed between the 3 groups. The half-life of the injected protein is slightly longer than 2.5 days. The AAT protein was not stored. These results confirm the observations collected during the clinical trials. That is, a weekly infusion is necessary to obtain stable serum AAT concentrations. Monthly infusions are unable to maintain a 'plateau' phase. The periodicity may be limited to every 2 weeks.
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PMID:Clinical pharmacokinetics of alpha 1-antitrypsin in homozygous PiZ deficient patients. 151 30

Using a database of allozyme studies, correlations in heterozygosity between selected enzyme loci (MDH, alpha GPDH, IDH, 6PGDH, LDH, SOD, AAT, PGM, EST, PGI) were calculated across vertebrate species. Large and positive correlations were observed with untransformed heterozygosity values. However, after transformation to correct for mean species heterozygosity, correlations were substantially reduced and median values were closer to zero. Some enzymes were more often involved in significant correlations than others, and correlations calculated across species within vertebrate classes were significant for different enzyme pairs in different classes. There was no evidence that significant correlations occurred primarily between functionally related enzymes. It is suggested that the observed correlations are best explained by variation between enzyme loci in functional constraint and effective neutral mutation rate.
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PMID:A study of interlocus allozyme heterozygosity correlations: implications for neutral theory. 152 53

alpha 1 antitrypsin deficiency is associated with predisposition to the development of pulmonary emphysema and childhood cirrhosis. There are two common deficiency alleles in the European population, proteinase inhibitor (Pi) Z and S. In addition, there are rare Pinull or QO variants which can be difficult to diagnose. A family assigned as having the PiQO allele by AAT protein quantification and isoelectric focusing was shown by DNA sequencing to have the PiMheerlen mutation (Pro369-Leu). This highlights the difficulties of diagnosis of PiQO.
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PMID:What is Pi (proteinase inhibitor) null or PiQO?: a problem highlighted by the alpha 1 antitrypsin Mheerlen mutation. 155 39

The capsule of Bacteroides fragilis is unusual in that it consists of two distinct capsular polysaccharides. Using a combination of high-resolution NMR spectroscopy, theoretical calculations, and as few chemical procedures as required, the structure of both polysaccharide antigens (polysaccharides A and B) was elucidated. Using the above procedures, it was possible to obtain the complete structures using minimal quantities of polysaccharides A and B (8 and 5 mg, respectively). Only small amounts of each subjected to chemical analysis were not recoverable. Polysaccharide A is composed of the following repeating unit: [----3)alpha-D-AATp(1----4)[beta-D-Galf(1----3)]alpha-D- GalpNAc(1----3)beta-D-Galp(1----], where AAT is 2-acetamido-4-amino-2,4,6-trideoxygalactose. A pyruvate substituent having the R configuration spans O-4 and O-6 of the beta-D-galactopyranosyl residue. Polysaccharide B is composed of the following repeating unit: [----4)alpha-L-QuipNAc(1----3)beta-D-QuipNAc(1----4)[alpha-L - Fucp(1----2)beta-D-GalpA(1----3)beta-D-GlcpNAc(1----3)]alpha -D-Galp(1----]. A 2-aminoethylphosphonate substituent is situated on O-4 of the N-acetyl-beta-D-glucopyranosyl residue.
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PMID:Structural elucidation of two capsular polysaccharides from one strain of Bacteroides fragilis using high-resolution NMR spectroscopy. 156 54

Human liver cholesterol 7 alpha-hydroxylase (CYP7) cDNAs were isolated from a human liver cDNA library. A full-length cDNA has 2901 nucleotides which encode a typical P450 polypeptide of 504 amino acid residues. Two different sequences of codon 100, TTT (Phe) and TCT (Ser), were identified in cDNA clones. In addition, codons 347 and 385 are GAT (Asp) and GAC (Asp) in all cDNA clones, whereas those reported previously (FEBS Lett. 268, 137-140, 1990) are AAT (Asn) and AGC (Ser), respectively. Since there is only one 7 alpha-hydroxylase gene in the human genome, it is likely that polymorphisms at the codon 100 of cDNA clones arise from two different alleles in the 7 alpha-hydroxylase gene of this human liver.
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PMID:Polymorphisms of human cholesterol 7 alpha-hydroxylase. 161 Mar 52

To assess functional activity of leukocytes, lipid peroxidation and enzymes indicating the severity of organ lesion in food poisoning and acute dysentery, the investigators employed the techniques of luminol- and biacridine-activated chemiluminescence of pure granulocyte population and whole blood, plasma chemiluminescence, assays of AAT, AsAT, AP, LDG. A relationship was established between chemiluminescence of leukocytes and whole blood, between leukocytic functional activity and the disease duration and severity. Indomethacin treatment of the patients reduced intoxication, did not affect leukocytic function, diminished plasma chemiluminescence. Functional activity of leukocytes and the enzymes levels were prognostically significant. Low response of leukocytes to the stimulus, i.e. a small rise of functional activity, served an unfavourable prognostic sign. A role of active oxygen forms produced by leukocytes is suggested in pathogenesis of alimentary toxo-infection.
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PMID:[Functional activity of leukocytes and enzyme indicators in acute intestinal infections]. 161 Dec 59

Two isoenzymic forms of aspartate aminotransferase are present in the plant fraction of developing lupin root nodules. One of these forms, aspartate aminotransferase-P2 (AAT-P2), increases dramatically with the onset of biological nitrogen fixation and is associated with the assimilation of ammonia by the plant in the Rhizobium-legume symbiosis. A day 18 lupin nodule cDNA library in the lambda ZapII vector was immunoscreened with a monoclonal antibody specific for AAT-P2 and yielded two near-full-length 1700 bp clones. These clones were sequenced. Amino acid sequences from three peptides derived from immunopurified AAT-P2 were aligned, and showed 100% homology with the amino acid sequence deduced from the cDNA clones. The DNA sequence showed 50% homology with AAT sequences from a range of animal sources. Conversion of the clones to the phagemid form allowed their expression in Escherichia coli where both exhibited enzyme activity that could be immunoprecipitated with AAT-P2-specific monoclonal antibodies. Western blot analysis revealed protein moieties with molecular masses of 39, 43, 45 and 55 kDa. The 5' end of the clones coded for a hydrophobic leader sequence of about 50 amino acids indicative of a targeting sequence and consistent with the plastid localisation of nodule AAT-P2.
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PMID:Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules. 162 92


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