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At least 865 records · Page 48Linked to original sources
PubMed1983

Immunocytochemical localization of L-glutamate decarboxylase, gamma-aminobutyric acid transaminase, cysteine sulfinic acid decarboxylase, aspartate aminotransferase and somatostatin in rat retina.

The regional distribution and cellular location of GABA-synthesizing enzyme, L-glutamate decarboxylase (GAD), GABA degrading enzyme, GABA-transaminase (GABA-T), taurine synthesizing enzyme, cysteine sulfinic acid decarboxylase (CSAD), aspartate and glutamate converting enzyme, aspartate aminotransferase (AAT), and somatostatin have been visualized in the rat retina by immunocytochemical methods. GAD immunoreactivity was found to be concentrated in the inner plexiform layer. A moderate to weak staining of GAD was found in the inner nuclear layer. The distribution of GABA-T immunoreactivity was similar to that of GAD with the exception that a weak to moderate staining of GABA-T was also observed in the outer plexiform layer. CSAD immunoreactivity was seen in every layer with the heaviest staining in the inner plexiform layer, and moderate staining in the inner and outer nuclear layers and ganglion cell layer. AAT immunoreactivity was mostly concentrated in the outer nuclear layer; there was weak staining in the inner nuclear layer and inner and outer plexiform layer. Dense somatostatin staining was seen in the inner plexiform layer and moderate staining was present in the inner nuclear layer, outer plexiform layer and ganglion cell layer. These findings suggest that in rat retina, GABA-containing cells occur in some types of amacrine cells only, while taurine and somatostatin appear in both amacrine and horizontal cells. AAT immunoreactivity was primarily associated with the photoreceptor cells suggesting that AAT may be used as a marker for aspartergic/glutamergic cells and their endings in the central nervous system.

4-Aminobutyrate Transaminase↗
PubMed2001

Activities of gamma-glutamyltransferase, alkaline phosphatase and aspartate-aminotransferase in colostrum, milk and blood plasma of calves fed first colostrum at 0-2, 6-7, 12-13 and 24-25 h after birth.

Enzyme activities of gamma-glutamyltransferase (gamma-GT), alkaline phosphatase (AP) and aspartate-aminotransferase (AST) were measured from birth to the age of 28 days in calves which were fed colostrum at 0-2, 6-7, 12-13, or 24-25 h after birth. Enzyme activities were also measured in colostrum (first to fifth milking) and in mature milk. Activities were highest in the first colostrum milking and decreased to the lowest activities in mature milk. Plasma gamma-GT activity transiently increased after first colostrum intake and was greater in calves fed first colostrum within less than 6-7 h than in those fed first colostrum later than 12 h after birth. Activity of gamma-GT reflected the absorption of colostral gamma-GT, which decreased with time after birth. The AP activity transiently increased after colostrum intake and was higher in calves fed colostrum within the first 12 h of life than in those fed later after birth. The transient rise of plasma AP activity also indicated absorption of colostral AP, although endogenous sources of AP could not be excluded. The activity of AST also transiently increased after colostrum intake but there was no association with time of first colostrum feeding, indicating that the rise of plasma AST activity was the consequence of enhanced endogenous production and was independent of colostrum intake. In conclusion, there are different causes leading to postnatal changes in enzyme activities.

Alkaline Phosphatase↗
PubMed1999

Monitoring of extracellular aspartate aminotransferase and troponin T by microdialysis during and after cardioplegic heart arrest.

This study aims at developing per- and postopertive surveillance of the myocardium and focuses on ischemic damage following cardioplegic heart arrest. Levels of troponin T and total aspartate aminotransferase (ASAT) were analyzed in the myocardial interstitium of 10 patients with ischemic heart disease (IHD) who underwent coronary bypass surgery and in 12 patients with nonischemic heart disease (N-IHD) who underwent valvular surgery. Fluid from the myocardial interstitium of the anterior and the lateral wall of the heart was sampled by microdialysis probes that were implanted during surgery and extracted percutaneously 70-100 h later. There were no adverse reactions, and the equipment did not interfere with the surgical procedures. The peak in troponin T serum levels that occurred 4 h after cardiac arrest was preceded by a peak in troponin T levels in the microdialysates from the interstitium that occurred 1 h earlier. The concentration of troponin T in the microdialysate peak was 300 times higher than in the serum peak. The increase in serum ASAT levels during the first 7 h after cardiac arrest corresponded in time with a decrease in interstitial ASAT levels, which had already reached a maximum during cardiac arrest. The microdialysate/serum concentration ratio was considerably smaller for ASAT than for troponin T. Interstitial peak levels of troponin T correlated positively and significantly with peak levels of ASAT. Of the 22 patients, 15 had no postoperative events according to clinical outcome, ECG and serum tests. Fourteen of these had low to normal levels of interstitial ASAT and troponin T. Conversely, atrial fibrillation and/or premature atrial contractions were recorded in 8/22 patients, 7 of whom had elevated interstitial ASAT and/or troponin T concentrations in one or both of the sampled heart regions. The N-IHD patients had higher levels of troponin T in the interstitium 20-70 h following cardioplegia, while the peak levels did not differ between the groups. In conclusion, microdialysis sampling of troponin T and ASAT is safe and allows a highly sensitive analysis of the ischemic trauma exerted by the cardioplegic arrest.

Adult↗
PubMed1991

Unfolding of truncated and wild type aspartate aminotransferase studied by size-exclusion chromatography.

The reversible unfolding of globular proteins with increasing concentration of guanidinium chloride (GuCl) can be analysed by size-exclusion chromatography, because the hydrodynamic volume of the proteins increases during unfolding. The dimeric enzyme aspartate aminotransferase (AAT) shows an uncoupled dissociation of the identical subunits followed by the unfolding of the monomers. During the monomer unfolding formation of an intermediate is observed. A monomeric mutant of AAT unfolds with a similar shape of the unfolding transition phase, but is less stable, as shown by a shift of the transition mid-point from 1.7 M GuCl for the wild type to 1.3 M GuCl for the mutant.

Aspartate Aminotransferases↗
PubMed1982

Effect of inhibitors of RNA and protein synthesis on mitochondrial aspartate aminotransferase response to testosterone in rat ventral prostate.

The prostate gland is unusual in that it has a high content of citric acid compared with other soft tissues. The mechanism of citrate accumulation in prostate is unknown. One possibility is that aspartate aminotransferase (AAT) could supply an extra Krebs cycle source of oxaloacetate for citrate formation. Since testosterone regulates citrate production and secretion and strong transaminase activity exists in prostate, a relationship between AAT and citrate production could exist if testosterone also regulates AAT activity. To investigate this possibility, animals were castrated and given testosterone. After a total castration period of 72 hours, animals were sacrificed and mitochondrial AAT activity determined. Results revealed that castration decreased AAT activity and testosterone replacement stimulated activity. Neither castration nor testosterone affected malate dehydrogenase (MDH) activity. Both actinomycin D and cycloheximide blocked the testosterone stimulation of AAT activity. These studies indicate that testosterone may regulate AAT activity in rat ventral prostate. Furthermore, regulation may occur through testosterone stimulation of specific RNA and protein synthesis.

Animals↗
PubMed1989

Aspartate aminotransferase from Panicum maximum Jacq. var. trichoglume Eyles, a C4 plant: purification, molecular properties, and preparation of antibody.

Extracts of the leaf tissue of Panicum maximum Jacq. var. trichoglume Eyles (a phosphoenolpyruvate carboxykinase type of C4 plant) were examined and at least two isoforms of aspartate aminotransferase (EC 2.6.1.1), with different electrophoretic mobilities, were detected. The predominant isoform was purified to homogeneity from mesophyll cells. The purification procedure included fractionation with ammonium sulfate followed by chromatography on diethylaminoethyl-cellulose, Sephacryl S-300, and hydroxyapatite. The purified enzyme had specific activities of 182 and 165 mumol/min/mg protein, measured in terms of the synthesis of oxaloacetate and aspartate, respectively, at pH 8.0. The enzyme, with an apparent molecular size of 100 kDa, appears to be a dimer of a single polypeptide with a molecular size of 42 kDa. Mono specific polyclonal antibodies were raised against the 42-kDa polypeptide. Only a single stained band was detected in extracts of whole leaves by immunoblot analysis with this antibody after two-dimensional polyacrylamide electrophoresis. Furthermore, no difference in mobility was observed between the enzymes extracted from mesophyll and bundle sheath cells on native polyacrylamide gels. These findings are discussed in relation to the other isoform in the leaves of this species.

Antibodies↗
PubMed2000

Interaction of the precursor to mitochondrial aspartate aminotransferase and its presequence peptide with model membranes.

The possible contribution of the mature portion of a mitochondrial precursor protein to its interaction with membrane lipids is unclear. To address this issue, we examined the interaction of the precursor to mitochondrial aspartate aminotransferase (pmAAT) and of a synthetic peptide corresponding to the 29-residue presequence peptide (mAAT-pp) with anionic phospholipid vesicles. The affinity of mAAT-pp and pmAAT for anionic vesicles is nearly identical. Results obtained by analyzing the effect of mAAT-pp or full-length pmAAT on either the permeability or microviscosity of the phospholipid vesicles are consistent with only a shallow insertion of the presequence peptide in the bilayer. Analysis of the quenching of Trp-17 fluorescence by brominated phospholipids reveals that this presequence residue inserts to a depth of approximately 9 A from the center of the bilayer. Furthermore, in membrane-bound pmAAT or mAAT-pp, both Arg-8 and Arg-28 are accessible to the solvent. These results suggest that the presequence segment lies close to the surface of the membrane and that the mature portion of the precursor protein has little effect on the affinity or mode of binding of the presequence to model membranes. In the presence of vesicles, mAAT-pp adopts considerable alpha-helical structure. Hydrolysis by trypsin after Arg-8 results in the dissociation of the remaining 21-residue C-terminal peptide fragment from the membrane bilayer, suggesting that the N-terminal portion of the presequence is essential for membrane binding. Based on these results, we propose that the presequence peptide may contain dual recognition elements for both the lipid and import receptor components of the mitochondrial membrane.

Aspartate Aminotransferases↗
PubMed1990

Clinical usefulness of malate dehydrogenase and its mitochondrial isoenzyme in comparison with aspartate aminotransferase and its mitochondrial isoenzyme in sera of patients with liver disease.

The activities of serum malate dehydrogenase (MDH) and its mitochondrial isoenzyme (MDHm) were studied in sera of patients with liver disease. They proved to be more useful than those of aspartate aminotransferase (AST) and its mitochondrial isoenzyme for detection of hepatocellular carcinoma and acute circulatory failure, and for estimation of the severity of acute hepatitis. The N/T value measuring system, which is adaptable for autoanalysis and allows simultaneous determination of activities depending on NAD and thionicotinamide adenine dinucleotide (thio-NAD), yields both the total activity of MDH and the N/T value which was correlated significantly with MDHm/MDH (r = 0.748). Assay of MDH and its mitochondrial isoenzyme in association with the N/T value measuring system seems to be more useful and less time consuming for estimation of the severity of liver diseases than that of AST and its mitochondrial isoenzyme.

Acute Disease↗
PubMed2003

An aspartate aminotransferase of Wolbachia endobacteria from Onchocerca volvulus is recognized by IgG1 antibodies from residents of endemic areas.

Wolbachia are intracellular alpha-proteobacteria, closely related to Rickettsia, that infect various arthropods and filarial parasites. In the present study, the cDNA encoding the aspartate aminotransferase (AspAT) of Wolbachia from the human pathogenic filarial parasite Onchocerca volvulus (Ov-WolAspAT) was identified. At the amino acid level, the identity of the Ov-WolAspAT was 56% to Rickettsia prowazekii AspAT and 54% to the AspAT of the nitrogen-fixing bacterium Sinorhizobium meliloti, but the highest degree of identity was found to the putative AspAT of Wolbachia from Brugia malayi and Drosophila melanogaster (85%). All of these bacterial AspATs are members of the AspAT subclass Ib. A 35 kDa fragment of the Ov-WolAspAT was expressed in Escherichia coli, and immunolocalization using polyclonal antibodies against this antigen revealed that Ov-WolAspAT is present in a considerable proportion of the Wolbachia from O. volvulus, as well as in the endobacteria of several other filarial parasites. Western blot analysis using recombinant Ov-WolAspAT as antigen showed that IgG1 antibodies were present in 70 (51%) individuals living in areas endemic for O. volvulus, B. malayi or Wuchereria bancrofti and no IgG4 or IgE antibodies were found. Among 40 sera of persons from Uganda and Liberia who were putatively not infected with human filarial parasites, 11 (28%) individuals presented IgG1 antibodies, while none of the 33 sera from healthy Europeans and none of the 14 sera from patients with proven Rickettsia or Brucella infections reacted with the antigen. These results also show that an intracellular protein of Wolbachia endobacteria (WolAspAT) acts as antigen in human filariasis.

Amino Acid Sequence↗
PubMed2004

Longitudinal monitoring of subgingival colonization by Actinobacillus actinomycetemcomitans, and crevicular alkaline phosphatase and aspartate aminotransferase activities around orthodontically treated teeth.

OBJECTIVES: During orthodontic treatment, changes in subgingival plaque colonization and tissue inflammation and remodelling have been described. This study uses a longitudinal design to examine subgingival colonization of Actinobacillus actinomycetemcomitans (Aa) and alkaline phosphatase (ALP) and aspartate aminotransferase (AST) activities in gingival crevicular fluid (GCF) in order to assess whether these parameters have potential as biomarkers of tissue responses to orthodontic tooth movement in humans. MATERIALS & METHODS: Twenty-one patients (ages: 11.2-22.5; mean 17.1 +/- 3.3 years) participated in the study. An upper canine from each patient undergoing treatment for distal movement served as the test tooth (DC), and its contralateral (CC) and antagonist (AC) canines were used as controls. The CC was included in the orthodontic appliance, but was not subjected to the orthodontic force; the AC was free from any orthodontic appliance. The subgingival plaque and GCF around the experimental teeth was harvested from both mesial and distal tooth sites immediately before appliance activation and on day 28. Clinical gingival condition was evaluated at the baseline and at the end of the experimental period. Aa colonization was determined by culture methods, while ALP and AST activities were evaluated spectrophotometrically. RESULTS: Throughout the study, the clinical conditions worsened in both the DCs and the CCs as compared with the baseline, whereas no significant differences were found between the DCs and the CCs, or between mesial and distal sites of each of these teeth on day 28. In the ACs, clinical parameters remained at baseline levels throughout the study. Similar results were found for Aa colonization, which increased significantly on day 28 in the DC and CC groups. On day 28, ALP and AST activities were significantly elevated in all sites from the DC and CC groups as compared with the ACs, where, conversely, enzymatic activities remained at the baseline levels. However, ALP activity in the DC group was significantly greater than in the CCs at mesial (tension) sites on day 28, while AST activity in the DCs was significantly elevated as compared with the CC group at the distal (compression) sites. Greater ALP activity in the DC group was observed at the tension sites compared with the compression sites on day 28. CONCLUSIONS: Our results suggest that Aa subgingival colonization, and ALP and AST activities in GCF reflect the tissue responses that occur in the periodontium during orthodontic treatment.

Adolescent↗
PubMedDate not supplied

[The usefulness of determining myoglobin, creatine phosphokinase MB isoenzyme, lactate dehydrogenase and aspartate aminotransferase in the diagnosis of acute myocardial infarct].

Diagnosis of acute myocardial infarction is made with the aid of biomarkers such as structural myocardial proteins, myoglobin (MG) or specific enzymes, creatine phosphokinase isoenzyme MB (CK-MB) or non specific enzymes, lactic dehydrogenase (DHL) and aspartate aminotransferase (AST). We found good sensitivity (71%-50%), specificity (85%-100%) and predictive values (Pos. 77%-100%, Neg. 82%-72%) for Mg and CK-MB, supporting their clinical usefulness. In contrast DHL and AST were not clinically useful for early diagnosis.

Adolescent↗
PubMed1994

Significant improvement to the catalytic properties of aspartate aminotransferase: role of hydrophobic and charged residues in the substrate binding pocket.

The substrate specificity of tyrosine aminotransferase (eTAT) from Escherichia coli has been tested by transferring the critically different residues Leu39, Glu141, and Arg293 into equivalent positions of aspartate aminotransferase (eAAT). These residues are not directly involved in the catalytic process. The single mutant eAAT V39L possesses greater values of kcat/KM not only for tyrosine but also for aspartate and glutamate. In contrast, the double mutant eAAT P141E,A293R and also the triple mutant eAAT V39L,P141E,A293R exhibit smaller changes of kcat/KM. The converse mutants of tyrosine aminotransferase, in which critical residues of eAAT (Val39) and of mitochondrial AAT (Ala39, Val37) were transferred into equivalent positions of eTAT, exhibited generally decreased values of kcat/KM for both dicarboxylic and aromatic substrates. On the basis of the known structures of eAAT and eAAT V39L as well as of a refined model of eTAT, these results indicate that the different substrate specificities of eAAT and eTAT are due to multiple side chain differences and minor rearrangements of the backbone. The generally improved catalytic efficiency of the mutant eAAT V39L appears to be due to an indirect effect, namely, the facilitated closure of the active site upon substrate binding.

Amino Acid Sequence↗
PubMed1990

Effect of sampling time and repetition on gingival crevicular fluid and aspartate aminotransferase activity.

Tests based on the composition of gingival crevicular fluid (GCF) for detection of active periodontitis require a better understanding of sampling variables than currently exists. We have studied the effects of sample time and repetition on the presence and activity of aspartate aminotransferase (AST). Two 30-second samples of GCF were harvested within 10-minute intervals from 192 teeth with periodontitis. GCF sample size and AST activity were measured. GCF volume and AST activity of first samples were each approximately 10% greater than for second samples. The differences were significant. AST activity correlated positively with gingival index scores and probing pocket depth. Samples were also harvested from groups of 4 teeth during 5-, 10-, 20- and 30-s periods with 1-min intervals and varying sample order. For these samples, first samples contained the greatest amount of enzyme activity, regardless of sample time. When only first samples were considered, the 5- and 10-s samples showed more total activity than the 20- and 30-s samples, and differences were statistically significant. Flow rate for the 5-s sample was always higher than for all other samples, regardless of its position in the sampling sequence. Our observations are consistent with the existence of a reservoir of AST activity that is, in major part, depleted during the first 5 to 10 s of sampling, and that requires a time period of more than 10 min to reequilibrate. Five- to 10-s samples may distinguish active disease better than 20- or 30-s samples, since most of the activity is taken onto the strip in the first few seconds, and the activity is subsequently partly inactivated or diluted by the uptake of fluid less rich in enzyme activity.

Aspartate Aminotransferases↗
PubMed2001

Abamectin effects on aspartate aminotransferase and nitric oxide in rats.

Abamectin is widely used as an insecticide and an anthelmintic. A previous report indicated that abamectin was used to commit suicide and led to death in Taiwan. This investigation focused on the toxicological effects of abamectin on serum aspartate aminotransferase (AST) and nitrate/nitrite (NO) levels in rats. After rats were gavaged with abamectin ranging from 1 to 20 mg/kg/body weight, AST and NO levels were examined within 12 h. AST and NO levels were elevated in abamectin-dosed rats in a dose-dependent manner. The least increase of AST corresponded to the highest enhancement of NO release at 6 h. A negative correlation coefficient (r=-0.55) between AST and NO was found. Both NG-nitro-L-arginine-methyl ester and aminoguanidine, inhibitors of nitric oxide synthase, increased the AST level induced by abamectin. These findings suggest that NO may be involved in the alteration of AST release induced by abamectin in rats.

Animals↗
PubMed1992

[Gingival crevicular aspartate aminotransferase levels in periodontitis patients before and after periodontal treatment].

Gingival crevicular fluid samples were collected from 296 teeth from 40 subjects, including 19 rapidly progressive periodontitis (RPP), 8 chronic adult periodontitis (CAP), 7 marginal gingivitis (MG) and 6 healthy subjects (H). The activities of aspartate aminotransferase (AST) in each sample were tested. The results were as follows: (1) The two groups with destructive periodontal disease (RPP and CAP) had greater GCF-AST levels than that from the two non-destructive groups (MG and H). (2) The GCF-AST activities showed significant positive correlations with clinical periodontal parameters, such as probing depth, attachment loss, bleeding index and suppuration. (3) Four weeks after thorough full-mouth root planing, both clinical parameters and GCF-AST levels decreased significantly. The present study suggests that GCF-AST activity might be a sensitive and objective marker for detection of periodontal tissue destruction and inflammation.

Adult↗
PubMed1994

NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase.

Continuing a previous investigation (Kintanar, A., Metzler, C. M., Metzler, D. E., and Scott, R. D. (1991) J. Biol. Chem. 266, 17222-17229), we have recorded 1H NMR spectra at 500 MHz in the 10-18-ppm range for the 93-kDa porcine cytosolic aspartate aminotransferase and for four specific mutant forms of the enzyme in which histidine 68 has been replaced by lysine or histidine 143, 189, or 193 has been replaced by glutamine. We have correlated resonances for apoenzyme, pyridoxamine and pyridoxal phosphate forms, and dicarboxylate complexes and have assigned imidazole NH resonances of active site histidines. The chemical shifts of several resonances undergo pH-dependent changes around the pKa of the Schiff base proton at the active site. Other resonances shift upon binding of dicarboxylates or other ligands. Phosphate or carboxylate ions, which can also occupy the site of the substrate's alpha-carboxylate, cause rapid exchange of the Schiff base proton. Although most resonances in the 10-18-ppm range disappear rapidly in D2O, a few are retained for months in the presence of the dicarboxylate inhibitor glutarate. We demonstrate that changes in chemical shifts and in exchange rates are sensitive indicators of electronic interactions of the enzyme with ligands and of conformational change. Nuclear Overhauser effects from NH protons have allowed us to identify resonances of CH protons of the imidazole rings of histidines 143, 189, and 193. Observed and predicted chemical shifts have been compared. We conclude that the net charge on this histidine cluster is zero but that some negative charge from the aspartate 222 carboxylate is donated inductively into the histidine 143 ring. Studies of the related enzyme from Escherichia coli are provided in an accompanying paper (Metzler, D. E., Metzler, C. M., Scott, R. D., Mollova, E. T., Kagamiyama, H., Yano, T., Kuramitsu, S., Hayashi, H., Hirotsu, K., and Miyahara, I. (1994) J. Biol. Chem. 269, 28027-28033). Our approach should be applicable to the study of active sites of a broad range of relatively large proteins.

Amino Acid Sequence↗