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At least 883 records · Page 49Linked to original sources
PubMed1993

Differential effects of diclofenac and aspirin on serum glutamic oxaloacetic transaminase elevations in patients with rheumatoid arthritis and osteoarthritis.

OBJECTIVE: To examine elevations in levels of serum glutamic oxaloacetic transaminase (SGOT) in patients with rheumatoid arthritis (RA) and osteoarthritis (OA) taking placebo, aspirin, or diclofenac, and to seek possible explanations for the occurrence of these elevations. METHODS: We conducted a meta-analysis of individual case reports from 3 RA protocols and 5 OA protocols, encompassing 814 diclofenac-treated patients, 443 aspirin-treated patients, and 359 placebo-treated patients. All of the RA protocols had nearly identical inclusion and exclusion criteria, as well as safety studies and followup; the same was true for the OA protocols. Analysis included correlation analysis and multiple linear and logistic regression, accounting for numerous potential confounding variables, with the SGOT as the dependent variable. F tests were used for hypothesis testing. RESULTS: By several analytic approaches, the principal determinants of SGOT concentrations were found to be baseline SGOT value, the use of aspirin in RA patients, and the use of diclofenac in OA patients. Other significant factors contributing to an increase in SGOT concentrations were duration of therapy and, perhaps, daily dosage (mg/lb). Hypothesis testing supported these results. Given a statistically average patient, we predicted a 1-2% chance of a mildly elevated SGOT level occurring among placebo-treated patients, a 6-7% chance among diclofenac- or aspirin-treated patients with RA, a 12% chance among diclofenac-treated patients with OA, and a 2% chance among aspirin-treated patients with OA. CONCLUSION: This study demonstrates a powerful method for performing meta-analysis, using available individual patient data to examine numerous factors that may affect an outcome of interest. In this case, mild elevations of SGOT were examined and found to be related to baseline SGOT levels, diclofenac use (in OA), and aspirin use (in RA). Of numerous other potential factors examined, including age, sex, alcohol use, concomitant medications, and concomitant diagnoses, only duration of therapy and, to a small extent, daily dosage, were also consistent determinants of SGOT elevation. The SGOT elevations were minimal and were not related to the occurrence of clinical hepatitis: No clinical hepatitis occurred.

Arthritis, Rheumatoid↗
PubMed1991

Description of a new variant in the glutamate-oxaloacetate transaminase system by thin-layer agarose gel isoelectric focusing.

Thin-layer isoelectric focusing in agarose within the pH range of 4.0-6.5 has shown a high resolution of the soluble cytoplasmic glutamate-oxaloacetate transaminase (GOT1) banding pattern. The complex pattern of the common GOT1 phenotype consists of eight bands with different intensities. A genetic variant of GOT1, which has been designated GOT1 Mexico, could tentatively be identified.

Alleles↗
PubMed1994

HSV-2 increases the mitochondrial aspartate amino transaminase characteristic of tumor cells.

A set of polypeptides has previously been described as being immunoprecipitated from tumor cell lysates by the sera of tumor-bearing animals (TBS) or by antisera raised to herpes simplex virus type 2 (HSV-2)-infected cells. These polypeptides were not immunoprecipitated from control cells. The principal polypeptides detected of MW 200, 90 (U90 and L90), 40, and 32 kDa were increased by HSV-2 infection. This communication describes the purification of the 40-kDa protein and its identification by amino acid sequence analysis as being homologous to the mature form of mitochondrial aspartate amino transaminase (mAAT). Two different forms of mAAT were purified and sequenced. One form, of low abundance, was immunoprecipitated by TBS and corresponded to the 40-kDa protein immunoprecipitated from tumor, but not control, cell lysates. Western blotting of the 40-kDa protein immunoprecipitated by TBS showed that it was a form of mAAT found only in tumor cells. The other abundant form reacted in Western blots with antibody to mAAT and was clearly the constitutive enzyme, present in all cells. In general, mAAT was increased up to fourfold after infection with HSV-2, HSV-2 infection also increased mAAT enzyme activity. Northern blotting and quantitative PCR showed that mAAT was induced by HSV-2 at the level of transcription. The specific form of mAAT immunoprecipitated from tumor, but not control, cell lysates could have a role in tumorigenesis, could be a putative tumor cell marker, or could be a target for antitumor drugs. HSV-2 probably induces enzymes of glutamine metabolism because HSV-2 requires glutamine for growth, thus revealing potential new antiviral targets.

Amino Acid Sequence↗
PubMed1982

Retardation of calcium oxalate precipitation by glutamic-oxalacetic-transaminase activity.

It has been found that calcium oxalate stone formers have low UGOT activity compared to healthy individuals (controls). Urine from stone formers with no GOT activity and no effect on calcium oxalate precipitation was incubated with GOT for various periods. Subsequently calcium oxalate precipitation was decreased and found to be considerably retarded i.e., the pathological urine after the incubation acted in a way similar to that of normal urine. The yield of Glutamic-Oxalacetic Transaminase (GOT) activity is glutamic acid. It was shown that glutamic acid has a significant retardation effect on the precipitation of calcium oxalate stone formation. Therefore it may be suggested that GOT activity involved in glutamic acid creation in situ, has a role in kidney stone formation.

Aspartate Aminotransferases↗
PubMed1984

Genetic polymorphism of mitochondrial glutamate-oxaloacetate transaminase in Japanese.

A survey of a number of unselected sera indicated the presence of a variant allele of mitochondrial glutamate-oxaloacetate transaminase (Got2m) in Japanese with appreciable frequency, which was confirmed in white blood cells. The mode of an autosomal codominant inheritance was confirmed by two independent family studies.

Aspartate Aminotransferases↗
PubMed1984

Genetics of mitochondrial glutamate-oxaloacetate transaminase (GOT-2) in Tigriopus californicus.

Glutamate-oxaloacetate transaminase (GOT; EC 2.6.1.1) occurs as two electrophoretically distinguishable isozymes in the copepod Tigriopus californicus. The slower-migrating form, referred to as GOT2 , is shown to be associated with the mitochondrial cell fraction. GOT2 phenotypes are inherited in typical Mendelian fashion, indicating that they are encoded by a nuclear gene. Allelic frequencies for electrophoretic variants of the two Got loci in 12 California populations of T. californicus show a sharp differentiation of local populations. Linkage studies demonstrated that Got-2 is linked to Got-1; a map of four loci in linkage group I is presented.

Alleles↗
PubMed1975

Genetic control and intracellular localization of glutamate oxaloacetic transaminase in maize.

Glutamate oxaloacetic transaminase (L-aspertate: 2-oxoglutarate aminotransferase, E.C. 2.6.1.1; GOT) was found to occur in five distinct electrophoretic forms in different tissue extracts from a number of highly inbred strains of Zea mays L. No major qualitative differences were detected in the various tissues examined, and the isozyme patterns did not undergo changes during temporal development of any given inbred strain. Cell fractionation studies showed one isozyme to be associated with the mitochondria (mGOT), another to be exclusively associated with the soluble fraction (sGOT), and a third to be associated with the glyoxysomes (gGOT). The glyoxysomal form occurs as two electrophoretically distinct variants which exist in different inbred strains of maize. The gGOT variants are under the control of two codiminant alleles (Got1A and Got1B) at the Got1 locus (isozyme5, gGOT). The genetic data and gene dosage effects suggest that GOT in maize is functionally a dimer.

Aspartate Aminotransferases↗
PubMed1980

Assignment to chromosome 16 of a gene necessary for the expression of human mitochondrial glutamate oxaloacetate transaminase (aspartate aminotransferase) (E.C. 2.6.1.1.).

A gene necessary for the expression of human mitochondrial glutamate oxaloacetate transaminase (GOT-2) has been assigned to chromosome 16 on the basis of an immunochemical analysis of human-mouse somatic cell hybrids. Mitochondrial GOT cosegregates with adenine phosphoribosyl transferase (E.C. 2.4.2.7.).

Adenine Phosphoribosyltransferase↗
PubMed1991

Genetic polymorphism of human glutamate oxaloacetate transaminase (GOT1) detected using isoelectric focusing and a sensitive and positive staining method.

Genetic polymorphism of glutamate oxaloacetate transaminase (GOT1) was demonstrated in human erythrocytes by isoelectric focusing in thin layer polyacrylamide gels and a sensitive and positive detection method. Using this technique, five phenotypes, GOT1 1, 2, 2-1, 3-1 and 3-2 were determined and the estimated gene frequencies of GOT1*1, GOT1*2 and GOT1*3 in the Japanese population were 0.9740, 0.0173 and 0.0087, respectively.

Aspartate Aminotransferases↗
PubMed1980

Assignment of the gene for cytoplasmic glutamate-oxaloacetate transaminase to mouse chromosome 19 using chinese hamster x mouse somatic cell hybrids.

Chinese hamster and mouse cytoplasmic glutamate-oxaloacetate transaminase (GOT-1, EC 2.6.1.1) were separated by isoelectric focusing of cell extracts on thin-layer polyacrylamide plates. The expression of mouse GOT-1 was correlated with the retention of mouse chromosomes and the expression of 16 marker isozymes in 77 Chinese hamster x mouse somatic cell hybrids. Mouse GOT-1 expression was discordant to the expression of isozyme genes assigned to mouse chromosomes 1, 2, 4, 5, 6, 7, 8, 9, 10, 11, 12, 14, 16, 17, 18, and X. Furthermore it showed no concordant expression with mouse chromosomes 3, 13, and 15. The expression of mouse GOT-1 was highly concordant to mouse chromosome 19 in 21 hybrid clones analyzed karyotypically. Our data confirm by means of somatic cell genetics the chromosomal assignment of the mouse GOT-1 gene based on Mendelian genetics by Eicher, Reynolds, and Southard (3). The appearance of a heteropolymeric band in hybrid cells expressing mouse GOT-1 suggests that this enzyme molecule is probably composed of two subunits.

Animals↗
PubMed1984

The L-aspartate oxidase reported to be present in higher plants is actually glutamic oxaloacetic transaminase.

We previously reported (Biochem. Biophys. Res. Commun. (1983) 111, 188-193) that cotton callus cells contain an L-aspartate oxidase which requires an unidentified cofactor with an apparent molecular weight of 1,050. Further study has revealed that this report was in error. The enzyme is actually glutamic oxaloacetic transaminase and the "cofactor" has been identified as alpha-ketoglutarate.

Amino Acid Oxidoreductases↗
PubMed1984

Immunocytochemical localizations of cytosolic and mitochondrial glutamic oxaloacetic transaminase isozymes in rat brain.

The localizations of cytosolic (s-) and mitochondrial (m-) glutamic oxaloacetic transaminase (GOT) were examined by immunocytochemical methods using specific antibodies. Staining of s-GOT-like immunoreactivity was seen in periglomerular cells of the olfactory bulb, and basket, stellate cells of the cerebellum, and second layer cells of the neocortex. On the other hand, m-GOT-like immunoreactivity was found in mitral cells and glomerular regions of the olfactory bulb and deep Golgi cells of the cerebellum. These different distributions of s- and m-GOT isozymes suggest that these isozymes are available as markers of glutamergic or aspartergic neurons.

Animals↗
PubMed1985

Immunocytochemical localizations of cytosolic and mitochondrial glutamic oxaloacetic transaminase isozymes in rat retina as markers for the glutamate-aspartate neuronal system.

The localization of cytosolic (s) or mitochondrial (m) glutamic oxaloacetic transaminase (GOT) was examined in the rat retina by means of an indirect immunofluorescence method using antibodies specific for s- and m-GOT. The m-GOT-like immunoreactive structures were seen on the inner segments of the photoreceptor cells and other outer and inner plexiform layers. These structures were dot-like in appearance. Somas were not labeled. In contrast, s-GOT-like structures were found on the inner segments and inner fibers of the photoreceptor cells, numerous cell somas in the inner nuclear layer (horizontal, amacrine and bipolar cells), and ganglion cell layer (displaced amacrine cells) and inner plexiform layer. The difference in distribution between s- and m-GOT isozymes suggests that they may be useful as markers for glutamatergic and/or aspartinergic neurons.

Animals↗
PubMed1987

Immunocytochemical localizations of cytosolic and mitochondrial glutamic oxaloacetic transaminase isozymes in rat primary sensory neurons as a marker for the glutamate neuronal system.

The localization of cytosolic (s-) and mitochondrial (m-) glutamic oxaloacetic transaminase (GOT) was examined in the rat trigeminal, jugular and dorsal root ganglia by means of an indirect immunofluorescence method using antibodies specific for s- and m-GOT. Staining of s-GOT-like immunoreactivity was seen in giant, large, medium and small cells in these ganglia. On the other hand, m-GOT-like immunoreactivity was not seen in them. The distribution of GOT suggests that glutamate may be a transmitter released from primary sensory neurons.

Animals↗
PubMed1978

Mitochondrial fraction of serum glutamic-oxaloacetic transaminase in Duchenne muscular dystrophy.

The mitochondrial fraction of serum glutamic-oxaloacetic transaminase was measured in the serum of 50 patients with Duchenne muscular dystrophy by an immunoadsorbent method. The enzyme activities in patients in the early, midstage, and late stages of the disease and controls were 21.8 +/- 7.4 (N=9), 12.2 +/- 3.7 (N=38), 6.4 +/- 1.2 (N=3) and 4.2 +/1 1.2 units/ml (N=15), respectively. The enzyme level in the early stage was significantly elevated (p less than 0.01, vs. control, p less than 0.05 vs. mid stage). As the disease progressed, the levels gradually declined, but mid-stage values were still higher than the late stage (p less than 0.01) or control values (p less than 0.01). In the late stage, enzyme activity was within the control range.

Adolescent↗
PubMed1983

Isoniazid inhibition of liver glutamic oxaloacetic transaminase from the goat Capra hircus.

Glutamic oxaloacetic transaminase (EC 2.6.1.1), has been prepared from the liver of Hausa he-goat (Capra hircus). 2. Gel filtration of the liver extract presents evidence of two molecular species of the enzyme; one species (Fraction A) has a specific activity of 280 U/mg protein and the other (Fraction B) has a specific activity of 338 U/mg protein. 3. Fraction A has optimum activity at pH 6.8 and Fraction B is optimally active at pH 5.5. The observed variation in activity with pH variation may be due to ionisation of some group(s) on the enzyme. 4. Characteristic spectral changes typical of INH/GOT interactions at low and high pH values are presented. 5. Typical Dixon's plot indicates a competitive inhibition of the enzyme by INH. Ki and Km of 0.04 and 2.5 mM for Fraction A and Ki and Km of 0.098 and 4.7 mH for Fraction B have been calculated from the data. 6. These results have been discussed in the light of the properties of the enzyme from other sources.

Animals↗
PubMed1995

Partial purification and kinetic properties of human placental cytosolic aspartate transaminase.

Human placental cytoplasmic aspartate transaminase was purified 404-fold by heat treatment, ammonium sulfate fractionation, dialysis and DEAE-Sephadex chromatography. The pH optimum of the enzyme was 6.8 in either phosphate or cacodylate buffer. The Km values of alpha-ketoglutarate and L-aspartate were 2.06 and 22.5 mM, respectively. A 78% inhibition of the enzyme was noted at 4 mM concentration of maleate which inhibited the enzyme upon competing with alpha-ketoglutarate with a Ki value of 1.72 mM. The kinetic properties of this enzyme are compared with those of the enzyme from various mammalian and other sources. The data are discussed in terms of the probable effectiveness of this enzyme in catabolizing L-aspartate in placenta especially after the consumption of a high protein diet by the pregnant mother.

Animals↗