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At least 217 records · Page 12Linked to original sources
PubMed1993

FAD-linked glycerophosphate dehydrogenase activity in islets, liver, and splenocytes of NOD mice.

The activity of FAD-linked glycerophosphate dehydrogenase (m-GDH), as well as that of glutamate dehydrogenase and both glutamate-oxalacetate and glutamate-pyruvate transaminases, were measured in islet, liver, and splenocyte homogenates from 6- to 7-week-old female nonobese diabetic mice (NOD) and age- and sex-matched control mice. Despite incipient insulitis and euglycemia, the NOD mice displayed both high islet insulin content and elevated insulinemia. The activity of m-GDH, expressed relative to protein content, was not decreased in islets of NOD mice, despite the fact that such a specific activity is lower in splenic lymphocytes than islet cells. In liver homogenates, the activity of m-GDH was even higher in NOD than control mice. It is proposed, therefore, that in this model of insulin-dependent diabetes no primary decrease in islet m-GDH activity occurs, at variance with the situation recently documented in several animal models of non-insulin-dependent diabetes.

Alanine Transaminase↗
PubMed1996

Immunodetection of mitochondrial glycerophosphate dehydrogenase (mGDH) by a polyclonal antibody raised against a recombinant mGDH fragment product.

The mitochondrial enzyme glycerophosphate dehydrogenase (mGDH) plays an essential role in the B-cell glucose-sensing device and its activity in islet homogenates is impaired in several animal models of type 2 diabetes. We have now developed a polyclonal antibody, raised against a recombinant mGDH fragment product, that could be used for the immunodetection of mGDH. Total RNA was isolated from rat pancreatic islets and used in the synthesis of cDNA. Specific primers were designed that corresponded to the FAD binding domain of mGDH. The PCR product was purified and cloned into an appropriate expression vector used for transformation of Escherichia coli cells. The fusion protein was extracted from the transformed cells, further purified, and used for immunization of rabbits. The antibody recognized a single band of 72 kDa in rat islets and testis. The recombinant mGDH product was also recognized as a single band with the expected 65-kDa reference. An ELISA procedure was designed for detection of antibodies against the recombinant mGDH fragment product. The availability of the mGDH antibody opens the way to a number of further applications such as immunocytochemis- try and mGDH quantification in biological material.

Animals↗
PubMed1997

Enzyme-linked immunosorbent assay of autoantibodies against mitochondrial glycerophosphate dehydrogenase in insulin-dependent and non-insulin-dependent diabetic subjects.

The mitochondrial enzyme FAD-linked glycerophosphate dehydrogenase (mGDH) plays a key role in the recognition of glucose as a stimulus for insulin release from the pancreatic islet B-cell. In the present study, an ELISA procedure was used for the measurement of mGDH antibodies in both insulin-dependent (IDDM) and non-insulin-dependent (NIDDM) diabetic patients. Positive readings, exceeding the upper limit of the normal range, were recorded in 7 out of 12 IDDM patients, as distinct (P < 0.01) from 2 out of 12 nondiabetic subjects of comparable age. The study conducted in 41 NIDDM patients and 15 control subjects of similar age indicated that the incidence of mGDH-positive cases was not significantly different in the diabetic (4/41) and control (1/15) groups, the measurement of optical density in the positive cases barely exceeding the upper limit of the normal range. These findings indicate that the mitochondrial enzyme mGDH often acts as an antigenic determinant in IDDM, but not in NIDDM, patients.

Adolescent↗
PubMed2002

Site-directed mutations in the FAD-binding domain of glycerophosphate dehydrogenase: catalytic defects with preserved mitochondrial anchoring of the enzyme in transfected COS-7 cells.

Single-strand conformational polymorphism analysis of mitochondrial FAD-linked glycerophosphate dehydrogenase (mGDH) gene has revealed mutations in both the calcium- and FAD-binding domains of this enzyme in some diabetic patients. It was now investigated whether site-directed mutations in the FAD-binding domain of the mGDH gene may affect the mitochondrial anchoring and catalytic activity of the enzyme. COS-7 cells were transfected with plasmid cDNA coding for either wild-type or mutated human mGDH (G --> A substitutions at positions 352, 355, and 364 and A --> C substitution at position 390) fused, when required, at the N-terminus of green fluorescent protein. The activity of mGDH was measured by both radioisotopic ((3)HOH production from l-[2-(3)H]glycerol 3-phosphate) and colorimetric (iodoformazan formation) procedures. In cells transfected with the mGDHwt-EGFP or mGDHmut-EGFP constructs, the fused protein was found by confocal microscopy exclusively in the mitochondria, colocalized with a mitochondrial marker. In homogenates of COS-7 cells transfected with mGDHmut, however, the catalytic activity of the enzyme was decreased, this coinciding with low ratios between both the activities measured in the absence/presence of exogenous FAD and the results obtained by the colorimetric/radioisotopic procedure. Thus, although the present site-directed mutations of the mGDH gene failed to impair the mitochondrial anchoring of the enzyme, they led to catalytic defects that were, in some respect, comparable to those previously encountered in the lymphocytes or islets of type 2 diabetic patients.

Animals↗
PubMed1981

Extensive variation at the alpha-glycerophosphate dehydrogenase locus in species of waterstriders (Gerridae: Hemiptera).

Variation at the alpha-glycerophosphate dehydrogenase (alpha-Gpdh; EC 1.1.1.8) locus was surveyed in 11 species of waterstriders (Gerridae: Hemiptera) and five other species of aquatic Hemiptera. Species of waterstriders exhibited considerable inter- and intraspecific variation in degree of winglessness. Average heterozygosity (0.401 +/- 0.090) and average number of observed electromorphs (5.36 +/- 0.96) for the 11 gerrid species were well above values reported for nearly all other insect species surveyed to date. Wing-monomorphic and wing-polymorphic species did not differ in average alpha Gpdh heterozygosity. Of the three wing-polymorphic species surveyed geographically, two species exhibited marked variation in wing-morph frequencies but homogeneous alpha-Gpdh allele frequencies. The third species exhibited geographically homogeneous alpha-Gpdh and wing-morph frequencies, but no significant association between alpha-Gpdh phenotype and wing morph was observed in any surveyed population. These results are consistent with hypotheses evoking either relaxed purifying selection at the alpha-Gpdh locus in species of Gerridae due to the apparent reduced importance of flight, or selective maintenance of common alpha-Gpdh electromorphs.

Alleles↗
PubMed1984

Linkage studies on alpha-glycerophosphate and isocitrate dehydrogenases in Aedes albopictus (Diptera: Culicidae).

Linkage studies were carried out on alpha-glycerophosphate dehydrogenase (alpha-GPDH) and isocitrate dehydrogenase (IDH) in the mosquito Aedes (Stegomyia) albopictus. Only one locus coding for alpha-GPDH was revealed on agar gels by applying adult homogenates. Two loci for IDH were observed using either fourth-instar larvae, pupae, or adults. This study was restricted to the more anodal Idh-2 of the two loci, and alpha-Gpdh. Both alpha-Gpdh and Idh-2 encode dimeric enzymes. Thirteen backcrosses indicated that the alpha-Gpdh and Idh-2 loci are arranged in linkage group 2 in the following order: p (pigmented pupa)--(ca. 2 map units)--Wb (white-body)--(7.5-17.8)--Idh-2--(13.1)--alpha-Gpdh. Females exhibited more recombination than males.

Aedes↗
PubMed1975

Polymorphism at the alpha-glycerophosphate dehydrogenase locus in Drosophila melanogaster. I. Properties of adult allozymes.

A biochemical comparison was made between alpha-glycerophosphate dehydrogenase allozymes from Drosophila melanogaster. Enzymes extracted from the three major genotypes were indistinguishable in terms of their pH optima and thermal stabilities. Distinctive differences were observed for three parameters; temperature dependence of specific activity, temperature dependence of K-m, and reaction rate constancy over a physiological temperature range. These results are discussed in terms of a model of balancing selection and the existence of spatial and temporal allele frequency clines in natural populations.

Alleles↗
PubMed1976

Polymorphism and predictability at the alpha-glycerophosphate dehydrogenase locus in Colias butterflies: gradients in allele frequency within single populations.

Heterozygosity at the alpha-glycerophosphate dehydrogenase locus of five species of Colias butterflies is widespread in montane populations; alpine and lowland populations are not heterozygous. Within a single demographically characterized population of C. meadii where the population extends from alpine down into montane habitats, a marked cline in allele frequency is seen. Such within-population clines suggest the involvement of strong selection across the marked ecological interface. Thermal factors are the most likely causative agents, but associative overdominance is not excluded.

Acclimatization↗
PubMed1986

Relationship between alpha-glycerophosphate dehydrogenase activity and metabolic rate during flight in Drosophila melanogaster.

Measurements of wing-beat frequency (WBF) have been used to characterize flight muscle metabolic rate in Drosophila melanogaster during tethered flight. Progeny of crosses between 17 X-chromosome substitution lines and three null-activity stocks have been studied in order to determine the effect on flight metabolism of sharply reduced activity of alpha-glycerophosphate dehydrogenase (alpha GPDH). It was found that flies with an approximate 50% reduction in alpha GPDH activity have a metabolic rate that is, in most cases, indistinguishable from that of wild-type flies and, in the most extreme cases, reduced by only 4%. These results demonstrate that alpha Gpdh is not a "major gene" for flight metabolism, in the quantitative genetic sense of the term. These results are in agreement with the Kacser and Burns (1973, 1979, 1981) theory of flux, which postulates that the activity of an enzyme embedded in a multienzyme pathway can sometimes vary from wild-type to very low levels (perhaps 5-10% wild type) with no significant effect on flux through the total pathway.

Alleles↗
PubMed1981

Thermal stability of alpha-glycerophosphate dehydrogenase in Drosophila.

Thermal stability of alpha-glycerophosphate dehydrogenase-1 (alpha-Gpdh-1) in nine Drosophila species was studied at pH's ranging form 6.4 to 8.5. This was done by measuring the changes in the activity of enzymes during the heat denaturation process. In addition to temperature, the rate of denaturation is highly dependent on the pH of the incubation buffer. The results of this study show that the thermal stability of enzyme molecules is different in different species. This holds true also in the species in which the enzymes have been found to be identical by other means. The differences between species of the Drosophila virilis group are discussed.

Animals↗
PubMed1993

Is type 2 diabetes due to a deficiency of FAD-linked glycerophosphate dehydrogenase in pancreatic islets?

The mitochondrial enzyme FAD-linked glycerophosphate dehydrogenase (m-GDH) is thought to play a key role in the glucose-sensing mechanism of the insulin-producing B-cell. It catalyses a rate-limiting step of the glycerol phosphate shuttle in pancreatic islets. Its activation by Ca2+ accounts for the preferential stimulation of oxidative glycolysis and, hence, pyruvate oxidation in glucose-stimulated islets. Reduced activity of m-GDH was recently observed in islet, but not liver, homogenates from rats injected with streptozotocin during the neonatal period and in two models of inherited diabetes, i.e. GK rats and db/db mice. In the streptozotocin-injected and GK rats the m-GDH islet defect coincided, in intact islets, with an abnormally low ratio between oxidative and total glycolysis. Decreased activity of m-GDH in T-lymphocytes was also observed in 12 of 32 type 2 (non-insulin-dependent) diabetic patients, but only once among 26 other subjects including 11 healthy volunteers, 9 non-diabetics and 6 patients with either type 1 (insulin-dependent) or symptomatic diabetes. In the T-lymphocytes of type 2 diabetics the m-GDH deficiency occasionally coincided with an abnormally high ratio between glutamate-pyruvate and glutamate-oxaloacetate transaminase activities, as also observed in islets from streptozotocin-injected or GK rats. It is speculated that an islet m-GDH defect could represent a far from uncommon factor contributing to the pathogenesis of type 2 diabetes mellitus.

Animals↗
PubMed1989

Menadione-linked alpha-glycerophosphate dehydrogenase activity of motoneurons in rat soleus and extensor digitorum longus neuron pools.

After injection of horseradish peroxidase into the soleus (slow twitch) and extensor digitorum longus (fast twitch) muscles, glycolytic enzyme activity as reflected by alpha-glycerophosphate dehydrogenase activity of labeled motoneurons in the neuron pool was examined. No differences were found in glycolytic enzyme activity of motoneurons between slow twitch and fast twitch neuron pools.

Animals↗
PubMedDate not supplied

Glycerophosphate acetyltransferase activity in perfused liver of normal and hyperlipemic rats: glucagon effect.

Mitochondrial glycerophosphate-acetyltransferase activity (GPAT) was determined in the isolated and perfused liver of diet-induced hyperlipemic rats, and was found to be significantly increased compared to normal rats, A positive correlation existed between hepatic triglyceride output and GPAT. Perfusion of 10(-5) M glucagon induced a significant reduction in GPAT levels. It is suggested that the lipid-lowering action of glucagon may be mediated also through an inhibition of GPAT activity.

Acyltransferases↗
PubMed1976

The activity of mitochondrial alpha-glycerophosphate dehydrogenase in the rat nephron following triiodo-L-thyronine treatment: a histochemical study.

The effect of triiodo-L-thyronine (T3) treatment (15 mug/100 g body weight daily for 10 days) on the activity of mitochondrial alpha-glycerophosphate dehydrogenase (GPOX) in different nephron segments of the male rat was investigated by a histochemical staining method. The study showed marked segmental differences regarding the response to T3-treatment: 1. The first two proximal segments were unstained in the control rats and intensely stained following treatment. 2. The third proximal segments, the thick ascending limbs of Henle's loop and the distal convolted tubules showed a strong or moderate reaction in controls and a moderate increase after T3-treatment. 3. The high activity of collecting ducts in the cortex and outer zone of the medulla in controls was slightly increased by treatment. 4. Faintly reacting glomeruli and negative thin limbs of Henle's loop and collecting ducts in the inner medulla (papilla) were unaffected by T3-treatment. The results are discussed in relation to biochemical and physiological data.

Animals↗
PubMed1990

Stimulation of liver mitochondrial alpha-glycerophosphate dehydrogenase activity by L-thyroxine in thyroidectomized rats: comparison with the suppression of pituitary TSH secretion.

The rate of liver mitochondrial alpha-glycerophosphate dehydrogenase (GPD) induction was compared to the suppression of pituitary thyrotropin (TSH) secretion in thyroidectomized rats submitted to prolonged administration of small amounts of L-thyroxine (T4). With both 350 and 530 ng T4/100 g bw/day, liver alpha-GPD activity remained at post-thyroidectomy level (mean +/- SE: 0.030 +/- 0.002 and 0.034 +/- 0.001 delta A/mg prot/min, respectively) throughout all experiment. A sharp increase in enzyme activity was observed after 3 weeks of treatment in rats receiving 715 ng T4 / 100 g bw / day (mean +/- SE: 0.086 +/- 0.003 delta A/mg prot/min). In contrast, serum TSH levels were lower than pretreatment values (199 +/- 8ng/dI) in rats receiving 350 ng T4/100 g bw/day (mean +/- SE: 104 +/- 15 ng/dI; t = 7.48, p less than 0.001), decreased progressively with increasing T4 doses (m +/- SE:530 ng T4/100 g/day = 36 +/- 7 ng/dI); after only 48 h of treatment and were not significantly modified thereafter. The data are in agreement with the hypothesis of a nonlinear relationship between the degree of thyroid hormone receptor occupancy and the rate of liver mitochondrial alpha-GPD induction.

Analysis of Variance↗
PubMed1997

Detection of variants in the mitochondrial glycerophosphate dehydrogenase gene in Japanese NIDDM patients.

Mitochondrial FAD-linked glycerophosphate dehydrogenase (mGPDH) is thought to be an important factor for glucose sensing in pancreatic beta cells. To evaluate the significance of the mGPDH gene in the development of non-insulin-dependent diabetes mellitus (NIDDM), we set up primers and conditions for polymerase chain reaction (PCR) amplification of the coding exons and flanking regions. Screening of 100 Japanese NIDDM patients for mutations using the PCR-single strand conformation polymorphism (SSCP) method revealed four variants (ACA:Thr243-ACG:Thr243, CAT:His264-CGT:Arg264, GCA:Ala305-GCC:Ala305, GCA:Ala 306-TCA:Ser306). The His264-Arg264 variant was found in 36 patients, while the other variants were found in only one patient each. Neither the genotypic (chi 2 = 3.15, p = 0.21) nor the allelic (chi 2 = 2.27, p = 0.13) frequency of the His264-Arg264 mutation differed between 253 Japanese NIDDM patients and 157 non-diabetic subjects. In addition, in NIDDM patients, neither the treatment modality nor body mass index differed between those with and without this mutation. These results suggest that inherited defects at this locus do not make a major contribution to genetic susceptibility to NIDDM in the Japanese population.

Amino Acid Sequence↗
PubMed1984

A sensitive, continuous spectrophotometric method for assaying alpha-glycerophosphate dehydrogenase: activation by menadione.

By use of a more sensitive method than standard assays, it is demonstrated that alpha-glycerophosphate dehydrogenase activity can be monitored continuously in rat liver mitochondria; maximum activity was obtained by sonication in the presence of Triton X-100. Vitamin K3 (menadione) seems to enhance the activity of the enzyme. The assay in the presence of menadione is linear over a much greater mitochondrial concentration (up to 250 micrograms of protein in the reaction mixture).

Animals↗