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At least 19 recordsLinked to original sources
PubMed1988

Phenotyping of phosphoglucomutase (PGM1) isoenzymes--a new method for the follow-up of chimerism after bone marrow transplantation. Follow-up of chimerism after bone marrow transplantation by phenotyping of phosphoglucomutase (PGM1) isoenzymes.

In this study, phenotyping of phosphoglucomutase isoenzymes (PGM1, EC 2.7.5.1) in erythrocytes of bone marrow donors and hosts was shown to present a simple and exact method for the follow-up of chimerism after bone marrow transplantation, aimed at a better assessment of the transplant state and function.

Bone Marrow Transplantation↗
PubMed1977

The frequency in Japanese of genetic variants of 22 proteins. III. Phosphoglucomutase-1, phosphoglucomutase-2, 6-phosphogluconate dehydrogenase, adenylate kinase, and adenosine deaminase.

Five enzyme systems, PGM1, PGM2, ADA, 6-PGD and AK, were examined by electrophoresis in over 4000 samples from Hiroshima and Nagasaki for the frequencies of common and rare variants. In the PGM1 system, the PGM2(1) allele and PGM7(1) allele were found in polymorphic proportions, In addition, five kinds of slow variants and three types of fast variants of PGM1 were detected. The PGM3(1)NGS1 allele was found in five individuals from Nagasaki, but was not observed in samples from Hiroshima. There were no variants of PGM2. Three kinds of fast variants of 6-PGD were detected. No variation in AK was observed. There were no rare variants of ADA. The 6-PGDc allele had a frequency of 0.084 in Hiroshima and 0.093 in Nagasaki, and the ADA2 allele frequencies of 0.025 in Hiroshima and 0.032 in Nagasaki.

Adenosine Deaminase↗
PubMedDate not supplied

Phosphoglucomutase genetic polymorphism and human fertility.

We studied the phosphoglucomutase phenotype in relation to fertility parameters in a consecutive series of 204 women who had delivered a normal live-born child in Rome. A highly significant association was found between age of the women and phosphoglucomutase phenotype, suggesting a reduced rate of reproduction among women of phosphoglucomutase Type 1. Previous spontaneous abortion appears related to both age and phosphoglucomutase enzymatic type. An increased incidence of abortion in women of older ages was observed only in phosphoglucomutase Type 1. Gestational duration and fetal intrauterine growth rate are also significantly associated with maternal phosphoglucomutase phenotype. The pattern is complex, but also in this instance the influence of maternal age was evident. Considered altogether, the data suggest that phosphoglucomutase may have an important role in zygote development and survival through the whole span of intrauterine life.

Abortion, Spontaneous↗
PubMed1975

Complementarity in the regulation of phosphoglucomutase, phosphofructokinase and hexokinase; the role of glucose 1,6-bisphosphate.

ATP and citrate, the well known inhibitors of phosphofructokinase (ATP: D-fructose 6-phosphate 1-phosphotransferase, EC 2.7.1.11), were found to inhibit the activities of the multiple forms of phosphoglucomutase (alpha-D-glucose 1,6-bisphosphate: alpha-D-glucose 1-phosphate phosphotransferase, EC 2.7.5.1) from rat muscle and adipose tissue. This inhibition could be reversed by an increase in the glucose 1,6-bisphosphate (Glc-1,6-P2) concentration. Other known activators (deinhibitors) of phosphofructokinase, viz. cyclic AMP, AMP, ADP or Pi, had no direct deinhibitory action on the ATP or citrate inhibited multiple phosphoglucomutases. Cyclic AMP and AMP, could however lead indirectly to deinhibition of the phosphoglucomutases, by activating phosphofructokinase which catalyzes the ATP-dependent phosphorylation of glucose 1-phosphate to form Glc-1,6-P2, the la-ter then released the multiple phosphoglucomutases from ATP or citrate inhibition. The Glc-1,6-P2 was also found to exert a selective inhibitory effect on hexokinase (ATP: D-hexose 6-phosphotransferase, EC 2.7.1.1) type II, the predominant form in skeletal muscle. This selective inhibition by Glc-1,6-P2 was demonstrated on the multiple hexokinases which were resolved by cellogel electrophoresis or isolated by chromatography on DEAE-cellulose. Based on the in vitro studies it is suggested that during periods of highly active epinephrine-induced glycogenolysis in muscle, the Glc-1,6-P2, produced by the cyclic AMP-stimulated reaction of phosphofructokinase with glucose 1-phosphate, will release the phosphoglucomutases from ATP or citrate inhibition, and will depress the activity of muscle type II hexokinase.

Adenosine Triphosphate↗
PubMed1986

Subtyping phosphoglucomutase-1 in semen stains and bloodstains: a report on the method.

A method is described for obtaining nondistorted, reproducible phosphoglucomutase-1 subtyping patterns from semen stains and bloodstains. Isoelectric focusing of phosphoglucomutase-1 was accomplished in 80 min in a 0.2-mm-thick polyacrylamide gel with an interelectrode wick distance of 8.0 cm. The gel contained 1.2% (w/v) N-(2-hydroxyethyl) piperazine-N-3-propanesulfonic acid (EPPS) and pH 5 to 7 ampholytes (4% w/v). When maintained at room temperature, laboratory-prepared bloodstains and semen stains could be typed for phosphoglucomutase-1 up to four months and three weeks, respectively. An evaluation of phosphoglucomutase-1 typing by isoelectric focusing and the Group I system was performed on casework samples submitted to the FBI Laboratory. In addition to the increased discriminating probability of phosphoglucomutase-1 when subtyped, isoelectric focusing yielded an increase in positive calls on questioned bloodstains (65.6 versus 36.2%) and dried seminal stains (16.4 versus 13.1%) compared with the Group I system.

Blood Stains↗
PubMed1979

The regulation of hexokinase and phosphoglucomutase activity in Aspergillus nidulans.

The levels of glucose-6-phosphate and 6-phosphogluconate dehydrogenase in wildtype cells of Aspergillus nidulans varied with the carbon and nitrogen source. In general, hexokinase activity did not vary with carbon or nitrogen source. The ammonium derepressed mutant amrA1 had only 50% of the wildtype level of hexokinase. Phosphoglucomutase activity was low in wildtype cells grown with nitrate, but high in cells grown with ammonium when glucose was the carbon source. A non-inducible mutant, nirA-1, in the regulatory gene for nitrate reductase, had high phosphoglucomutase activity when grown with nitrate or ammonium. A constitutive mutant nirAc1, in the regulatory gene for nitrate reductase had low phosphoglucomutase activity when grown with nitrate or ammonium. The mutants nir-1 and nirAc1 are recessive and semi-dominant respectively for abnormal phosphoglucomutase activity.

Aspergillus nidulans↗
PubMed1986

Relationships between the age-dependent decay of glucose-1,6-bisphosphate synthesis, phosphoribomutase and phosphoglucomutase in human red cells.

In human red blood cells phosphoglucomutase exists in multiple molecular forms with different isoelectric points determined by two distinct loci called PGM1 and PGM2. With regard to the phosphoglucomutase PGM1 and PGM2 isoenzymes, the latter appear to be more important in erythrocyte metabolism owing to their ability to mutate ribose monophosphates and synthetize glucose-1,6-bisphosphate. In this paper we show that, beside undergoing age-related postranslational modifications, both phosphoglucomutase PGM1 and PGM2 forms decrease their activities as the mean cell age increases. Under the experimental conditions used to separate erythrocytes by age the comparison of the younger erythrocytes with the older shows that total phosphoglucomutase, phosphoribomutase and glucose-1,6-bisphosphate synthetic activities decay by 55%, 26% and 28%, respectively. We consider that these results substantiate the multifunctionality of PGM2 isoenzymes. Furthermore we discuss the role of these forms in the age-related decay of erythrocyte metabolism.

Aging↗
PubMed1978

The effect of epinephrine and dibutyryl cyclic AMP on glucose 1,6-bisphosphate levels and the activities of hexokinase, phosphofructokinase and phosphoglucomutase in the isolated rat diaphragm.

Based on previous studies which have revealed that glucose 1,6-bisphosphate (Glc-1,6-P2) is a potent inhibitor of muscle hexokinase and an activator (deinhibitor) of phosphofructokinase and phosphoglucomutase, the effect of epinephrine on the levels of this regulator in rat diaphragm muscle was investigated. It was found that epinephrine caused an increase in diaphragm Glc-1,6-P2 levels, accompanied by a reduction in the activity of hexokinase and an activation (deinhibition) of phosphofructokinase and phosphoglucomutase. N6-2'-O-dibutyryl cyclic AMP was able to mimic all these effects of epinephrine. The concentration of glucose-6-phosphate was not changed by epinephrine, under conditions in which the hormone produced an increase in cyclic AMP and Glc-1,6-P2 levels and the concomitant decrease in hexokinase activity. It was also shown that Glc-1,6-P, in the concentration range found after epinephrine, inhibited the diaphragm hexokinase and deinhibited phosphoglucomutase. These results may suggest a mechanism of epinephrine action by which the activities of hexokinase, phosphoglucomutase and phosphofructokinase, through the action of Glc-1,6-P2, are synchronized with the cyclic AMP-mediated activation of glycogen phosphorylase, to achieve an increase in total glycogenolysis and glycolysis and a concomitant reduction in glucose utilization by the muscle.

Adenosine Triphosphate↗
PubMed1990

Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible.

The Saccharomyces cerevisiae GAL5 (PGM2) gene was isolated and shown to encode the major isozyme of phosphoglucomutase. Northern (RNA) blot hybridization revealed that the GAL5 transcript level increased three- to fourfold in response to galactose and was severely repressed in response to glucose. Total cellular phosphoglucomutase activity was likewise responsive to galactose and to glucose, and this responsiveness was found to be due primarily to variation in the activity of the major isozyme of phosphoglucomutase. These results imply that the major and minor isozymes of phosphoglucomutase have distinct roles in yeast cells. The galactose inducibility of GAL5 was found to be under the control of the GAL4, GAL80, and GAL3 genes. In striking contrast to other galactose-inducible genes, the GAL5 gene exhibited an unusually high GAL4-independent basal level of expression. These results have implications for metabolic trafficking.

Cloning, Molecular↗
PubMed1991

Relationship between oxidative stress and hepatic phosphoglucomutase activity in rats.

The relationship between the oxidative stress and inactivation of hepatic enzymes was examined in rats. An intake of lipid peroxidation products or pro-oxidative drugs provokes oxidative stress in the living body. Secondary peroxidation products of linoleic acid were administered orally, and the oxidative stress was evaluated by thiobarbituric acid (TBA) and haemoglobin-methylene blue (HMB) tests, and by the reduction in tocopherol level. A specific decrease in hepatic phosphoglucomutase activity was found following the oxidative stress caused by the dose with secondary products. Then, ten pro-oxidative drugs were administered intraperitoneally and the effects on the enzymatic activity were determined. Among the ten drugs, CCl4, alcohol, paraquat, phenobarbital, thiopental and methylcholanthrene caused the TBA values to increase, and the phosphoglucomutase activity to decrease, in the liver 24 h after the doses. It was attempted to clarify the inactivation mechanism by using parenchymal hepatocytes. When the cells were cultured in medium containing aldehydic products originating from lipid peroxidation, these aldehydes significantly suppressed the induction of phosphoglucomutase by dexamethasone as compared with the cells in aldehyde-free medium. We consider that aldehydes inhibit the hormonal induction of phosphoglucomutase in the rat liver.

Administration, Oral↗
PubMed1990

Isoelectric focusing in immobilized pH gradients of phosphoglucomutase and esterases from the spiny lobster.

A method is described for detecting polymorphisms of cephalothorax and tail homogenates of 25 puerulus staged Panulirus argus in phosphoglucomutase (PGM) and esterases. Isoelectric focusing in immobilized pH gradients was used. In the pH 6.0-8.0 interval for phosphoglucomutase and in the pH 3.5-5.0 and 4.2-4.9 ranges for esterases, both enzymes appeared as polymorphic band patterns. These could be explained by one locus with 2 alleles for phosphoglucomutase and 3 loci with 2, 3 and 4 alleles for esterases. Esterases exhibit a more extensive polymorphism in immobilized pH gradients than in polyacrylamide gel electrophoresis.

Alleles↗
PubMed1977

An inverse relation between mitochondrial hexokinase content and phosphoglucomutase activity of rat tissues.

The hexokinase: fumarase ratios of mitochondria isolated from ten tissues of the rat were determined, and compared with the tissue content of phosphoglucomutase and phosphorylase, taken as representatives of enzymes concerned with glycogen metabolism. A generally inverse relationship was found between the mitochondrial hexokinase: fumarase ratio and phosphoglucomutase levels. The cytochrome: fumarase ratios were relatively invariant in these same mitochondria. The results are interpreted as indicating a specialization of mitochondria, with increased amounts to hexokinase being associated with the mitochondria in tissues exhibiting less dependence on glycogen metabolism, as judged from phosphoglucomutase levels.

Animals↗
PubMed1975

Enzymes of normal and malignant trophoblast: phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase.

In this study we compare the specific activities and isoenzyme patterns of five enzymes--phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase--in term placenta with the analogous enzymes in a clone of choriocarcinoma cells grown in culture. Phosphoglucose isomerase, phosphoglucomutase, and lactate dehydrogenase specific activities of the choriocarcinoma did not differ by more than two or three times from the mean activities of the comparable enzymes in placenta; the specific activity of hexokinase in the choriocarcinoma amounted to 14 per cent of the mean value for placenta. In contrast, the mean specific activity of heat-stable alkaline phosphatase in the choriocarcinoma amounted to only 1 per cent of the mean value for placenta. By growing the cells in 5-bromodeoxyuridine, 20 mug per milliliter, we were able to increase alkaline phosphatase activity to 68 per cent of the mean value for placenta. For both extracts, phosphoglucose isomerase zymograms were similar and phosphoglucomutase zymograms were similar. The hexokinase zymogram of term placenta showed two isoenzymes which stained more intensely with 0.5 mM. glucose than with 0.1M glucose. A hexokinase isoenzyme was observed in zymograms of both extracts which stained more intensely with 0.1M glucose than with 0.5 mM glucose. Lactate dehydrogenase exhibited an extra isoenzyme in the choriocarcinoma extract. When the cells were cultivated in medium containing 5 mug per milliliter of 5-bromodeoxyuridine, the induced phosphatase in the cell line was electrophoretically similar to placental phosphatase. At higher concentrations of 5-bromodeoxyuridine, the most anodal isoenzyme was 0.5 cm. slower in mobility than the comparable placental isoenzyme.

Alkaline Phosphatase↗
PubMed1978

The binding of lithium and of anionic metabolites to phosphoglucomutase.

Intercept inhibition of rabbit-muscle phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate: alpha-D-glucose-1-phosphate phosphotransferase, EC 2.7.5.1) produced by several nucleotide diphosphates and compounds related to coenzyme A was re-examined in order to re-evaluate an earlier suggestion that this enzyme has an allosteric regulatory site. However, in all cases intercept inhibition constants were much larger than those previously reported, and in all but two cases were too large to assess in the assay system, i.e., were greater than 10 mM. Most of the intercept inhibition previously observed apparently was caused by the use of the Li+ salts of inhibitors. Thus, Li+ binds competitively with the natural activator, Mg2+, and in the presence of glucose phosphates binds almost as well as Mg2+: Kd approximately 10 micrometer. The observation that glucose phosphates bind to the Li+ complex of phosphoglucomutase some 900 times more tenaciously than to the corresponding Mg2+ complex could provide a partial rationale for the lack of reactivity of the Le+ form of the enzyme. Attempts to verify the dimeric structure of phosphoglucomutase that was previously reported also produced negative results.

Binding Sites↗
PubMed1991

Entamoeba histolytica zymodemes: exhibition of gamma and delta bands only of glucose phosphate isomerase and phosphoglucomutase may be influenced by starch content in the medium.

Entamoeba histolytica isolated from human can be associated with either symptomatic disease or with asymptomatic carriers. Pathogenic and nonpathogenic strains can be distinguished on the basis of differences in the electrophoretic patterns of four isoenzymes (zymodeme). With glucose phosphate isomerase and phosphoglucomutase, we observed variation of the expression of their gamma bands as a function of starch volume in culture. We cultured E. histolytica strains from different zymodemes in Robinson medium using both a low (2-4 mg/bottle) and a high (12-15 mg/bottle) content of rice starch as supplement. These cultures were monitored by electrophoresis of glucose phosphate isomerase and phosphoglucomutase. Strains having gamma or delta bands exhibited those bands when a high content of starch was used in culture, but did not do so with a low content. Contrarily, strains that never exhibited those bands did not express them when the amount of starch in the culture was increased. However, alpha and beta bands of the same isoenzymes were always present and never showed any variation. The results suggest that expression of gamma and delta bands of glucose phosphate isomerase and phosphoglucomutase are subject to culture conditions and that genes coding for those isoenzymes may be different from those coding for the alpha and beta bands.

Animals↗
PubMed1990

Inhibition of phosphoglucomutase by vanadate.

Phosphoglucomutase is inhibited by a complex formed from alpha-D-glucose 1-phosphate (Glc-1-P) and inorganic vanadate (Vi). Both the inhibition at steady state and the rate of approach to steady state are dependent on the concentrations of both Glc-1-P and Vi. Inhibition is competitive versus alpha-D-glucose 1,6-bisphosphate (Glc-P2) and is ascribed to binding of the 6-vanadate ester of Glc-1-P (V-6-Glc-1-P) to the dephospho form of phosphoglucomutase (E). The inhibition constant for V-6-Glc-1-P at pH 7.4 was determined from steady-state kinetic measurements to be 2 x 10(-12) M. The first-order rate constant for approach to steady state increases hyperbolically with inhibitor concentration. The results are consistent with rapid equilibrium binding of V-6-Glc-1-P to E, with dissociation constant 1 x 10(-9) M, followed by rate-limiting conversion of the E.V-6-Glc-1-P complex to another species, E*.V-6-Glc-1-P, with first-order rate constant 4 x 10(-2)s-1. The rate constant determined for the reverse reaction, conversion of E*.V-6-Glc-1-P to E.V-6-Glc-1-P, is 2.5 x 10(-4)s-1. Formation of E*.V-6-Glc-1-P can also occur via binding of glucose 6-vanadate to the phospho form of phosphoglucomutase (E-P) followed by phosphoryl transfer and rearrangement of the enzyme-product complex.

Glucose-6-Phosphate↗
PubMed1989

Isoenzymes of phosphoglucomutase from human red blood cells: isolation and kinetic properties.

A procedure has been developed for the purification of phosphoglucomutase from human red cell (phenotype PGM1 a1 or a3) lysates. It yields homogeneous isoenzyme preparations of the products ("primary" and "secondary") of the two PGM1 and PGM2 loci with distinctive pI (from 6.07 to 5.29). There are substantial differences between PGM1 and PGM2 isoenzymes, having single polypeptide chains of 58,500 and 69,000 Mr respectively and showing different thermostability. The kinetic properties of all the isoenzymes for the phosphoglucomutase reaction are essentially the same (apart from the specific activity of 1089-1263 units/mg for PGM1 forms vs 37-42 units/mg for PGM2 forms), but there are striking differences in substrate specificity. In fact the products of PGM1 locus are "true" phosphoglucomutases, being specific to mutate glucose monophosphates, whereas the PGM2 forms also display phosphoribomutase and glucose 1,6-bisphosphate synthetic activities. Some kinetic properties of these "side activities" are also reported.

Chromatography, DEAE-Cellulose↗