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Proceedings of the National Academy of... Jul 1969If benign cystic teratomas (dermoid cysts) of the ovary arise from a germ cell that has undergone meiosis, they should be missing genes which are present in the person....
If benign cystic teratomas (dermoid cysts) of the ovary arise from a germ cell that has undergone meiosis, they should be missing genes which are present in the person. Three independently segregating allelic isozymes in 11 benign cystic teratomas of the human female ovary were compared with normal tissue of the same case. Dermoid cysts from persons heterozygous for these isozymes are frequently homozygous for that particular gene product. One of two dermoid cysts is homozygous for glucose-6-phosphate dehydrogenase, two of four tumors are homozygous for phosphoglucomutase at the PGM(1) locus, and two (or more) of eight tumors are homozygous for phosphoglucomutase at the PGM(3) locus in women heterozygous for these allelic isozymes. These findings are consistent with the hypothesis that these tumors arise from a germ cell which has undergone meiosis with varying degrees of crossing-over.
Topics: Chromosome Mapping; Crossing Over, Genetic; Electrophoresis; Female; Glucosephosphate Dehydrogenase; Humans; Isoenzymes; Karyotyping; Meiosis; Ovarian Cysts; Phenotype; Phosphoglucomutase; Teratoma
PubMed: 5259759
DOI: 10.1073/pnas.63.3.699 -
The Journal of Biological Chemistry Oct 1994Phosphoglucomutase is the acceptor for UDP-glucose: glycoprotein glucose-1-phosphotransferase and contains Glc in a phosphodiester linkage to O-linked Man. In this...
Phosphoglucomutase is the acceptor for UDP-glucose: glycoprotein glucose-1-phosphotransferase and contains Glc in a phosphodiester linkage to O-linked Man. In this study, we have characterized the glycosylation of phosphoglucomutase by Saccharomyces cerevisiae in response to heat shock and growth in media containing carbon sources other than Glc. Phosphoglucomutase synthesized under these conditions is underglucosylated relative to that synthesized during logarithmic growth in Glc. The underglucosylation results in increased UDP-glucose:glycoprotein glucose-1-phosphotransferase acceptor activity in in vitro assays and a newly appearing less negatively charged form of phosphoglucomutase resolvable by anion exchange chromatography. Utilizing a yeast strain in which phosphoglucomutase is overexpressed via a multicopy plasmid, metabolic labeling of the enzyme with [35S]Met and [3H]Man increased in response to heat shock, whereas [3H]Glc labeling decreased. The glucosylation state of phosphoglucomutase was also compared in cells grown in media containing various carbon sources and was found to be lowest in cells utilizing Gal as the sole carbon source compared with Glc or lactate. In mammalian cells, the glucosylation of phosphoglucomutase has been shown to be sensitive to changes in cytoplasmic Ca2+ and to correlate with a change in its membrane association. The change in phosphoglucomutase's oligosaccharide in Saccharomyces cerevisiae may be important to alterations in its distribution under conditions of nutrient deprivation or metabolic stress.
Topics: Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Fungal; Glucose; Glycoproteins; Glycosylation; Hot Temperature; Mannose; Phosphoglucomutase; Phosphotransferases; Protein Processing, Post-Translational; Recombinant Proteins; Saccharomyces cerevisiae
PubMed: 7929458
DOI: No ID Found -
Proceedings of the National Academy of... May 1978It is possible to generate interspecific somatic cell hybrids that preferentially segregate mouse chromosomes, thus making possible mapping of mouse genes. Therefore,...
It is possible to generate interspecific somatic cell hybrids that preferentially segregate mouse chromosomes, thus making possible mapping of mouse genes. Therefore, comparison of the linkage relationships of homologous genes in man and mouse is now possible. Chinese hamster x mouse somatic cell hybrids segregating mouse chromosomes were tested for the expression of mouse enolase (ENO-1; EC 4.2.1.11, McKusick no. 17245), 6-phosphogluconate dehydrogenase [PGD; EC 1.1.1.44, McKusick no. 17220], phosphoglucomutase-2 (PGM-2; EC 2.7.5.1, McKusick no. 17190), and adenylate kinase-2 (AK-2; EC 2.7.4.3, McKusick no. 10302). In man, genes coding for the homologous forms of these enzymes have been assigned to the short arm of human chromosome 1. Analysis of 41 primary, independent, hybrid clones indicated that, in the mouse, ENO-1 and AK-2 are syntenic with PGD and PGM-2 and therefore can be assigned to mouse chromosome 4. In contrast, they were asyntenic with 21 other enzymes including mouse dipeptidase-1 (DIP-1, human PEP-C; EC 3.4.11.(*), McKusick no. 17000) assigned to human chromosome arm 1q and mouse chromosome 1. Karyologic analysis confirmed this assignment. These data demonstrate that a large autosomal region (21 map units in the mouse and 51 map units in the human male) has been conserved in the evolution of mouse chromosome 4 and the short arm of human chromosome 1. Identification of such conserved regions will contribute to our understanding of the evolution of the mammalian genome and could suggest gene location by homology mapping.
Topics: Adenylate Kinase; Animals; Biological Evolution; Chromosomes, Human, 1-3; Genetic Linkage; Humans; Hybrid Cells; Mice; Phosphoglucomutase; Phosphogluconate Dehydrogenase; Phosphopyruvate Hydratase; Phosphotransferases
PubMed: 209463
DOI: 10.1073/pnas.75.5.2382 -
FEBS Letters Aug 1979
Comparative Study
Changes in glucose 1,6-diphosphate and in the activities of phosphofructokinase, phosphoglucomutase and glucose 1,6-diphosphate phosphatase induced by fasting and refeeding in dystrophic muscle.
Topics: Animals; Fasting; Glucosephosphates; Mice; Mice, Inbred Strains; Muscles; Muscular Dystrophy, Animal; Phosphofructokinase-1; Phosphoglucomutase; Phosphoric Monoester Hydrolases
PubMed: 225208
DOI: 10.1016/0014-5793(79)80824-8 -
European Journal of Biochemistry Sep 19751. A procedure has been described for the purification of the major isozyme of yeast phosphoglucomutase of highest known specific activity. 2. The native enzyme has a...
1. A procedure has been described for the purification of the major isozyme of yeast phosphoglucomutase of highest known specific activity. 2. The native enzyme has a molecular weight of about 65400 and was found to be homogeneous as judged by sucrose density gradient centrifugation, gel filtration, electrophoresis on acrylamide gel and ultracentrifugal analysis. In the presence of denaturing agents such as guanidine hydrochloride or sodium dodecyl sulfate, the enzyme dissociated into 32000-molecular-weight subunits. 3. As isolated, the enzyme has one mole of phosphate bound per mole of enzyme. Preparations incubated with 1.0 mM EDTA in 10 mM citrate buffer, pH 5.5 and dialysed against 10 mM metal-free citrate buffer, pH 5.5, contain no intrinsically bound Zn2+ and were enzymically inactive but fully active in the presence of 5 mM Mg2+ and 84% as active with 0.5 mM Zn2+. Simultaneous presence of both ions at these concentrations did not enhance activity. Enzyme was completely and irreversibly inactivated by preincubation with Be2+. Inactive enzyme had one mole of Be2+ bound per mole of enzyme. 4. Enzyme exhibited "ping-pong" kinetics rather than "random sequential". Km values for glucose 1-phosphate and for glucose 1,6-bisphosphate were calculated to be 2.34 times 10(-5) M and 2.24 times 10(-6) M, respectively. Rate of enzyme phosphate turnover was studied with rapid-mixing technique. The rates of 32P release from 32P-labeled enzyme and its appearance as glucose 6-[32P]phosphate were comparable and remained unaffected by addition of glucose 1,6-bisphosphate.
Topics: Amino Acids; Beryllium; Cations, Divalent; Isoenzymes; Kinetics; Magnesium; Molecular Weight; Phosphoglucomutase; Saccharomyces cerevisiae; Zinc
PubMed: 1100398
DOI: 10.1111/j.1432-1033.1975.tb02282.x -
The Journal of Biological Chemistry Oct 1953
Topics: Animals; Glucose-6-Phosphate Isomerase; Intramolecular Transferases; Isomerases; Phosphoglucomutase; Urochordata
PubMed: 13117844
DOI: No ID Found -
Infection and Immunity Jun 2003A homologue of the algC gene, responsible for the production of a phosphoglucomutase (PGM) associated with LPS and alginate biosynthesis in Pseudomonas aeruginosa, spgM,...
A homologue of the algC gene, responsible for the production of a phosphoglucomutase (PGM) associated with LPS and alginate biosynthesis in Pseudomonas aeruginosa, spgM, was cloned from Stenotrophomonas maltophilia. The spgM gene was shown to encode a bifunctional enzyme with both PGM and phosphomannomutase activities. Mutants lacking spgM produced less LPS than the SpgM(+) parent strain and had a tendency for shorter O polysaccharide chains. No changes in LPS chemistry were obvious as a result of the loss of spgM. Significantly, however, spgM mutants displayed a modest increase in susceptibility to several antimicrobial agents and were completely avirulent in an animal model of infection. The latter finding may relate to the resultant serum sensitivity of spgM mutants which, unlike the wild-type parent strain, were rapidly killed by human serum. These data highlight the contribution made by LPS to the antimicrobial resistance and virulence of S. maltophilia.
Topics: Animals; Cloning, Molecular; Drug Resistance, Bacterial; Humans; Lipopolysaccharides; Magnetic Resonance Spectroscopy; Microbial Sensitivity Tests; O Antigens; Phosphoglucomutase; Rats; Stenotrophomonas maltophilia; Virulence
PubMed: 12761084
DOI: 10.1128/IAI.71.6.3068-3075.2003 -
Infection and Immunity Oct 2005Streptococcus iniae represents a major health and economic problem in fish species worldwide. Random Tn917 mutagenesis and high-throughput screening in a hybrid striped...
Streptococcus iniae represents a major health and economic problem in fish species worldwide. Random Tn917 mutagenesis and high-throughput screening in a hybrid striped bass (HSB) model of meningoencephalitis identified attenuated S. iniae mutants. The Tn917 insertion in one mutant disrupted an S. iniae homologue of a phosphoglucomutase (pgm) gene. Electron microscopy revealed a decrease in capsule thickness and cell wall rigidity, with DeltaPGM mutant cells reaching sizes approximately 3-fold larger than those of the wild type (WT). The DeltaPGM mutant was cleared more rapidly in HSB blood and was more sensitive to killing by cationic antimicrobial peptides including moronecidin from HSB. In vivo, the DeltaPGM mutant was severely attenuated in HSB, as intraperitoneal challenge with 1,000 times the WT lethal dose produced only 2.5% mortality. Reintroduction of an intact copy of the S. iniae pgm gene on a plasmid vector restored antimicrobial peptide resistance and virulence to the DeltaPGM mutant. In analysis of the aborted infectious process, we found that DeltaPGM mutant organisms initially disseminated to the blood, brain, and spleen but were eliminated by 24 h without end organ damage. Ninety to 100% of fish injected with the DeltaPGM mutant and later challenged with a lethal dose of WT S. iniae survived. We conclude that the pgm gene is required for virulence in S. iniae, playing a role in normal cell wall morphology, surface capsule expression, and resistance to innate immune clearance mechanisms. An S. iniae DeltaPGM mutant is able to stimulate a protective immune response and may have value as a live attenuated vaccine for aquaculture.
Topics: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides; Bass; Fish Diseases; Fish Proteins; Gene Deletion; Genes, Bacterial; Molecular Sequence Data; Mutation; Phosphoglucomutase; Streptococcal Infections; Streptococcal Vaccines; Streptococcus; Virulence; Virulence Factors
PubMed: 16177373
DOI: 10.1128/IAI.73.10.6935-6944.2005 -
Biochemistry Jan 2012Phosphomannomutase/phosphoglucomutase contributes to the infectivity of Pseudomonas aeruginosa, retains and reorients its intermediate by 180°, and rotates domain 4 to...
Phosphomannomutase/phosphoglucomutase contributes to the infectivity of Pseudomonas aeruginosa, retains and reorients its intermediate by 180°, and rotates domain 4 to close the deep catalytic cleft. Nuclear magnetic resonance (NMR) spectra of the backbone of wild-type and S108C-inactivated enzymes were assigned to at least 90%. (13)C secondary chemical shifts report excellent agreement of solution and crystallographic structure over the 14 α-helices, C-capping motifs, and 20 of the 22 β-strands. Major and minor NMR peaks implicate substates affecting 28% of assigned residues. These can be attributed to the phosphorylation state and possibly to conformational interconversions. The S108C substitution of the phosphoryl donor and acceptor slowed transformation of the glucose 1-phosphate substrate by impairing k(cat). Addition of the glucose 1,6-bisphosphate intermediate accelerated this reaction by 2-3 orders of magnitude, somewhat bypassing the defect and apparently relieving substrate inhibition. The S108C mutation perturbs the NMR spectra and electron density map around the catalytic cleft while preserving the secondary structure in solution. Diminished peak heights and faster (15)N relaxation suggest line broadening and millisecond fluctuations within four loops that can contact phosphosugars. (15)N NMR relaxation and peak heights suggest that domain 4 reorients slightly faster in solution than domains 1-3, and with a different principal axis of diffusion. This adds to the crystallographic evidence of domain 4 rotations in the enzyme, which were previously suggested to couple to reorientation of the intermediate, substrate binding, and product release.
Topics: Catalytic Domain; Crystallography, X-Ray; Nuclear Magnetic Resonance, Biomolecular; Phosphoglucomutase; Phosphorylation; Phosphotransferases (Phosphomutases); Protein Binding; Protein Transport; Pseudomonas aeruginosa; Substrate Specificity
PubMed: 22242625
DOI: 10.1021/bi201609n -
Circulation Journal : Official Journal... 2012Phosphoglucomutase (PGM), a key enzyme in cellular glucose utilization and energy homeostasis, has been reported to show a relationship with oxidative stress. However,...
BACKGROUND
Phosphoglucomutase (PGM), a key enzyme in cellular glucose utilization and energy homeostasis, has been reported to show a relationship with oxidative stress. However, the clinical importance of PGM activity has not been investigated in patients with ischemic heart disease (IHD). The aim of the present pilot study was to clarify whether PGM activity has potential as a cardiovascular risk predictor in patients with IHD.
METHODS AND RESULTS
The levels of serum PGM activity in 237 patients with IHD (63 patients with acute myocardial infarction (AMI) and 174 patients with stable effort angina pectoris (EAP)) were evaluated. PGM activity was compared with levels of various myocardial, thrombosis, and inflammatory biomarkers on admission. PGM activity in the AMI group was significantly increased relative to that in the EAP group on admission (AMI, 55.5 μmol·min(-1)·L(-1) (U/L); EAP, 14.4 U/L (P<0.001)), and was observed to increase in parallel with well-established myocardial markers (P<0.001). Moreover, PGM activity and the lipid, thrombosis, and inflammatory biomarkers in the AMI group were higher than those in the EAP group.
CONCLUSIONS
PGM activity increased with levels of myocardial, thrombosis, and inflammatory biomarkers in patients with AMI, and might be useful in diagnostic applications during the acute phase in patients with AMI.
Topics: Adult; Aged; Angina, Stable; Animals; Biomarkers; Cattle; Female; Humans; Male; Middle Aged; Myocardial Infarction; Phosphoglucomutase; Pilot Projects; Thrombosis
PubMed: 22785563
DOI: 10.1253/circj.cj-11-1444