Database : MEDLINE
Search on : Glycogen and Storage and Disease and Type and VII [Words]
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[PMID]: 27142047
[Au] Autor:Mori M; Bailey LA; Estrada J; Rehder CW; Li JS; Rogers JG; Bali DS; Buckley AF; Kishnani PS
[Ad] Address:Division of Medical Genetics, Department of Pediatrics, Duke University Medical Center (DUMC), Box 103856, Durham, NC, 27710, USA. mari.mori@duke.edu.
[Ti] Title:Severe Cardiomyopathy as the Isolated Presenting Feature in an Adult with Late-Onset Pompe Disease: A Case Report.
[So] Source:JIMD Rep;31:79-83, 2017.
[Is] ISSN:2192-8304
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Many inborn errors of metabolism can cause cardiomyopathy. Cardiomyopathy associated with glycogen storage includes PRKAG2-associated glycogen storage disease (GSD), Danon disease, infantile-onset Pompe disease (GSD II), GSD III, GSD IV, and phosphofructokinase deficiency (Tarui disease or GSD VII).We present a 35-year-old female who presented with cardiomyopathy after a pregnancy complicated by primary hyperparathyroidism. She had enjoyed excellent health until her first pregnancy at age 33. One week postpartum, she developed dyspnea and an echocardiogram revealed left ventricular ejection fraction (LVEF) of 35%. A cardiac MRI was consistent with nonischemic cardiomyopathy with an infiltrative process. Endomyocardial biopsy showed striking sarcoplasmic vacuolization, excess glycogen by PAS staining, and frequent membrane-bound glycogen by electron microscopy, consistent with lysosomal GSD. Acid alpha-glucosidase (GAA) activity in skin fibroblasts was in the affected range for Pompe disease. Sequencing of the GAA gene revealed a paternally inherited pathogenic c.525delT (p.Glu176Argfs*45) and a de novo c.309C>G (p.Cys103Trp) with unknown pathogenicity. Testing of the familial mutations in her daughter indicated that the variants in the proband were in trans. 26-gene cardiomyopathy sequencing panel had normal results thereby excluding GSD III, Danon disease, Fabry disease, and PRKAG2-associated cardiomyopathy. Therefore, results strongly suggest a diagnosis of Pompe disease.Pompe disease has a broad disease spectrum, including infantile-onset (IOPD) and late-onset (LOPD) forms. LOPD typically presents with proximal muscle weakness and respiratory insufficiency in childhood or late adulthood. Our case may represent a very unusual presentation of adult LOPD with isolated cardiomyopathy without skeletal muscle involvement or respiratory failure.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1605
[Cu] Class update date: 170816
[Lr] Last revision date:170816
[St] Status:PubMed-not-MEDLINE
[do] DOI:10.1007/8904_2016_563

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[PMID]: 27393412
[Au] Autor:Vianey-Saban C; Acquaviva C; Cheillan D; Collardeau-Frachon S; Guibaud L; Pagan C; Pettazzoni M; Piraud M; Lamazière A; Froissart R
[Ad] Address:Service Maladies Héréditaires du Métabolisme et Dépistage Néonatal, Centre de Biologie et de Pathologie Est CHU de Lyon, Lyon, France. christine.saban@chu-lyon.fr.
[Ti] Title:Antenatal manifestations of inborn errors of metabolism: biological diagnosis.
[So] Source:J Inherit Metab Dis;39(5):611-24, 2016 Sep.
[Is] ISSN:1573-2665
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Inborn errors of metabolism (IEMs) that present with abnormal imaging findings in the second half of pregnancy are mainly lysosomal storage disorders (LSDs), cholesterol synthesis disorders (CSDs), glycogen storage disorder type IV (GSD IV), peroxisomal disorders, mitochondrial fatty acid oxidation defects (FAODs), organic acidurias, aminoacidopathies, congenital disorders of glycosylation (CDGs), and transaldolase deficiency. Their biological investigation requires fetal material. The supernatant of amniotic fluid (AF) is useful for the analysis of mucopolysaccharides, oligosaccharides, sialic acid, lysosphingolipids and some enzyme activities for LSDs, 7- and 8-dehydrocholesterol, desmosterol and lathosterol for CSDs, acylcarnitines for FAODs, organic acids for organic acidurias, and polyols for transaldolase deficiency. Cultured AF or fetal cells allow the measurement of enzyme activities for most IEMs, whole-cell assays, or metabolite measurements. The cultured cells or tissue samples taken after fetal death can be used for metabolic profiling, enzyme activities, and DNA extraction. Fetal blood can also be helpful. The identification of vacuolated cells orients toward an LSD, and plasma is useful for diagnosing peroxisomal disorders, FAODs, CSDs, some LSDs, and possibly CDGs and aminoacidopathies. We investigated AF of 1700 pregnancies after exclusion of frequent etiologies of nonimmune hydrops fetalis and identified 108 fetuses affected with LSDs (6.3 %), 29 of them with mucopolysaccharidosis type VII (MPS VII), and six with GSD IV (0.3 %). In the AF of 873 pregnancies, investigated because of intrauterine growth restriction and/or abnormal genitalia, we diagnosed 32 fetuses affected with Smith-Lemli-Opitz syndrome (3.7 %).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1607
[Cu] Class update date: 171018
[Lr] Last revision date:171018
[Js] Journal subset:IM
[St] Status:In-Process
[do] DOI:10.1007/s10545-016-9947-8

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[PMID]: 26108272
[Au] Autor:Wu PL; Yang YN; Tey SL; Yang CH; Yang SN; Lin CS
[Ad] Address:Department of Pediatrics, E-DA Hospital, School of Medicine, College of Medicine, I-Shou University, Kaohsiung, Taiwan.
[Ti] Title:Infantile form of muscle phosphofructokinase deficiency in a premature neonate.
[So] Source:Pediatr Int;57(4):746-9, 2015 Aug.
[Is] ISSN:1442-200X
[Cp] Country of publication:Australia
[La] Language:eng
[Ab] Abstract:Muscle phosphofructokinase (PFK) deficiency is a rare autosomal recessive disease. We report the case of a preterm female infant who was diagnosed with the infantile form of phosphofructokinase deficiency due to a lack of PFK activity in her muscles, manifesting at a corrected age of 1 month as floppy infant syndrome, congenital joint contracture, cleft palate and duplication of the pelvicalyceal system. She died at a corrected age of 6 months due to respiratory failure. We further reviewed other infantile cases in the literature. Congenital hypotonia (78.6%), arthrogryposis (64.3%) and other systemic involvement including encephalopathy (35.7%) and cardiomyopathy (21.4%) are common presentations of the infantile form of PFK deficiency. The overall survival rate of the infantile form is low. The early recognition of multiple system involvement is essential to provide better clinical care for infants with the infantile form of PFK deficiency.
[Mh] MeSH terms primary: Glycogen Storage Disease Type VII/diagnosis
Infant, Premature
[Mh] MeSH terms secundary: Fatal Outcome
Female
Glycogen Storage Disease Type VII/complications
Humans
Immunohistochemistry
Infant
Infant, Newborn
Respiratory Insufficiency/diagnosis
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Em] Entry month:1702
[Cu] Class update date: 170202
[Lr] Last revision date:170202
[Js] Journal subset:IM
[Da] Date of entry for processing:150626
[St] Status:MEDLINE
[do] DOI:10.1111/ped.12616

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[PMID]: 26001726
[Au] Autor:Nilsson MI; MacNeil LG; Kitaoka Y; Suri R; Young SP; Kaczor JJ; Nates NJ; Ansari MU; Wong T; Ahktar M; Brandt L; Hettinga BP; Tarnopolsky MA
[Ad] Address:Department of Pediatrics and Medicine, Neuromuscular Clinic, McMaster University, Hamilton, Ontario L8N 3Z5, Canada.
[Ti] Title:Combined aerobic exercise and enzyme replacement therapy rejuvenates the mitochondrial-lysosomal axis and alleviates autophagic blockage in Pompe disease.
[So] Source:Free Radic Biol Med;87:98-112, 2015 Oct.
[Is] ISSN:1873-4596
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:A unifying feature in the pathogenesis of aging, neurodegenerative disease, and lysosomal storage disorders is the progressive deposition of macromolecular debris impervious to enzyme catalysis by cellular waste disposal mechanisms (e.g., lipofuscin). Aerobic exercise training (AET) has pleiotropic effects and stimulates mitochondrial biogenesis, antioxidant defense systems, and autophagic flux in multiple organs and tissues. Our aim was to explore the therapeutic potential of AET as an ancillary therapy to mitigate autophagic buildup and oxidative damage and rejuvenate the mitochondrial-lysosomal axis in Pompe disease (GSD II/PD). Fourteen weeks of combined recombinant acid α-glucosidase (rhGAA) and AET polytherapy attenuated mitochondrial swelling, fortified antioxidant defense systems, reduced oxidative damage, and augmented glycogen clearance and removal of autophagic debris/lipofuscin in fast-twitch skeletal muscle of GAA-KO mice. Ancillary AET potently augmented the pool of PI4KA transcripts and exerted a mild restorative effect on Syt VII and VAMP-5/myobrevin, collectively suggesting improved endosomal transport and Ca(2+)- mediated lysosomal exocytosis. Compared with traditional rhGAA monotherapy, AET and rhGAA polytherapy effectively mitigated buildup of protein carbonyls, autophagic debris/lipofuscin, and P62/SQSTM1, while enhancing MnSOD expression, nuclear translocation of Nrf-2, muscle mass, and motor function in GAA-KO mice. Combined AET and rhGAA therapy reactivates cellular clearance pathways, mitigates mitochondrial senescence, and strengthens antioxidant defense systems in GSD II/PD. Aerobic exercise training (or pharmacologic targeting of contractile-activity-induced pathways) may have therapeutic potential for mitochondrial-lysosomal axis rejuvenation in lysosomal storage disorders and related conditions (e.g., aging and neurodegenerative disease).
[Mh] MeSH terms primary: Enzyme Replacement Therapy
Exercise
Glycogen Storage Disease Type II/therapy
Mitochondria/metabolism
alpha-Glucosidases/therapeutic use
[Mh] MeSH terms secundary: Adaptor Proteins, Signal Transducing/genetics
Adaptor Proteins, Signal Transducing/metabolism
Animals
Autophagy/genetics
Disease Models, Animal
Glycogen Storage Disease Type II/genetics
Glycogen Storage Disease Type II/pathology
Heat-Shock Proteins/genetics
Heat-Shock Proteins/metabolism
Humans
Lysosomes/metabolism
Lysosomes/pathology
Mice
Mitochondria/pathology
Sequestosome-1 Protein
alpha-Glucosidases/genetics
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Adaptor Proteins, Signal Transducing); 0 (Heat-Shock Proteins); 0 (Sequestosome-1 Protein); 0 (Sqstm1 protein, mouse); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Entry month:1608
[Cu] Class update date: 161125
[Lr] Last revision date:161125
[Js] Journal subset:IM
[Da] Date of entry for processing:150524
[St] Status:MEDLINE

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[PMID]: 25985179
[Au] Autor:Webb BA; Forouhar F; Szu FE; Seetharaman J; Tong L; Barber DL
[Ad] Address:Department of Cell and Tissue Biology, University of California, San Francisco, California 94143, USA.
[Ti] Title:Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.
[So] Source:Nature;523(7558):111-4, 2015 Jul 02.
[Is] ISSN:1476-4687
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Phosphofructokinase-1 (PFK1), the 'gatekeeper' of glycolysis, catalyses the committed step of the glycolytic pathway by converting fructose-6-phosphate to fructose-1,6-bisphosphate. Allosteric activation and inhibition of PFK1 by over ten metabolites and in response to hormonal signalling fine-tune glycolytic flux to meet energy requirements. Mutations inhibiting PFK1 activity cause glycogen storage disease type VII, also known as Tarui disease, and mice deficient in muscle PFK1 have decreased fat stores. Additionally, PFK1 is proposed to have important roles in metabolic reprogramming in cancer. Despite its critical role in glucose flux, the biologically relevant crystal structure of the mammalian PFK1 tetramer has not been determined. Here we report the first structures of the mammalian PFK1 tetramer, for the human platelet isoform (PFKP), in complex with ATP-Mg(2+) and ADP at 3.1 and 3.4 Å, respectively. The structures reveal substantial conformational changes in the enzyme upon nucleotide hydrolysis as well as a unique tetramer interface. Mutations of residues in this interface can affect tetramer formation, enzyme catalysis and regulation, indicating the functional importance of the tetramer. With altered glycolytic flux being a hallmark of cancers, these new structures allow a molecular understanding of the functional consequences of somatic PFK1 mutations identified in human cancers. We characterize three of these mutations and show they have distinct effects on allosteric regulation of PFKP activity and lactate production. The PFKP structural blueprint for somatic mutations as well as the catalytic site can guide therapeutic targeting of PFK1 activity to control dysregulated glycolysis in disease.
[Mh] MeSH terms primary: Models, Molecular
Neoplasms/enzymology
Phosphofructokinase-1/chemistry
Phosphofructokinase-1/genetics
[Mh] MeSH terms secundary: Enzyme Activation
Humans
Microscopy, Electron, Transmission
Mutation/genetics
Neoplasms/genetics
Phosphofructokinase-1/ultrastructure
Protein Structure, Tertiary
Recombinant Proteins/chemistry
Recombinant Proteins/genetics
Recombinant Proteins/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Recombinant Proteins); EC 2.7.1.11 (Phosphofructokinase-1)
[Em] Entry month:1508
[Cu] Class update date: 161019
[Lr] Last revision date:161019
[Js] Journal subset:IM
[Da] Date of entry for processing:150519
[St] Status:MEDLINE
[do] DOI:10.1038/nature14405

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[PMID]: 24234586
[Au] Autor:Parker EI; Xing M; Moreno-De-Luca A; Harmouche E; Terk MR
[Ti] Title:Radiological and clinical characterization of the lysosomal storage disorders: non-lipid disorders.
[So] Source:Br J Radiol;87(1033):20130467, 2014 Jan.
[Is] ISSN:1748-880X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Lysosomal storage diseases (LSDs) are a large group of genetic metabolic disorders that result in the accumulation of abnormal material, such as mucopolysaccharides, glycoproteins, amino acids and lipids, within cells. Since many LSDs manifest during infancy or early childhood, with potentially devastating consequences if left untreated, timely identification is imperative to prevent irreversible damage and early death. In this review, the key imaging features of the non-lipid or extralipid LSDs are examined and correlated with salient clinical manifestations and genetic information. Disorders are stratified based on the type of excess material causing tissue or organ dysfunction, with descriptions of the mucopolysaccharidoses, mucolipidoses, alpha-mannosidosis, glycogen storage disorder II and cystinosis. In addition, similarities and differences in radiological findings between each of these LSDs are highlighted to facilitate further recognition. Given the rare and extensive nature of the LSDs, mastery of their multiple clinical and radiological traits may seem challenging. However, an understanding of the distinguishing imaging characteristics of LSDs and their clinical correlates may allow radiologists to play a key role in the early diagnosis of these progressive and potentially fatal disorders.
[Mh] MeSH terms primary: Lysosomal Storage Diseases/diagnosis
[Mh] MeSH terms secundary: Diagnosis, Differential
Glucuronidase/metabolism
Humans
Lyases/metabolism
Lysosomal Storage Diseases/enzymology
Metabolism, Inborn Errors/diagnosis
Mucopolysaccharidosis I/diagnosis
Mucopolysaccharidosis II/diagnosis
Mucopolysaccharidosis III/diagnosis
Mucopolysaccharidosis IV/diagnosis
Mucopolysaccharidosis VI/diagnosis
Mucopolysaccharidosis VII/diagnosis
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:9031-30-5 (mucopolysaccharidase); EC 3.2.1.31 (Glucuronidase); EC 4.- (Lyases)
[Em] Entry month:1402
[Cu] Class update date: 160804
[Lr] Last revision date:160804
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:131116
[St] Status:MEDLINE
[do] DOI:10.1259/bjr.20130467

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[PMID]: 24011984
[Au] Autor:Drouet A; Zagnoli F; Fassier T; Rannou F; Baverel F; Piraud M; Bahuau M; Petit F; Streichenberger N; Marcorelles P; Vital Durand D
[Ad] Address:Service de neurologie, HIA Desgenettes, 108, boulevard Pinel, 69275 Lyon cedex 3, France. Electronic address: drouetalain@yahoo.fr.
[Ti] Title:Intolérance musculaire à l'effort par déficit en phosphofructokinase : apport au diagnostic du bilan métabolique musculaire (tests d'effort, spectroscopie RMN du P31). [Exercise-induced muscle pain due to phosphofrutokinase deficiency: Diagnostic contribution of metabolic explorations (exercise tests, 31P-nuclear magnetic resonance spectroscopy)].
[So] Source:Rev Neurol (Paris);169(8-9):613-24, 2013 Aug-Sep.
[Is] ISSN:0035-3787
[Cp] Country of publication:France
[La] Language:fre
[Ab] Abstract:INTRODUCTION: Muscle phosphofructokinase deficiency, the seventh member of the glycogen storage diseases family, is also called Tarui's disease (GSD VII). METHODS: We studied two patients in two unrelated families with Tarui's disease, analyzing clinical features, CK level, EMG, muscle biopsy findings and molecular genetics features. Metabolic muscle explorations (forearm ischemic exercise test [FIET]; bicycle ergometer exercise test [EE]; 31P-nuclear magnetic resonance spectroscopy of calf muscle [31P-NMR-S]) are performed as appropriate. RESULTS: Two patients, a 47-year-old man and a 38-year-old woman, complained of exercise-induced fatigue since childhood. The neurological examination was normal or showed light weakness. Laboratory studies showed increased CPK, serum uric acid and reticulocyte count without anemia. There was no increase in the blood lactate level during the FIET or the EE although there was a light increase in the respiratory exchange ratio during the EE. 31P-NMR-S revealed no intracellular acidification or accumulated intermediates such as phosphorylated monoesters (PME) known to be pathognomic for GSD VII. Two new mutations were identified. DISCUSSION: FIET and EE were non-contributive to diagnosis, but 31P-NMR provided a characteristic spectra of Tarui's disease, in agreement with phosphofructokinase activity level in erythrocytes. Muscle biopsy does not always provide useful information for diagnosis. In these two cases, genetic studies failed to establish a genotype-phenotype correlation. CONCLUSION: The search for phosphofructokinase deficiency should be continued throughout life in adults experiencing fatigability or weakness because of the severe disability for daily life activities caused by the late onset form.
[Mh] MeSH terms primary: Exercise/physiology
Glycogen Storage Disease Type VII/complications
Glycogen Storage Disease Type VII/diagnosis
Muscle, Skeletal/metabolism
Myalgia/etiology
[Mh] MeSH terms secundary: Adult
Exercise Test
Female
Glycogen Storage Disease Type VII/genetics
Glycogen Storage Disease Type VII/metabolism
Humans
Magnetic Resonance Spectroscopy/methods
Male
Middle Aged
Myalgia/diagnosis
Myalgia/metabolism
Phosphorus Isotopes
[Pt] Publication type:CASE REPORTS; ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Name of substance:0 (Phosphorus Isotopes)
[Em] Entry month:1406
[Cu] Class update date: 151119
[Lr] Last revision date:151119
[Js] Journal subset:IM
[Da] Date of entry for processing:130910
[St] Status:MEDLINE

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[PMID]: 23897158
[Au] Autor:Papazian Ó; Rivas-Chacón R
[Ad] Address:Miami Children's Hospital, Miami, EE.UU.
[Ti] Title:Miopatías metabólicas. [Metabolic myopathies].
[So] Source:Rev Neurol;57 Suppl 1:S65-73, 2013 Sep 06.
[Is] ISSN:1576-6578
[Cp] Country of publication:Spain
[La] Language:spa
[Ab] Abstract:AIM: To review the metabolic myopathies manifested only by crisis of myalgias, cramps and rigidity of the muscles with decreased voluntary contractions and normal inter crisis neurologic examination in children and adolescents. DEVELOPMENT: These metabolic myopathies are autosomic recessive inherited enzymatic deficiencies of the carbohydrates and lipids metabolisms. The end result is a reduction of intra muscle adenosine triphosphate, mainly through mitochondrial oxidative phosphorylation, with decrease of available energy for muscle contraction. The one secondary to carbohydrates intra muscle metabolism disorders are triggered by high intensity brief (< 10 min) exercises. Those secondary to fatty acids metabolism disorders are triggered by low intensity prolonged (> 10 min) exercises. The conditions in the first group in order of decreasing frequency are the deficiencies of myophosforilase (GSD V), muscle phosphofructokinase (GSD VII), phosphoglycerate mutase 1 (GSD X) and beta enolase (GSD XIII). The conditions in the second group in order of decreasing frequency are the deficiencies of carnitine palmitoyl transferase II and very long chain acyl CoA dehydrogenase. CONCLUSIONS: The differential characteristics of patients in each group and within each group will allow to make the initial presumptive clinical diagnosis in the majority and then to order only the necessary tests to achieve the final diagnosis. Treatment during the crisis includes hydration, glucose and alkalinization of urine if myoglobin in blood and urine are elevated. Prevention includes avoiding exercise which may induce the crisis and fasting. The prognosis is good with the exception of rare cases of acute renal failure due to hipermyoglobinemia because of severe rabdomyolisis.
[Mh] MeSH terms primary: Carbohydrate Metabolism, Inborn Errors/genetics
Lipid Metabolism, Inborn Errors/genetics
Muscular Diseases/genetics
[Mh] MeSH terms secundary: Adolescent
Carbohydrate Metabolism, Inborn Errors/metabolism
Carnitine O-Palmitoyltransferase/deficiency
Carnitine O-Palmitoyltransferase/genetics
Exercise Tolerance
Genes, Recessive
Glycogen Phosphorylase, Muscle Form/deficiency
Glycogen Phosphorylase, Muscle Form/genetics
Glycogen Storage Disease Type V/genetics
Glycogen Storage Disease Type VII/enzymology
Glycogen Storage Disease Type VII/genetics
Humans
Infant, Newborn
Lipid Metabolism, Inborn Errors/metabolism
Metabolism, Inborn Errors/genetics
Muscle Contraction
Muscular Diseases/enzymology
Muscular Diseases/metabolism
Phosphofructokinase-1, Muscle Type/genetics
[Pt] Publication type:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.4.1.- (Glycogen Phosphorylase, Muscle Form); EC 2.7.1.- (Phosphofructokinase-1, Muscle Type)
[Em] Entry month:1406
[Cu] Class update date: 130730
[Lr] Last revision date:130730
[Js] Journal subset:IM
[Da] Date of entry for processing:130731
[St] Status:MEDLINE

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[PMID]: 23729568
[Au] Autor:Schöneberg T; Kloos M; Brüser A; Kirchberger J; Sträter N
[Ad] Address:Institute of Biochemistry, Molecular Biochemistry, Medical Faculty, University of Leipzig, Johannisallee 30, D-04103 Leipzig, Germany.
[Ti] Title:Structure and allosteric regulation of eukaryotic 6-phosphofructokinases.
[So] Source:Biol Chem;394(8):977-93, 2013 Aug.
[Is] ISSN:1437-4315
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Although the crystal structures of prokaryotic 6-phosphofructokinase, a key enzyme of glycolysis, have been available for almost 25 years now, structural information about the more complex and highly regulated eukaryotic enzymes is still lacking until now. This review provides an overview of the current knowledge of eukaryotic 6-phosphofructokinase based on recent crystal structures, kinetic analyses and site-directed mutagenesis data with special focus on the molecular architecture and the structural basis of allosteric regulation.
[Mh] MeSH terms primary: Phosphofructokinase-1/chemistry
Phosphofructokinase-1/metabolism
[Mh] MeSH terms secundary: Allosteric Regulation
Animals
Glycogen Storage Disease Type VII/genetics
Glycogen Storage Disease Type VII/metabolism
Glycolysis
Humans
Models, Molecular
Mutation
Phosphofructokinase-1/genetics
Protein Conformation
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:EC 2.7.1.11 (Phosphofructokinase-1)
[Em] Entry month:1401
[Cu] Class update date: 130703
[Lr] Last revision date:130703
[Js] Journal subset:IM
[Da] Date of entry for processing:130605
[St] Status:MEDLINE

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[PMID]: 22995305
[Au] Autor:Brüser A; Kirchberger J; Schöneberg T
[Ad] Address:Institute of Biochemistry, Medical Faculty, University of Leipzig, 04103 Leipzig, Germany.
[Ti] Title:Altered allosteric regulation of muscle 6-phosphofructokinase causes Tarui disease.
[So] Source:Biochem Biophys Res Commun;427(1):133-7, 2012 Oct 12.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Tarui disease is a glycogen storage disease (GSD VII) and characterized by exercise intolerance with muscle weakness and cramping, mild myopathy, myoglobinuria and compensated hemolysis. It is caused by mutations in the muscle 6-phosphofructokinase (Pfk). Pfk is an oligomeric, allosteric enzyme which catalyzes one of the rate-limiting steps of the glycolysis: the phosphorylation of fructose 6-phosphate at position 1. Pfk activity is modulated by a number of regulators including adenine nucleotides. Recent crystal structures from eukaryotic Pfk displayed several allosteric adenine nucleotide binding sites. Functional studies revealed a reciprocal linkage between the activating and inhibitory allosteric binding sites. Herein, we showed that Asp(543)Ala, a naturally occurring disease-causing mutation in the activating binding site, causes an increased efficacy of ATP at the inhibitory allosteric binding site. The reciprocal linkage between the activating and inhibitory binding sites leads to reduced enzyme activity and therefore to the clinical phenotype. Pharmacological blockage of the inhibitory allosteric binding site or highly efficient ligands for the activating allosteric binding site may be of therapeutic relevance for patients with Tarui disease.
[Mh] MeSH terms primary: Glycogen Storage Disease Type VII/enzymology
Muscle, Skeletal/enzymology
Phosphofructokinase-1/metabolism
[Mh] MeSH terms secundary: Alanine/chemistry
Alanine/genetics
Allosteric Regulation
Animals
Asparagine/chemistry
Asparagine/genetics
Binding Sites/genetics
Glycogen Storage Disease Type VII/genetics
Humans
Ligands
Mice
Mutation
Phosphofructokinase-1/chemistry
Phosphofructokinase-1/genetics
Protein Conformation
Rabbits
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Ligands); 7006-34-0 (Asparagine); EC 2.7.1.11 (Phosphofructokinase-1); OF5P57N2ZX (Alanine)
[Em] Entry month:1302
[Cu] Class update date: 131121
[Lr] Last revision date:131121
[Js] Journal subset:IM
[Da] Date of entry for processing:120922
[St] Status:MEDLINE


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