Journal of Inherited Metabolic Disease, ISSN 0141-8955, 8/2010, Volume 33, Issue 4, pp. 387 - 396
The aim of this retrospective study was to determine the prevalence of lysosomal storage disorders (LSDs) in the Czech Republic. The data on cases diagnosed...
Biochemistry, general | Human Genetics | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MEDICINE, RESEARCH & EXPERIMENTAL | NEURONAL CEROID-LIPOFUSCINOSES | MUCOPOLYSACCHARIDOSES | NEWBORN | INVOLVEMENT | FABRY-DISEASE | INBORN-ERRORS | GERMANY | GENE | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | PROSAPOSIN DEFICIENCY | MUTATIONS | Prevalence | Humans | Netherlands - epidemiology | Lysosomal Storage Diseases - epidemiology | Lysosomal Storage Diseases - genetics | Male | Genetic Counseling | Australia - epidemiology | Czech Republic - epidemiology | Portugal - epidemiology | Female | Heterozygote | Italy - epidemiology | Retrospective Studies | Genetic Predisposition to Disease - epidemiology | Infant, Newborn | Genetic counseling | Universities and colleges | Analysis | Medical genetics | Prevalence studies (Epidemiology) | Lsds with Neurologic Involvement
Biochemistry, general | Human Genetics | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MEDICINE, RESEARCH & EXPERIMENTAL | NEURONAL CEROID-LIPOFUSCINOSES | MUCOPOLYSACCHARIDOSES | NEWBORN | INVOLVEMENT | FABRY-DISEASE | INBORN-ERRORS | GERMANY | GENE | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | PROSAPOSIN DEFICIENCY | MUTATIONS | Prevalence | Humans | Netherlands - epidemiology | Lysosomal Storage Diseases - epidemiology | Lysosomal Storage Diseases - genetics | Male | Genetic Counseling | Australia - epidemiology | Czech Republic - epidemiology | Portugal - epidemiology | Female | Heterozygote | Italy - epidemiology | Retrospective Studies | Genetic Predisposition to Disease - epidemiology | Infant, Newborn | Genetic counseling | Universities and colleges | Analysis | Medical genetics | Prevalence studies (Epidemiology) | Lsds with Neurologic Involvement
Journal Article
Journal of Inherited Metabolic Disease, ISSN 0141-8955, 3/2018, Volume 41, Issue 2, pp. 221 - 229
Mucopolysaccharidosis type II (MPSII) is a rare X-linked lysosomal storage disorder caused by mutations in the iduronate-2-sulfatase (IDS) gene (IDS, Xq28)....
Human Genetics | Biochemistry, general | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MEDICINE, RESEARCH & EXPERIMENTAL | HUNTER-SYNDROME | DEFECTS | PROTEIN | DISEASE | GROWTH | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | NEURONS | ENZYME REPLACEMENT THERAPY | Neurons - pathology | Iduronate Sulfatase - metabolism | Oligodendrocyte Precursor Cells - enzymology | Neuroglia - pathology | Humans | Astrocytes - pathology | Lysosomes - enzymology | Male | Astrocytes - enzymology | Neurogenesis | Mucopolysaccharidosis II - pathology | Mucopolysaccharidosis II - genetics | Female | Lysosomes - pathology | Induced Pluripotent Stem Cells - pathology | Induced Pluripotent Stem Cells - enzymology | Mucopolysaccharidosis II - enzymology | Glycosaminoglycans - metabolism | Neuroglia - enzymology | Cells, Cultured | Oligodendrocyte Precursor Cells - pathology | Neural Stem Cells - enzymology | Neural Stem Cells - pathology | Oligodendroglia - pathology | Cell Lineage | Phenotype | Neurons - enzymology | Iduronate Sulfatase - genetics | Oligodendroglia - enzymology | Medical research | Enzymes | Genetic vectors | Neurons | Analysis | Stem cells | Medicine, Experimental | Mucopolysaccharidosis | Sulfates | Tubulins | Cell culture | Animal models | Media (culture) | Glycosaminoglycans | Central nervous system | Stem cell transplantation | Leukocytes | Neuronal-glial interactions | Respiratory tract | Airway management | Tubulin | Allografts | Gag protein | Oligodendrocytes | Rheumatic heart disease | Heart diseases | Astrocytes | Blood cells | Glial fibrillary acidic protein | Coronary artery disease | Hearing loss | Neurological complications | Pluripotency
Human Genetics | Biochemistry, general | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | MEDICINE, RESEARCH & EXPERIMENTAL | HUNTER-SYNDROME | DEFECTS | PROTEIN | DISEASE | GROWTH | ENDOCRINOLOGY & METABOLISM | GENETICS & HEREDITY | NEURONS | ENZYME REPLACEMENT THERAPY | Neurons - pathology | Iduronate Sulfatase - metabolism | Oligodendrocyte Precursor Cells - enzymology | Neuroglia - pathology | Humans | Astrocytes - pathology | Lysosomes - enzymology | Male | Astrocytes - enzymology | Neurogenesis | Mucopolysaccharidosis II - pathology | Mucopolysaccharidosis II - genetics | Female | Lysosomes - pathology | Induced Pluripotent Stem Cells - pathology | Induced Pluripotent Stem Cells - enzymology | Mucopolysaccharidosis II - enzymology | Glycosaminoglycans - metabolism | Neuroglia - enzymology | Cells, Cultured | Oligodendrocyte Precursor Cells - pathology | Neural Stem Cells - enzymology | Neural Stem Cells - pathology | Oligodendroglia - pathology | Cell Lineage | Phenotype | Neurons - enzymology | Iduronate Sulfatase - genetics | Oligodendroglia - enzymology | Medical research | Enzymes | Genetic vectors | Neurons | Analysis | Stem cells | Medicine, Experimental | Mucopolysaccharidosis | Sulfates | Tubulins | Cell culture | Animal models | Media (culture) | Glycosaminoglycans | Central nervous system | Stem cell transplantation | Leukocytes | Neuronal-glial interactions | Respiratory tract | Airway management | Tubulin | Allografts | Gag protein | Oligodendrocytes | Rheumatic heart disease | Heart diseases | Astrocytes | Blood cells | Glial fibrillary acidic protein | Coronary artery disease | Hearing loss | Neurological complications | Pluripotency
Journal Article
Clinica Chimica Acta, ISSN 0009-8981, 10/2013, Volume 425, pp. 153 - 159
Prediagnostic steps in suspected metachromatic leukodystrophy (MLD) rely on clinical chemical methods other than enzyme assays. We report a new diagnostic...
Tandem mass spectrometry | Urinary sulfatide | DEAE-cellulose membrane | Screening for metachromatic leukodystrophy | Isoforms | Dry urinary samples | DIAGNOSIS | ASSAY | RENAL TUBULAR CELLS | ARYLSULFATASE-A | DEFICIENCY | PSEUDO ARYLSULFATASE | ARYLSULPHATASE-A | SAPOSIN-B | MOUSE MODEL | DISEASE | MEDICAL LABORATORY TECHNOLOGY | Sulfoglycosphingolipids - urine | Desiccation | Humans | Middle Aged | Specimen Handling - standards | Child, Preschool | Membranes, Artificial | Infant | Male | Leukodystrophy, Metachromatic - urine | Case-Control Studies | Tandem Mass Spectrometry | DEAE-Cellulose | Reference Standards | Leukodystrophy, Metachromatic - diagnosis | Adolescent | Solid Phase Extraction | Female | Child | Sphingolipidoses | Mass spectrometry | dry urinary samples | isoforms | tandem mass spectrometry | screening for metachromatic leukodystrophy | urinary sulfatide
Tandem mass spectrometry | Urinary sulfatide | DEAE-cellulose membrane | Screening for metachromatic leukodystrophy | Isoforms | Dry urinary samples | DIAGNOSIS | ASSAY | RENAL TUBULAR CELLS | ARYLSULFATASE-A | DEFICIENCY | PSEUDO ARYLSULFATASE | ARYLSULPHATASE-A | SAPOSIN-B | MOUSE MODEL | DISEASE | MEDICAL LABORATORY TECHNOLOGY | Sulfoglycosphingolipids - urine | Desiccation | Humans | Middle Aged | Specimen Handling - standards | Child, Preschool | Membranes, Artificial | Infant | Male | Leukodystrophy, Metachromatic - urine | Case-Control Studies | Tandem Mass Spectrometry | DEAE-Cellulose | Reference Standards | Leukodystrophy, Metachromatic - diagnosis | Adolescent | Solid Phase Extraction | Female | Child | Sphingolipidoses | Mass spectrometry | dry urinary samples | isoforms | tandem mass spectrometry | screening for metachromatic leukodystrophy | urinary sulfatide
Journal Article
American Heart Journal, ISSN 0002-8703, 2000, Volume 139, Issue 6, pp. 1101 - 1108
Background Fabry's disease is on X-linked recessive genetic deficiency of the enzyme cr-galactosidase leading to the pathologic intracellular deposition of...
HYPERTROPHY | CARDIAC & CARDIOVASCULAR SYSTEMS | RESTRICTIVE CARDIOMYOPATHY | ADULTS | LEFT-VENTRICULAR MASS | ECHOCARDIOGRAPHY | HYPERTENSION | MANIFESTATIONS | CHILDREN | Biomarkers - urine | Fabry Disease - genetics | Humans | Middle Aged | Male | Fabry Disease - enzymology | Heart Ventricles - diagnostic imaging | Electrocardiography | Adult | Female | Retrospective Studies | Glycosphingolipids - urine | Heart Ventricles - pathology | Myocardial Contraction | Severity of Illness Index | Diagnosis, Differential | Echocardiography | Fabry Disease - complications | Ventricular Dysfunction, Left - etiology | Genotype | Ventricular Dysfunction, Left - diagnosis | Biomarkers - blood | Sex Characteristics | Ventricular Dysfunction, Left - physiopathology | Heart Valves - ultrastructure | alpha-Galactosidase - blood | Heart Ventricles - physiopathology | Biopsy | Adolescent | Heart Valves - diagnostic imaging | Fabry Disease - diagnosis | Heart | Physiological aspects | Fabry's disease | Enzymes
HYPERTROPHY | CARDIAC & CARDIOVASCULAR SYSTEMS | RESTRICTIVE CARDIOMYOPATHY | ADULTS | LEFT-VENTRICULAR MASS | ECHOCARDIOGRAPHY | HYPERTENSION | MANIFESTATIONS | CHILDREN | Biomarkers - urine | Fabry Disease - genetics | Humans | Middle Aged | Male | Fabry Disease - enzymology | Heart Ventricles - diagnostic imaging | Electrocardiography | Adult | Female | Retrospective Studies | Glycosphingolipids - urine | Heart Ventricles - pathology | Myocardial Contraction | Severity of Illness Index | Diagnosis, Differential | Echocardiography | Fabry Disease - complications | Ventricular Dysfunction, Left - etiology | Genotype | Ventricular Dysfunction, Left - diagnosis | Biomarkers - blood | Sex Characteristics | Ventricular Dysfunction, Left - physiopathology | Heart Valves - ultrastructure | alpha-Galactosidase - blood | Heart Ventricles - physiopathology | Biopsy | Adolescent | Heart Valves - diagnostic imaging | Fabry Disease - diagnosis | Heart | Physiological aspects | Fabry's disease | Enzymes
Journal Article
Virchows Archiv, ISSN 0945-6317, 6/2008, Volume 452, Issue 6, pp. 651 - 665
The function and intracellular delivery of enzyme therapeutics for Fabry disease were studied in cultured fibroblasts and in the biopsied tissues of two male...
Pathology | Medicine & Public Health | α-Galactosidase A deficiency | Enzyme replacement therapy | Persistent storage | Enzyme targeting | Clearance of storage lysosomes | PROGENITOR CELLS | persistent storage | enzyme replacement therapy | EFFICACY | SAFETY | LYSOSOMAL STORAGE | clearance of storage lysosomes | PATHOLOGY | alpha-galactosidase A deficiency | enzyme targeting | ENZYME REPLACEMENT | THERAPY | COLOCALIZATION | ENDOTHELIAL-CELLS | AGALSIDASE-ALPHA | MICE | Microscopy, Confocal | alpha-Galactosidase - therapeutic use | Fibroblasts - enzymology | Myocardium - enzymology | Biopsy | Humans | Middle Aged | Cells, Cultured | Male | alpha-Galactosidase - metabolism | Fabry Disease - therapy | Genetic Therapy - methods | Original
Pathology | Medicine & Public Health | α-Galactosidase A deficiency | Enzyme replacement therapy | Persistent storage | Enzyme targeting | Clearance of storage lysosomes | PROGENITOR CELLS | persistent storage | enzyme replacement therapy | EFFICACY | SAFETY | LYSOSOMAL STORAGE | clearance of storage lysosomes | PATHOLOGY | alpha-galactosidase A deficiency | enzyme targeting | ENZYME REPLACEMENT | THERAPY | COLOCALIZATION | ENDOTHELIAL-CELLS | AGALSIDASE-ALPHA | MICE | Microscopy, Confocal | alpha-Galactosidase - therapeutic use | Fibroblasts - enzymology | Myocardium - enzymology | Biopsy | Humans | Middle Aged | Cells, Cultured | Male | alpha-Galactosidase - metabolism | Fabry Disease - therapy | Genetic Therapy - methods | Original
Journal Article
Molecular and Cellular Biochemistry, ISSN 0300-8177, 08/2010, Volume 341, Issue 1-2, p. 51
Human acid [alpha]-glucosidase (GAA, EC 3.2.1.20) is a lysosomal enzyme that belongs to the glycoside hydrolase family 31 (GH31) and catalyses the hydrolysis...
Hydrolysis | Glucose metabolism | Caenorhabditis elegans | Amylases | RNA | Glycogen | Analysis | Genomics | Proteins | Enzymes | Nematodes | Phylogenetics | Biochemistry | Bioinformatics | Metabolic disorders
Hydrolysis | Glucose metabolism | Caenorhabditis elegans | Amylases | RNA | Glycogen | Analysis | Genomics | Proteins | Enzymes | Nematodes | Phylogenetics | Biochemistry | Bioinformatics | Metabolic disorders
Journal Article
American Journal of Medical Genetics Part A, ISSN 1552-4825, 04/2009, Volume 149A, Issue 4, pp. 613 - 621
Prosaposin deficiency (pSap‐d) and saposin B deficiency (SapB‐d) are both lipid storage disorders caused by mutations in the PSAP gene that codes for the 65–70...
prosaposin | metachromatic leukodystrophy | sphingolipid activator proteins | PSAP gene | mass spectrometry | urinary lipids | saposin deficiency | Metachromatic leukodystrophy | Urinary lipids | Saposin deficiency | Sphingolipid activator proteins | Mass spectrometry | Prosaposin | GAUCHER-DISEASE PATIENT | STORAGE DISEASE | TANDEM MASS-SPECTROMETRY | CERAMIDE | QUANTITATIVE-DETERMINATION | A DEFICIENCY | PROTEIN-DEFICIENCY | CODING REGION | GENETICS & HEREDITY | ACCUMULATION | D DOMAIN | Sequence Deletion | RNA Splice Sites - genetics | Humans | Child, Preschool | Saposins - genetics | Sphingolipids - urine | Infant | Male | Brain - abnormalities | Codon, Nonsense | Homozygote | Leukodystrophy, Metachromatic - genetics | Magnetic Resonance Imaging | Leukodystrophy, Metachromatic - metabolism | DNA Mutational Analysis | Brain - pathology | Heterozygote | Mutation | Saposins - deficiency | Child | Leukodystrophy, Metachromatic - pathology | Infant, Newborn | Skin - pathology
prosaposin | metachromatic leukodystrophy | sphingolipid activator proteins | PSAP gene | mass spectrometry | urinary lipids | saposin deficiency | Metachromatic leukodystrophy | Urinary lipids | Saposin deficiency | Sphingolipid activator proteins | Mass spectrometry | Prosaposin | GAUCHER-DISEASE PATIENT | STORAGE DISEASE | TANDEM MASS-SPECTROMETRY | CERAMIDE | QUANTITATIVE-DETERMINATION | A DEFICIENCY | PROTEIN-DEFICIENCY | CODING REGION | GENETICS & HEREDITY | ACCUMULATION | D DOMAIN | Sequence Deletion | RNA Splice Sites - genetics | Humans | Child, Preschool | Saposins - genetics | Sphingolipids - urine | Infant | Male | Brain - abnormalities | Codon, Nonsense | Homozygote | Leukodystrophy, Metachromatic - genetics | Magnetic Resonance Imaging | Leukodystrophy, Metachromatic - metabolism | DNA Mutational Analysis | Brain - pathology | Heterozygote | Mutation | Saposins - deficiency | Child | Leukodystrophy, Metachromatic - pathology | Infant, Newborn | Skin - pathology
Journal Article
Nephrology Dialysis Transplantation, ISSN 0931-0509, 1/2007, Volume 22, Issue 1, pp. 179 - 186
Background. Fabry disease (FD) is a genetic disorder characterized by accumulation of trihexosylceramide in lysosomes of various tissues leading to multiorgan...
Fabry disease | End-stage renal disease | α-galactosidase A | Haemodialysis | Enzyme replacement therapy | Blood spot screening | STORAGE | DIAGNOSIS | enzyme replacement therapy | haemodialysis | end-stage renal disease | ALPHA-GALACTOSIDASE-A | DIALYSIS | TRANSPLANTATION | ENZYME | alpha-galactosidase A | UROLOGY & NEPHROLOGY | blood spot screening | Humans | Middle Aged | Renal Dialysis - methods | Spectrometry, Fluorescence | Male | alpha-Galactosidase - chemistry | Czech Republic | Fabry Disease - blood | Lysosomes - metabolism | Pedigree | Adult | Female | Protein Conformation | Aged | Fabry Disease - therapy | Enzymes - therapeutic use | Fabry Disease - diagnosis
Fabry disease | End-stage renal disease | α-galactosidase A | Haemodialysis | Enzyme replacement therapy | Blood spot screening | STORAGE | DIAGNOSIS | enzyme replacement therapy | haemodialysis | end-stage renal disease | ALPHA-GALACTOSIDASE-A | DIALYSIS | TRANSPLANTATION | ENZYME | alpha-galactosidase A | UROLOGY & NEPHROLOGY | blood spot screening | Humans | Middle Aged | Renal Dialysis - methods | Spectrometry, Fluorescence | Male | alpha-Galactosidase - chemistry | Czech Republic | Fabry Disease - blood | Lysosomes - metabolism | Pedigree | Adult | Female | Protein Conformation | Aged | Fabry Disease - therapy | Enzymes - therapeutic use | Fabry Disease - diagnosis
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 2017, Volume 105, pp. 257 - 270
Abstract Mucolipidosis type IV (MLIV) is a lysosomal storage disease exhibiting progressive intellectual disability, motor impairment, and premature death....
Neurology | small molecule therapy | mucolipidosis type IV | lysosomal storage disease | Purkinje cells | glycosphingolipids | miglustat | mucolipin-1
Neurology | small molecule therapy | mucolipidosis type IV | lysosomal storage disease | Purkinje cells | glycosphingolipids | miglustat | mucolipin-1
Journal Article
Molecular and Cellular Biochemistry, ISSN 0300-8177, 8/2010, Volume 341, Issue 1, pp. 51 - 63
Human acid α-glucosidase (GAA, EC 3.2.1.20) is a lysosomal enzyme that belongs to the glycoside hydrolase family 31 (GH31) and catalyses the hydrolysis of...
Life Sciences | Biochemistry, general | Glycogen storage disease type II | α-Glucosidase | GH31 family | Caenorhabditis elegans | Oncology | Medical Biochemistry | Cardiology | Caenorhabditis elegans | MALTASE-GLUCOAMYLASE | ASPERGILLUS-NIGER | POMPE-DISEASE | GLYCOSIDASE | SPECIFICITY | ACTIVE-SITE | LYSOSOMAL STORAGE DISORDERS | IDENTIFICATION | CELL BIOLOGY | alpha-Glucosidase | INTERMEDIATE | INHIBITORS | Acarbose - pharmacology | Glycoside Hydrolase Inhibitors | Catalytic Domain | Computational Biology - methods | Caenorhabditis elegans Proteins - chemistry | Humans | Phylogeny | alpha-Glucosidases - genetics | Sequence Alignment | Animals | Caenorhabditis elegans Proteins - antagonists & inhibitors | Caenorhabditis elegans Proteins - genetics | alpha-Glucosidases - chemistry
Life Sciences | Biochemistry, general | Glycogen storage disease type II | α-Glucosidase | GH31 family | Caenorhabditis elegans | Oncology | Medical Biochemistry | Cardiology | Caenorhabditis elegans | MALTASE-GLUCOAMYLASE | ASPERGILLUS-NIGER | POMPE-DISEASE | GLYCOSIDASE | SPECIFICITY | ACTIVE-SITE | LYSOSOMAL STORAGE DISORDERS | IDENTIFICATION | CELL BIOLOGY | alpha-Glucosidase | INTERMEDIATE | INHIBITORS | Acarbose - pharmacology | Glycoside Hydrolase Inhibitors | Catalytic Domain | Computational Biology - methods | Caenorhabditis elegans Proteins - chemistry | Humans | Phylogeny | alpha-Glucosidases - genetics | Sequence Alignment | Animals | Caenorhabditis elegans Proteins - antagonists & inhibitors | Caenorhabditis elegans Proteins - genetics | alpha-Glucosidases - chemistry
Journal Article
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 03/2015, Volume 407, Issue 8, p. 2283
Electronic supplementary material
Immunohistochemistry | Usage | Physiological aspects | Sphingolipids | Health aspects | Mass spectrometry | Fabry's disease | Methods
Immunohistochemistry | Usage | Physiological aspects | Sphingolipids | Health aspects | Mass spectrometry | Fabry's disease | Methods
Journal Article
12.
Full Text
Assessment of n-butyl-deoxynojirimycin as a therapeutic option for mucolipidosis type IV
Molecular Genetics and Metabolism, ISSN 1096-7192, 02/2016, Volume 117, Issue 2, pp. S29 - S29
Journal Article
BMC Cell Biology, ISSN 1471-2121, 01/2005, Volume 6, Issue 1, pp. 5 - 5
Human alpha-galactosidase A (alpha-GAL) and alpha-N-acetylgalactosaminidase (alpha-NAGA) are presumed to share a common ancestor. Deficiencies of these enzymes...
alpha-Galactosidase - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Caenorhabditis elegans Proteins - metabolism | Lysosomes | Molecular Sequence Data | alpha-Galactosidase - metabolism | alpha-N-Acetylgalactosaminidase - chemistry | Phylogeny | Sequence Analysis, DNA | Sequence Homology, Nucleic Acid | Proteins | Sequence Alignment | alpha-N-Acetylgalactosaminidase - metabolism | Animals | Base Sequence | Cloning, Molecular | Structural Homology, Protein | alpha-N-Acetylgalactosaminidase - genetics | Caenorhabditis elegans Proteins - genetics | Evolution, Molecular
alpha-Galactosidase - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Caenorhabditis elegans Proteins - metabolism | Lysosomes | Molecular Sequence Data | alpha-Galactosidase - metabolism | alpha-N-Acetylgalactosaminidase - chemistry | Phylogeny | Sequence Analysis, DNA | Sequence Homology, Nucleic Acid | Proteins | Sequence Alignment | alpha-N-Acetylgalactosaminidase - metabolism | Animals | Base Sequence | Cloning, Molecular | Structural Homology, Protein | alpha-N-Acetylgalactosaminidase - genetics | Caenorhabditis elegans Proteins - genetics | Evolution, Molecular
Journal Article
Glycobiology, ISSN 0959-6658, 06/2018, Volume 28, Issue 6, pp. 382 - 391
Blood group B glycosphingolipids (B-GSLs) are substrates of the lysosomal alpha-galactosidase A (AGAL). Similar to its major substrate-globotriaosylceramide...
Fabry disease | Gb3Cer | pancreas | blood group B antigens | ceroid | LOCALIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHENOTYPE | GROUP ANTIGENS | SPHINGOLIPIDS | CERAMIDE | DEFICIENCY | ABO | BETA-CELL FUNCTION | GLYCOSPHINGOLIPIDS | LIQUID-CHROMATOGRAPHY | Acinar Cells - metabolism | Acinar Cells - ultrastructure | Galactose - metabolism | Galactose - analysis | Humans | Middle Aged | ABO Blood-Group System - metabolism | Male | Pancreas - metabolism | Case-Control Studies | Fabry Disease - pathology | Insulin-Secreting Cells - ultrastructure | Fabry Disease - blood | Insulin-Secreting Cells - metabolism | Pancreas - ultrastructure | Fabry Disease - metabolism | Glycosphingolipids - metabolism | Glycosphingolipids - chemistry
Fabry disease | Gb3Cer | pancreas | blood group B antigens | ceroid | LOCALIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHENOTYPE | GROUP ANTIGENS | SPHINGOLIPIDS | CERAMIDE | DEFICIENCY | ABO | BETA-CELL FUNCTION | GLYCOSPHINGOLIPIDS | LIQUID-CHROMATOGRAPHY | Acinar Cells - metabolism | Acinar Cells - ultrastructure | Galactose - metabolism | Galactose - analysis | Humans | Middle Aged | ABO Blood-Group System - metabolism | Male | Pancreas - metabolism | Case-Control Studies | Fabry Disease - pathology | Insulin-Secreting Cells - ultrastructure | Fabry Disease - blood | Insulin-Secreting Cells - metabolism | Pancreas - ultrastructure | Fabry Disease - metabolism | Glycosphingolipids - metabolism | Glycosphingolipids - chemistry
Journal Article
Molecular and Cellular Biochemistry, ISSN 0300-8177, 08/2010, Volume 341, Issue 1-2, pp. 51 - 63
Human acid a-glucosidase (GAA, EC 3.2.1.20) is a lysosomal enzyme that belongs to the glycoside hydrolase family 31 (GH31) and catalyses the hydrolysis of...
Journal Article
Virchows Archiv, ISSN 0945-6317, 06/2008, Volume 452, Issue 6, p. 651
The function and intracellular delivery of enzyme therapeutics for Fabry disease were studied in cultured fibroblasts and in the biopsied tissues of two male...
Comparative analysis | Enzymes
Comparative analysis | Enzymes
Journal Article
Neurobiology of Disease, ISSN 0969-9961, 09/2017, Volume 105, pp. 257 - 270
Mucolipidosis type IV (MLIV) is a lysosomal storage disease exhibiting progressive intellectual disability, motor impairment, and premature death. There is...
Mucolipidosis type IV | Glycosphingolipids | Mucolipin-1 | Purkinje cells | Small molecule therapy | Miglustat | Lysosomal storage disease | CHOLESTEROL | EXOCYTOSIS | LYSOSOMAL STORAGE | GANGLIOSIDES | SUBSTRATE REDUCTION THERAPY | NEUROSCIENCES | MIGLUSTAT THERAPY | GENE | DISEASE | MUTATIONS | Cell Count | Antigens, CD - metabolism | 1-Deoxynojirimycin - therapeutic use | Exploratory Behavior - drug effects | 1-Deoxynojirimycin - analogs & derivatives | Lipid Metabolism - genetics | Transient Receptor Potential Channels - metabolism | Purkinje Cells - drug effects | Gliosis - etiology | Disease Models, Animal | Mice, Inbred C57BL | Mice, Transgenic | Mucolipidoses - genetics | Psychomotor Performance - drug effects | Enzyme Inhibitors - therapeutic use | Cerebellum - pathology | Nerve Tissue Proteins - metabolism | Mucolipidoses - complications | Mucolipidoses - pathology | Animals | Transient Receptor Potential Channels - genetics | Movement Disorders - etiology | Lipid Metabolism - drug effects | Gliosis - drug therapy | Mice | Purkinje Cells - pathology | Retina - pathology | Movement Disorders - drug therapy | Cell death | Mass spectrometry | Analysis
Mucolipidosis type IV | Glycosphingolipids | Mucolipin-1 | Purkinje cells | Small molecule therapy | Miglustat | Lysosomal storage disease | CHOLESTEROL | EXOCYTOSIS | LYSOSOMAL STORAGE | GANGLIOSIDES | SUBSTRATE REDUCTION THERAPY | NEUROSCIENCES | MIGLUSTAT THERAPY | GENE | DISEASE | MUTATIONS | Cell Count | Antigens, CD - metabolism | 1-Deoxynojirimycin - therapeutic use | Exploratory Behavior - drug effects | 1-Deoxynojirimycin - analogs & derivatives | Lipid Metabolism - genetics | Transient Receptor Potential Channels - metabolism | Purkinje Cells - drug effects | Gliosis - etiology | Disease Models, Animal | Mice, Inbred C57BL | Mice, Transgenic | Mucolipidoses - genetics | Psychomotor Performance - drug effects | Enzyme Inhibitors - therapeutic use | Cerebellum - pathology | Nerve Tissue Proteins - metabolism | Mucolipidoses - complications | Mucolipidoses - pathology | Animals | Transient Receptor Potential Channels - genetics | Movement Disorders - etiology | Lipid Metabolism - drug effects | Gliosis - drug therapy | Mice | Purkinje Cells - pathology | Retina - pathology | Movement Disorders - drug therapy | Cell death | Mass spectrometry | Analysis
Journal Article
Analytical and Bioanalytical Chemistry, ISSN 1618-2642, 12/2014, Volume 407, Issue 8, pp. 2283 - 2291
Fabry disease is an X-linked lysosomal storage disease due to deficient alpha-galactosidase A (alpha-Gal A) activity and the resultant lysosomal accumulation...
Fabry disease | Glycosphingolipids | Quantitation | Kidney | Mass spectrometry imaging | STORAGE | CHEMISTRY, ANALYTICAL | MALDI-TOF | HEMIZYGOTES | BIOCHEMICAL RESEARCH METHODS | URINARY | GALACTOSIDASE | REPLACEMENT | GENE | GLOBOTRIAOSYLCERAMIDE | Sphingolipids - chemistry | alpha-Galactosidase - genetics | Fabry Disease - genetics | Humans | Sphingolipids - metabolism | alpha-Galactosidase - metabolism | Fabry Disease - enzymology | Immunochemistry | Mice, Knockout | Kidney - metabolism | Animals | Fabry Disease - metabolism | Mass Spectrometry | Kidney - chemistry | Mice | Disease Models, Animal | Spatial distribution | Kidneys | Mathematical analysis | Imaging | Organs | Blood vessels | Lipids | Mass spectrometry
Fabry disease | Glycosphingolipids | Quantitation | Kidney | Mass spectrometry imaging | STORAGE | CHEMISTRY, ANALYTICAL | MALDI-TOF | HEMIZYGOTES | BIOCHEMICAL RESEARCH METHODS | URINARY | GALACTOSIDASE | REPLACEMENT | GENE | GLOBOTRIAOSYLCERAMIDE | Sphingolipids - chemistry | alpha-Galactosidase - genetics | Fabry Disease - genetics | Humans | Sphingolipids - metabolism | alpha-Galactosidase - metabolism | Fabry Disease - enzymology | Immunochemistry | Mice, Knockout | Kidney - metabolism | Animals | Fabry Disease - metabolism | Mass Spectrometry | Kidney - chemistry | Mice | Disease Models, Animal | Spatial distribution | Kidneys | Mathematical analysis | Imaging | Organs | Blood vessels | Lipids | Mass spectrometry
Journal Article