acid-phosphatase and Glycogen-Storage-Disease

Topics: Acid Phosphatase; Acid-Base Equilibrium; Chediak-Higashi Syndrome; Cytoplasm; Diffuse Cerebral Sclerosis of Schilder; Gaucher Disease; Genes, Recessive; Glycogen Storage Disease; Humans; Hydrolases; Lipidoses; Lysosomes; Metabolism, Inborn Errors; Niemann-Pick Diseases

Topics: Abortion, Induced; Acid Phosphatase; Adrenal Hyperplasia, Congenital; Amnion; Amniotic Fluid; Carbohydrate Metabolism, Inborn Errors; Congenital Abnormalities; Counseling; Culture Techniques; Cystic Fibrosis; Economics, Medical; Ethics, Medical; Female; Fetal Diseases; Fibroblasts; Genetic Diseases, Inborn; Glycogen Storage Disease; Heterozygote; Homozygote; Humans; Lysosomes; Mannose; Marfan Syndrome; Methods; Mucopolysaccharidoses; Muscular Dystrophies; Porphyrias; Pregnancy; Punctures; Xeroderma Pigmentosum

Muscle cultures from patients with infantile and later-onset acid maltase deficiency (AMD) and from unaffected controls were studied immunocytochemically with anti-acid maltase (anti-AM) antibodies and fluorescein-labeled goat anti-rabbit IgG second antibody. In control muscle cells, an intense granular distribution of staining was seen, consistent with lysosomal localization of AM. Cultured muscle cells from two patients with infantile AMD (Pompe's disease) did not fluoresce, whereas cells from two patients with AMD of later onset did fluoresce, showing a distribution similar to that of controls.

Topics: Acid Phosphatase; Adult; alpha-Glucosidases; Child, Preschool; Culture Techniques; Fluorescent Antibody Technique; Glucan 1,4-alpha-Glucosidase; Glucosidases; Glycogen Storage Disease; Glycogen Storage Disease Type II; Histocytochemistry; Humans; Infant, Newborn; Male; Muscles

The pathology of canine glycogen storage disease type II (acid alpha-glucosidase deficiency, GSD II) was studied in three genetically related Lapland dogs and compared to the pathology of human GSD II (McKusick 23230). Canine GSD II closely parallels the infantile form of the human disease, except for the presence of oesophageal dilatation. Generalized glycogen storage particularly affected muscular tissues (skeletal, oesophageal, cardiac and smooth muscle). The altered cells showed glycogen accumulation in the cytosol and in autophagic membrane-bound vacuoles (glycogenosomes). They also showed increased acid phosphatase activity consistent with the lysosomal nature of this storage disorder. The cytopathology in canine and human GSD II appears to evolve from segregation of glycogen during regular cellular autophagy, phagolysosomal accumulation of the undigested glycogen, and eventually rupture of distended glycogenosomes. This study indicates that the usefulness of canine GSD II as an animal model of human disease, extends to the area of pathogenesis.

Topics: Acid Phosphatase; Animals; Brain; Cytoplasm; Disease Models, Animal; Dogs; Esophagus; Female; Glycogen; Glycogen Storage Disease; Glycogen Storage Disease Type II; Humans; Kidney; Liver; Male; Microscopy, Electron; Muscle, Smooth; Muscles; Myocardium; Neurons; Spinal Cord; Vacuoles

A 19-month-old girl with moderate hypotonia was studied. Histochemical and electronmicroscopic findings revealed that many skeletal muscle fibers contained an excess amount of glycogen. The phosphorylase reaction was normalized only after activation with 5' AMP. Biochemical studies showed an increased glycogen content and decreased activities of phosphorylase "a" and an active form of phosphorylase kinase, whereas activities of total phosphorylase, total phosphorylase kinase, and cyclic AMP-dependent protein kinase were all in the normal range. Thus, phosphorylase kinase in the patient's muscle seemed to be a variant form, which was activated partially under the physiologic condition. This condition may be inherited as an X-linked recessive trait.

Topics: Acid Phosphatase; Cyclic AMP; Female; Glycogen; Glycogen Storage Disease; Humans; Infant, Newborn; Muscle Hypotonia; Muscles; Phosphorylase Kinase

Two unrelated 16-year-old boys had mental retardation, cardiomegaly, and proximal myopathy. One also had hepatomegaly. Histochemistry and electronmicroscopy of muscle biopsies showed lysosomal glycogen storage resembling acid maltase deficiency. Biochemical studies of skeletal muscle showed increased content of glycogen of normal structure; acid alpha-glucosidase activity in both urine and muscle was normal. Other enzymes of glycogen metabolism were also normal. The cause of this apparently generalized glycogenosis with no demonstrable enzyme defect is unknown.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adolescent; alpha-Glucosidases; Glycogen; Glycogen Storage Disease; Histocytochemistry; Humans; Lysosomes; Male; Microscopy, Electron; Muscles; NADH Tetrazolium Reductase

Feeding of fructose for 7 days has been morphometrically shown to induce a SER-reduction and an accumulation of glycogen in rat liver cells. This hypothetical model "glycogenosis" is investigated with histochemical methods.. Rats are given a solution of 60% fructose in water as only nutritional source. Controls are given a solution of 60% glucose in water, an isocaloric Altromin-R-standard diet and an Altromin-R-standard diet ad libitum. Reversion of fructose induced metabolic changes is investigated by a 7 days fructose diet followed by an 1-4 days Altromin-R-standard diet ad libitum. Glycogen and glycogen metabolizing enzymes are demonstrated after a 7 days diet and in the course of an 1-7 days fructose diet.. Feeding of fructose leads to a high glycogen content, combined with a high activity of glycogen-phosphorylase and glucose-6-phosphatase in the liver parenchyma. Glycogen-synthetase activity increases during the first 4 days and then it drops to a low level. A pathological alteration of liver cell metabolism seems to be improbable, for all fructose induced changes are reversibel after 2 days of Altromin-R-standard diet. Glucose-6-phosphatase, as a marker-enzyme of the smooth endoplasmatic reticulum, is discussed to become activated by disruption of SER membranes due to fructose.

Topics: Acid Phosphatase; Animals; Disease Models, Animal; Endoplasmic Reticulum; Fructose; Glucose; Glucose-6-Phosphatase; Glycogen Storage Disease; Glycogen Storage Disease Type I; Glycogen Synthase; Histocytochemistry; Liver; Liver Glycogen; Male; Phosphorylases; Rats

We established muscle-tissue cultures from biopsy of a patient with adult-onset acid maltase deficiency. Morphologically and biochemically, the newly grown fibers of the cultured muscle showed the same abnormalities as those of the biopsied muscle. Light microscopy showed multiple vacuoles filled with acid-phosphatase-positive material; on ultrastructural examination there was abnormal accumulation of glycogen in membrane-bound sacs (secondary lysosomes), some of which also contained dark membranous of homogeneous material. Acid maltase (pH 4.0), a lysosomal enzyme, was undetectable in either cultured or biopsied muscle by maltose hydrolysis, whereas acid phosphatase, also a lysosomal enzyme, was increased in both sources of muscle cells. Cultured muscle fibers demonstrate the same morphologic and biochemical abnormalities characteristic of biopsied muscle, supporting the concept of a biochemically distinct primary myopathy in man.

Topics: Acid Phosphatase; Adult; Age Factors; Creatine Kinase; Culture Techniques; Glucosidases; Glycogen; Glycogen Storage Disease; Humans; Lysosomes; Male; Muscles; Muscular Diseases

In two new cases of centronuclear myopathy, histochemical findings included failure to differentiate fiber type with oxidative enzymes, the presence of core glycogenosis, and core acid phosphatase activity. Fluorescence microscopy demonstrated autofluorescent lipochrome in fiber centers and nonspecific fiber injury in some immunofluorescent preparations. Electron microscopical findings included the observation of unusually small myofibrils arrayed between central nuclei.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adolescent; Adult; Cell Nucleus; Cholinesterases; Complement System Proteins; Electron Transport Complex IV; Female; Fluorescent Antibody Technique; Fructose-Bisphosphate Aldolase; Glycogen Storage Disease; Glycogen Synthase; Histocytochemistry; Humans; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Male; Microscopy, Electron; Microscopy, Fluorescence; Mitochondria, Muscle; Myofibrils; Neuromuscular Diseases; Phosphorylases; Succinate Dehydrogenase

Topics: Acid Phosphatase; Biopsy; Child; Glucosidases; Glucosyltransferases; Glucuronidase; Glycogen; Glycogen Storage Disease; Hexosaminidases; Histocytochemistry; Humans; Intellectual Disability; Male; Microscopy; Microscopy, Electron; Muscles; Muscular Atrophy; Muscular Diseases

Topics: Acid Phosphatase; Adenoma; Adenosine Triphosphatases; Aged; Female; Glucosephosphate Dehydrogenase; Glucosyltransferases; Glycogen; Glycogen Storage Disease; Humans; Leucyl Aminopeptidase; Microscopy, Electron; Nucleotidases; Phosphotransferases; Polysaccharides; Skin; Succinate Dehydrogenase; Sweat Gland Neoplasms

Topics: Acid Phosphatase; Adult; Amniocentesis; Cardiomegaly; Female; Fetal Diseases; Genes, Recessive; Glucose; Glucosidases; Glycogen Storage Disease; Heart Defects, Congenital; Heart Diseases; Heterozygote; Humans; Infant, Newborn; Lectins; Lymphocytes; Male; Myocardium; Pregnancy; Prenatal Diagnosis; Syndrome; Time Factors

Topics: Acid Phosphatase; Axons; Brain; Brain Chemistry; Cell Nucleus; Cytoplasm; Glucosidases; Glucosyltransferases; Glycogen; Glycogen Storage Disease; Heart Diseases; Humans; Infant; Lysosomes; Male; Microscopy; Microscopy, Electron; Mitochondria; Myelin Sheath; Nervous System; Nervous System Diseases; Neuroglia; Neurons; Peripheral Nerves; Schwann Cells; Spinal Cord

Cortisone causes a marked increase in the activity of liver acid alpha-glucosidase 2h after injection into male Wistar rats. Studies on rat liver tissue slices, isolated lysosomes and cultured skin fibroblasts have demonstrated similar elevations of acid alpha-glucosidase activity after incubation with cortisone. Cortisone-treated human liver tissue, obtained by needle biopsy, also shows an increase in acid alpha-glucosidase activity. Neutral alpha-glucosidase activity was not stimulated by cortisone in vivo or in liver slices.

Topics: Acid Phosphatase; Animals; Biopsy; Carbon Isotopes; Cortisone; Culture Media; Culture Techniques; Enzyme Activation; Fibroblasts; Glucose; Glucosidases; Glutamate Dehydrogenase; Glycogen Storage Disease; Humans; Liver; Lysosomes; Male; Proteins; Rats; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bone Marrow; Bone Marrow Cells; Cats; Citric Acid Cycle; Cytoplasm; Dihydrolipoamide Dehydrogenase; Gluconeogenesis; Glucose; Glucosephosphate Dehydrogenase; Glycerolphosphate Dehydrogenase; Glycogen; Glycogen Storage Disease; Glycolysis; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Leukocytes; Lipid Metabolism; Lipoproteins; Malate Dehydrogenase; Megakaryocytes; Mice; Mitochondria; Neutrophils; Nucleoproteins; Oxidative Phosphorylation; Oxidoreductases; Proteins

Topics: Acid Phosphatase; Carrier State; Glucosidases; Glycogen Storage Disease; Humans; Infant; Lectins; Lymphocytes; Lysosomes; Metabolism, Inborn Errors

Topics: Acid Phosphatase; Culture Techniques; Fibroblasts; Genes; Glucosidases; Glycogen Storage Disease; Humans; Infant; Leukocytes; Male; Muramidase; Skin

Topics: Acid Phosphatase; Child; Diffuse Cerebral Sclerosis of Schilder; Glycogen Storage Disease; Humans; Leukodystrophy, Metachromatic; Mucopolysaccharidosis I; Niemann-Pick Diseases; Sulfatases; Tuberous Sclerosis; Urine

Topics: Acid Phosphatase; Alkaline Phosphatase; Diagnosis, Differential; Glucosidases; Glycogen Storage Disease; Glycogen Storage Disease Type I; Humans; Liver; Liver Cirrhosis; Liver Glycogen; Phosphorylase Kinase

Topics: Acid Phosphatase; Amylases; Chromatography, Paper; Glucose-6-Phosphatase; Glucosidases; Glucosyltransferases; Glycogen Storage Disease; Humans; In Vitro Techniques; Liver; Maltose; Oligosaccharides; Subcellular Fractions

Topics: Acid Phosphatase; Child; Electron Transport Complex IV; Electrons; Glucosephosphate Dehydrogenase; Glucosidases; Glycogen Storage Disease; Glycoside Hydrolases; Histocytochemistry; Humans; Liver; Liver Glycogen; Microscopy; Microscopy, Electron; Pathology; Proteins