acid-phosphatase and Metabolism--Inborn-Errors

Topics: Acid Phosphatase; Alkaline Phosphatase; alpha-Amylases; Biliary Tract Diseases; Clinical Enzyme Tests; Enzymes; Female; gamma-Glutamyltransferase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Lipase; Liver Diseases; Metabolism, Inborn Errors; Myocardial Infarction; Nucleotidases; Pancreas; Transaminases; Uterine Neoplasms

Topics: Acid Phosphatase; Adrenal Hyperplasia, Congenital; Amino Acid Metabolism, Inborn Errors; Amniocentesis; Amniotic Fluid; Blood Chemical Analysis; Carbohydrate Metabolism, Inborn Errors; Chromosome Aberrations; Chromosome Disorders; Cystic Fibrosis; Endoscopy; Female; Fetoscopy; Fetus; Genetic Diseases, Inborn; Humans; Lesch-Nyhan Syndrome; Lipid Metabolism, Inborn Errors; Lysosomes; Metabolism, Inborn Errors; Mucopolysaccharidoses; Pregnancy; Prenatal Diagnosis; Radiography; Ultrasonography; Urine

Topics: Acid Phosphatase; Cells, Cultured; Culture Media; Dactinomycin; Enzyme Induction; Fibroblasts; Humans; Leukocytes; Lysosomes; Metabolism, Inborn Errors; Prednisolone; Puromycin

Topics: Acid Phosphatase; Amino Acid Metabolism, Inborn Errors; Amniotic Fluid; Anemia, Hemolytic, Congenital Nonspherocytic; Anemia, Sickle Cell; Carbohydrate Metabolism, Inborn Errors; Cells, Cultured; Female; Glycolipids; Glycosaminoglycans; Heterozygote; Humans; Lipid Metabolism, Inborn Errors; Lipidoses; Metabolism, Inborn Errors; Muscular Atrophy; Pregnancy; Prenatal Diagnosis; Purine-Pyrimidine Metabolism, Inborn Errors; Transferases; Xanthomatosis

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: Acid Phosphatase; Clinical Enzyme Tests; Evaluation Studies as Topic; Genetic Diseases, Inborn; Glucosidases; Hemagglutination Tests; Heterozygote; Homozygote; Humans; Lectins; Leukocytes; Lymphocytes; Metabolism, Inborn Errors; Methods; Neutrophils; Nitrogen; Pressure; Stimulation, Chemical

Topics: Acid Phosphatase; Alleles; Anemia, Hemolytic, Congenital; Enzymes; Erythrocytes; Genetic Variation; Glucosephosphate Dehydrogenase; Humans; Isoenzymes; Metabolism, Inborn Errors; Molecular Biology; Mutation

Topics: Acid Phosphatase; Alleles; Cholinesterases; DNA; Enzymes; Genetic Code; Glucosephosphate Dehydrogenase Deficiency; Humans; Lesch-Nyhan Syndrome; Metabolism, Inborn Errors; Molecular Biology; Mutation; Pentosyltransferases; Polymorphism, Genetic; Pyruvate Kinase

Topics: Acid Phosphatase; Amino Acids; Citrulline; DNA; Erythrocytes; Genetic Diseases, Inborn; Glucosephosphate Dehydrogenase; Hemoglobins; Humans; Infant, Newborn; Metabolism, Inborn Errors

Electron-microscopic and cytochemical studies were carried out on tissues of NCTR-BALB/c mice. These mice are affected with a neurovisceral genetic disorder involving excessive tissue accumulation of lipid. Distinctive polymorphic intracellular inclusions, bounded by a membrane and containing lamellated bodies, were found in many cells of liver, spleen, lung, kidney, intestine, lymph nodes, and brain. The inclusions transformed reticuloendothelial cells into massive foam cells. Acid phosphatase cytochemical studies performed on sections of liver demonstrated that the inclusions were lysosomes. Fixation of liver in the presence of digitonin produced "spicules" in the inclusions characteristic of digitonin-cholesterol complexes. Clefts of cholesterol crystals were seen in the inclusions in liver, spleen, and lung. We conclude that the NCTR-BALB/c mice are affected by a lysosome lipid storage disease and that cholesterol is a major storage product.

Topics: Acid Phosphatase; Animals; Cholesterol; Female; Histocytochemistry; Lipid Metabolism; Liver; Lysosomes; Male; Metabolism, Inborn Errors; Mice; Mice, Mutant Strains; Microscopy, Electron; Spleen

The activity of acid hydrolases was studied in serum from patients with mucolipidosis (II and III) and other lysosomal disorders. In mucolipidosis II and III all hydrolases examined except alpha-glucosidase, beta-glucosidase and acid phosphatase were greatly increased. High values for beta-galactosidase were seen in mucopolysaccharidosis types I and II, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. N-Acetyl-beta-glucosaminidase activity was high in mucopolysaccharidosis types I, II, III and Gaucher's disease. The activity of beta-glucuronidase was increased in mucopolysaccharidosis types I, II and III, Gaucher's disease, juvenile amaurotic idiocy and metachromatic leucodystrophy. Acid phosphatase had increased activity only in Gaucher's disease. In several lysosomal storage disorders no increased values could be found. It is suggested that high values in serum from patients with lysosomal storage disorders (not including mucolipidosis II and III) may depend upon liver cell damage, which disturbs the clearing of acid hydrolases from serum.

Topics: Acid Phosphatase; Gaucher Disease; Glycoside Hydrolases; Humans; Leukodystrophy, Metachromatic; Lipidoses; Lysosomes; Metabolism, Inborn Errors; Mucopolysaccharidoses

Optimal assay conditions are described for plasma alpha-galactosidase, beta-glactosidase, beta-glucuronidase, alpha-mannosidase, alpha-glucosidase, N-acetyl-beta-glucosaminidase, alpha-fucosidase, N-acetyl-alpha-glucosaminidase, acid phosphatase and arylsulphatase A. The levels of these activities in normal adults and children, and the stabilities of the activities on storage at -20 degrees C or 4 degrees C, are reported. The levels of these enzymic activities in plasma from patients with Fabry, Pompe, Sanfilippo A, Sanfilippo B, Tay Sachs and Hunter diseases, GM1-gangliosidosis and metachromatic leucodystrophy are described, and the possibility of using plasma hydrolase activities in the diagnosis of these conditions is discussed.

Topics: Acid Phosphatase; Adolescent; Adult; Age Factors; Cerebroside-Sulfatase; Child; Child, Preschool; Glycoside Hydrolases; Humans; Infant; Kinetics; Lysosomes; Metabolism, Inborn Errors; Sulfatases

Lysosomal hydrolases participate substantially in the degradation of all classes of biological macromolecules. They act physiologically within the lysosome. The enzymes are either primarily included within primary lysosomes or are transported to these cell organelles after secretion and subsequent adsorptive pinocytosis. The involvement of these enzymes in a variety of pathological conditions can be understood on the basis of the known functions of lysosomal hydrolases. Inactivity of one or several of the enzymes causes lysosomal storage disorders. Similar metabolic consequences are found when the enzymes are unable to be concentrated within the lysosome. Lysosomal hydrolases participate, furthermore, in the pathogenesis of numerous diseases. A distinction can be made between lysosomal overload, pathologically-increased enzyme secretion into the extracellular space, and a release of lysosomal enzymes into the cytosol.

Topics: Acid Phosphatase; Cytosol; Extracellular Space; Genes; Glycoproteins; Heparitin Sulfate; Humans; Hydrolases; Lysosomes; Metabolism, Inborn Errors; Mucopolysaccharidoses; Mutation; Pinocytosis; Sphingolipidoses

Untreated cases of lichen planus have been studied by histochemical techniques. The acid phosphatase reaction in the transitional zone has been quantitatively estimated and compared with the adjacent relatively normal epidermis. It was found that despite a thickened and accentuated granular layer as seen by routine histological methods there was a marked reduction in the intensity of the acid phosphatase reaction. The glucose-6-phosphate dehydrogenase reaction was marked in the upper layers of the epidermis in active lesions of lichen planus. This is similar to psoriasis, but different from normal human epidermis. The suggestion by other authors that lichen planus is an inborn error of metabolism is discussed. The dendritic cells of the epidermis as studied by the ATPase reaction are virtually absent in regions of active lichen planus and the possible significance of this is mentioned. The horny layer gives a dense reaction for phospholipids in lichen planus and this is similar to psoriatic keratin. The significance of this finding is considered.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Dendrites; Glucosephosphate Dehydrogenase; Histocytochemistry; Humans; Keratins; Lichen Planus; Metabolism, Inborn Errors; Naphthols; Phospholipids; Skin

Topics: Abnormalities, Multiple; Acid Phosphatase; Arabinose; Corneal Opacity; Cytoplasmic Granules; Fibroblasts; Galactosidases; Glucosidases; Glucuronidase; Glycosaminoglycans; Glycoside Hydrolases; Hexosaminidases; Humans; Intellectual Disability; Mannose; Metabolism, Inborn Errors; Mucopolysaccharidoses; Phosphoric Diester Hydrolases; Retinitis Pigmentosa; Skin

Topics: Acid Phosphatase; Cell Line; Cells, Cultured; Female; Fibroblasts; Fucose; Glycosaminoglycans; Glycoside Hydrolases; Hexosaminidases; Humans; Inclusion Bodies; L-Lactate Dehydrogenase; Malate Dehydrogenase; Male; Metabolism, Inborn Errors; Phenols; Sulfatases; Sulfoglycosphingolipids; Sulfur Radioisotopes

Topics: Acid Phosphatase; Adult; Alleles; Blood Group Antigens; Blood Protein Electrophoresis; Child; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Family Characteristics; Female; Germany, West; Homozygote; Humans; Male; Metabolism, Inborn Errors; Paternity; Phenotype

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; alpha 1-Antitrypsin Deficiency; Aspartate Aminotransferases; Blood Proteins; Carbon Radioisotopes; Ceruloplasmin; Child; Densitometry; Electrophoresis, Disc; Electrophoresis, Starch Gel; Female; Galactose; Galactosidases; Glucosidases; Glycoproteins; Humans; L-Lactate Dehydrogenase; Liver; Liver Cirrhosis; Metabolism, Inborn Errors; Microscopy, Electron; Sialic Acids; Transferases; Ultracentrifugation

Topics: Acid Phosphatase; Amniotic Fluid; Female; Fetus; Galactosidases; Gestational Age; Glucosidases; Glycoside Hydrolases; Hexosaminidases; Humans; Lysosomes; Metabolism, Inborn Errors; Pregnancy; Prenatal Diagnosis; Proteins; Specimen Handling

Topics: Acid Phosphatase; Amniotic Fluid; Animals; Cattle; Cells, Cultured; Female; Galactosidases; Glucuronidase; Glycoside Hydrolases; Heterozygote; Hexosaminidases; Homozygote; Humans; Leukocytes; Male; Metabolism, Inborn Errors; Methods; Mucopolysaccharidoses; Pedigree; Skin; Sulfatases

Topics: Acid Phosphatase; Adult; Child, Preschool; Chromosome Aberrations; Chromosome Mapping; Chromosomes, Human, 1-3; Electrophoresis, Starch Gel; Female; Genes; Genotype; Humans; Karyotyping; Male; Metabolism, Inborn Errors; Middle Aged; Pedigree; Phenotype

Topics: Abnormalities, Multiple; Acid Phosphatase; Amniotic Fluid; Female; Fetus; Galactosidases; Glucosidases; Glucuronidase; Hexosaminidases; Humans; Lysosomes; Metabolism, Inborn Errors; Pregnancy; Prenatal Diagnosis; Sulfatases

Topics: Acid Phosphatase; Animals; Brain; Cattle; Cattle Diseases; Galactosidases; Gangliosides; Liver; Metabolism, Inborn Errors; Proteins

Large amounts of glycogen accumulate in rat skeletal muscle fibers during the late fetal stages and are mobilized in the first postnatal days. This glycogen depletion is relatively slow in the immature leg muscles, in which extensive deposits are still found 24 hr after birth and, to some extent, persist until the 3rd day. In the more differentiated psoas muscle and especially in the diaphragm, the glycogen stores are completely mobilized already during the early hours. Section of the sciatic nerve 3 days before birth or within the first 2 hr after delivery does not affect glycogen depletion in the leg muscles. Neonatal glycogenolysis in rat muscle fibers takes place largely by segregation and digestion of glycogen particles in autophagic vacuoles. These vacuoles: (a) are not seen in fetal muscle fibers or at later postnatal stages, but appear concomitantly with the process of glycogen depletion and disappear shortly afterwards; (b) are prematurely formed in skeletal muscles of fetuses at term treated with glucagon; (c) contain almost exclusively glycogen particles and no other recognizable cell constituents; (d) have a double or, more often, single limiting membrane and originate apparently from flattened sacs sequestering glycogen masses; (e) are generally found to contain reaction product in preparations incubated from demonstration of acid phosphatase activity. The findings emphasize the role of the lysosomal system in the physiological process of postnatal glycogen mobilization and appear relevant in the interpretation of type II glycogen storage disease.

Topics: Acid Phosphatase; Animals; Animals, Newborn; Diaphragm; Female; Fetus; Gestational Age; Glucagon; Glycogen; Golgi Apparatus; Histocytochemistry; Inclusion Bodies; Injections, Subcutaneous; Lysosomes; Metabolism, Inborn Errors; Methods; Microscopy, Electron; Muscles; Myofibrils; Pregnancy; Rats; Rats, Inbred Strains; Ribosomes; Sarcolemma; Sarcoplasmic Reticulum; Sciatic Nerve; Time Factors

Topics: Acid Phosphatase; Adenosine Diphosphate; Adenosine Triphosphate; Adult; Anemia, Hemolytic, Congenital; Anemia, Hemolytic, Congenital Nonspherocytic; Child, Preschool; Chromium Radioisotopes; Cyclic AMP; Erythrocytes; Female; Glucosephosphate Dehydrogenase; Glutathione Reductase; Glycolysis; Humans; Infant; Infant, Newborn; Male; Metabolism, Inborn Errors; Pedigree; Phosphogluconate Dehydrogenase; Potassium; Pregnancy; Pyruvate Kinase; Splenectomy

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Arm; Bone and Bones; Bone Diseases, Developmental; Child; Child, Preschool; Collagen; Diagnosis, Differential; Female; Haversian System; Humans; Infant; Infant, Newborn; Leg; Male; Metabolism, Inborn Errors; Osteitis Deformans; Pelvic Bones; Radiography; Skull; Syndrome

Ceramidase activity could not be demonstrated in the kidney and cerebellum from a deceased patient with Farber's disease, whereas the activities of six control acid hydrolase enzymes appeared normal. This enzyme defect presumably accounts for the accumulation that has been described in two patients and may represent the biochemical basis of this disorder.

Topics: Acid Phosphatase; Adult; Carbon Isotopes; Ceramides; Cerebellum; Cerebrosides; Child; Child, Preschool; Congenital Abnormalities; Female; Galactose; Galactosidases; Glucose; Glycoside Hydrolases; Heart Defects, Congenital; Hexosaminidases; Humans; Hydrolases; Infant; Infant, Newborn; Intellectual Disability; Kidney; Lipidoses; Liver Cirrhosis, Biliary; Male; Metabolism, Inborn Errors; Neuraminidase; Pigmentation Disorders; Respiratory Distress Syndrome, Newborn

Topics: Acid Phosphatase; Cells, Cultured; Culture Media; Diploidy; Fibroblasts; Gaucher Disease; Glucosidases; Histocytochemistry; Humans; In Vitro Techniques; Lipid Metabolism, Inborn Errors; Lysosomes; Metabolism, Inborn Errors; Skin; Sulfatases

Topics: Acid Phosphatase; Aging; Alkaline Phosphatase; Animals; Central Nervous System; Central Nervous System Diseases; Cerebrosides; Cholesterol; Demyelinating Diseases; Disease Models, Animal; Female; Genes, Recessive; Genotype; Lipids; Male; Metabolism, Inborn Errors; Mice; Mutation; Phosphoric Monoester Hydrolases; Thyroid Function Tests; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Amino Acid Metabolism, Inborn Errors; Amniotic Fluid; Catalase; Cell Line; Culture Techniques; Cystic Fibrosis; Cystinosis; Diffuse Cerebral Sclerosis of Schilder; Humans; Immunologic Deficiency Syndromes; Leukocytes; Lipid Metabolism, Inborn Errors; Metabolism, Inborn Errors; Methods; Mucopolysaccharidoses; Mucopolysaccharidosis IV; Muscular Dystrophies; Myotonia; Refsum Disease; Skin

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

Topics: Abortion, Therapeutic; Acid Phosphatase; Adult; Amniotic Fluid; Brain; Child; Culture Media; Culture Techniques; Electrophoresis; Female; Fetal Diseases; Fetus; Fibroblasts; Glucosephosphate Dehydrogenase; Glucosidases; Glucuronidase; Heterozygote; Humans; Infant; Infant, Newborn; Kidney; L-Lactate Dehydrogenase; Lectins; Liver; Lymphocyte Activation; Lymphocytes; Lysosomes; Male; Metabolism, Inborn Errors; Pregnancy; Spleen

Topics: Abortion, Therapeutic; Acid Phosphatase; Female; Fetal Diseases; Humans; Hydrogen-Ion Concentration; Infant, Newborn; Lysosomes; Metabolism, Inborn Errors; Pregnancy

Topics: Acid Phosphatase; Alkaline Phosphatase; Cell Nucleus; Cytogenetics; Eosinophils; Hematologic Diseases; Histocytochemistry; Humans; Metabolism, Inborn Errors; Microscopy, Electron; Mutation; Peroxidases; Phospholipids; Staining and Labeling

Topics: Acid Phosphatase; Alkaline Phosphatase; Amino Acids; Amnion; Amniotic Fluid; Arginase; Arginine; Caproates; Carboxy-Lyases; Female; Galactose; Glucosephosphate Dehydrogenase; Glucosidases; Glucuronidase; Humans; L-Lactate Dehydrogenase; Ligases; Metabolism, Inborn Errors; Mixed Function Oxygenases; Nucleotidyltransferases; Oxidoreductases; Phosphogluconate Dehydrogenase; Pregnancy; Pregnancy Complications; Punctures; Transaminases; Transferases

Topics: Acid Phosphatase; Alkaline Phosphatase; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Female; Humans; Isoenzymes; Liver Diseases; Male; Metabolism, Inborn Errors; Muscular Diseases; Myocardial Infarction; Transaminases

Topics: Acid Phosphatase; Animals; Catalase; Female; Histocytochemistry; Hypolipidemic Agents; Lipids; Liver; Male; Metabolism, Inborn Errors; Microscopy, Electron; Microsomes; Peroxidases; Rats; Urate Oxidase

Topics: Acid Phosphatase; Adult; Anemia; Cholesterol; Corneal Opacity; Electrophoresis; Esters; Female; Humans; Lysophosphatidylcholines; Metabolism, Inborn Errors; Phospholipids; Plasma; Proteinuria; Transferases; Triglycerides

Topics: Acid Phosphatase; Adolescent; Adult; Child; Child, Preschool; Female; Fructose-Bisphosphate Aldolase; Genetic Diseases, Inborn; Humans; Infant; L-Lactate Dehydrogenase; Male; Metabolism, Inborn Errors; Middle Aged; Osteopetrosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Humans; Hypophosphatasia; Metabolism, Inborn Errors; Phosphates