Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

beta-glucuronidase deficiency is an extremely rare disorder which is known to have a considerable phenotypic variation. A survey of the clinical findings in 19 previously reported patients with mucopolysaccharidosis VII is presented together with the results of clinical and biochemical studies in two further patients. Because a similar clinical picture is present in a heterozygotic sister it is doubted whether all signs and symptoms can be attributed to the beta-glucuronidase deficiency. The probability of a concomitant disorder is discussed. Diagnosis was made both by demonstration of the deficiency in plasma and leucocytes, and by means of hair root analysis. The phenotypic variation and the fact that increased levels of glycosaminoglycans were not found in the urine of the two patients lead to the suggestion that in certain cases a correct diagnosis may be missed if the beta-glucuronidase activity in plasma and leucocytes is not determined and only routine urine investigation is performed as a screening for a mucopolysaccharidosis. Hair root analysis may be a useful method to measure the beta-glucuronidase activity.
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PMID:Phenotypic expression in mucopolysaccharidosis VII. 311 9

We studied two cases of beta-glucuronidase deficiency. One patient's disease was present at birth and the other patient's disease appeared in early childhood. The symptoms observed in both patients, although of differing severity, included peculiar facies, cloudy cornea, hepatosplenomegaly, hernia, kyphosis, recurrent infections, short stature, and developmental delay, as well as increased excretion of urinary chondroitin sulfate A/C and decreased levels of beta-glucuronidase activity. We reviewed all of the reported cases and examined the biochemical and clinical heterogeneity observed in this disorder.
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PMID:Beta-glucuronidase deficiency. A heterogeneous mucopolysaccharidosis. 315 9

GUSB, the gene for beta-glucuronidase, has been localized to the proximal long arm of chromosome 7 between 7q11.2 and 7q22. Deficiency of beta-glucuronidase results in mucopolysaccharidosis type VII (MPS VII, Sly syndrome). The enzymatic defect has been demonstrated in cultured skin fibroblasts, leukocytes and serum of affected patients. An 8-yr-old boy presented with manifestations similar to MPS VII (mental retardation, short stature, "coarse" facial appearance, mild skeletal involvement and recurrent lower respiratory tract infection) but other, discrepant abnormalities, e.g., bilateral iris colobomata and cleft palate. Normal activity of beta-glucuronidase was found in the patient's leukocytes. Chromosome analysis disclosed an interstitial deletion of 7q with one breakpoint at the interface between bands 11.22 and 11.23 and the other breakpoint within band 21.1. DNA from this patient's leukocytes was analyzed for dosage of GUSB sequences. This locus appeared to be present at the normal diploid level. These findings suggest that GUSB is not in the portion of chromosome 7 deleted in our case, narrowing the smallest region of overlap to 7q21.1----7q22. We therefore assign the beta-glucuronidase gene to 7q21.1----7q22.
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PMID:Deletion mapping of the beta-glucuronidase gene. 337 95

Content of glycosaminoglycans and beta-glucuronidase activity were measured in leukocytes, blood serum and urine of patients with rheumatoid arthritis. Concentration of glycosaminoglycans was increased in blood serum and urine of the patients. The most distinct increase as compared with healthy persons in content of these substances was found in leukocytes of the patients with joint form of rheumatoid arthritis. Activity of beta-glucuronidase was also elevated in cells of peripheral blood, whereas content of protein was decreased in these cells. The enzymatic activity was reduced in the fraction of polymorphonuclear leukocytes of the patients as shown by estimation of the activity per 10(6) cells after fractionation using the Ficoll-verografin procedure. Deficiency of beta-glucuronidase activity in polymorphonuclear leukocytes appears to be among the factors responsible for excess of glycosaminoglycans in blood serum and urine of the patients as well as for chronic inflammation under conditions of rheumatoid arthritis.
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PMID:[Glycosaminoglycans and beta-glucuronidase in peripheral blood cells and biological fluids of patients with rheumatoid arthritis]. 342 Aug 12

Mucopolysaccharidosis type VII is a lysosomal storage disease resulting from a deficiency of beta-glucuronidase (BG) activity. To facilitate the investigation of mutation in the disease and provide molecular diagnostic tools for affected families, we have isolated human BG cDNA clones. The SV40-transformed human fibroblast cDNA library of Okayama and Berg [Mol. Cell. Biol. 3 (1982) 280-289] was screened with a fragment of a murine BG cDNA clone (pGUS-1). The 17 human cDNA clones (pHUG) isolated were identical by restriction mapping, varying only in length. The pHUG clones show 80% DNA sequence homology with pGUS-1 in a 198-bp PvuII-SstI restriction fragment. Both pGUS-1 and the pHUG clones contained an open reading frame (ORF) throughout the sequenced region with a predicted amino acid sequence homology of 73%. Expression in Escherichia coli of a 1150-bp fragment of pHUG-1 subcloned in pUC9 resulted in an isopropyl-thio-beta-galactoside (IPTG)-inducible 35-kDal fusion protein which was specifically immunoprecipitated by goat anti-human BG immunoglobulin G (IgG). This evidence provides direct confirmation that the pHUG cDNA clones correspond to human BG.
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PMID:Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase. 392 35

This report describes a third mucopolysaccharidosis in animals: canine mucopolysaccharidosis VII. The affected dog was the offspring of a father-daughter mating. Weakness in the rear legs was evident at 8 weeks of age and became progressively worse. He had a large head, a shortened maxilla, and corneal granularities. Most joints were extremely lax, easily subluxated, with joint capsules that were swollen and fluctuant. The dog was alert and had apparently normal pain perception. At 13 months of age, there was radiographic evidence of extensive skeletal disease including bilateral femoral head luxation, abnormalities in the shape and density of the carpal and tarsal bones, radiolucent lesions of the epiphyseal regions of most long bones, and cervical vertebral dysplasia and platyspondylia. The electrophoretic pattern of precipitated glycosaminoglycans indicated a predominance of chondroitin sulfate. The animal died suddenly from gastric dilatation. There was generalized hepatomegaly, thickening of the atrioventricular heart valves, and generalized polyarthropathy. Vacuolated cytoplasm was observed in hepatocytes, keratocytes, fibroblasts, chondrocytes and cells of the synovial membrane, retinal pigment epithelium, and cardiac valves. Neurons had cytoplasmic vacuoles. Electron microscopy demonstrated membrane-bound cytoplasmic inclusions in polymorphonuclear leukocytes, hepatocytes, synovium, heart valves and spleen. The activities of 12 lysosomal hydrolases were determined in liver from the affected and control dogs: beta-glucuronidase (EC 3.2.1.31), beta-hexosaminidases A and B (EC 3.2.1.30), alpha-hexosaminidase (EC 3.2.1.-), alpha-L-iduronidase (EC 3.2.1.76), alpha-galactosidase A (EC 3.2.1.22), beta-galactosidase (EC 3.2.1.23), arylsulfatases A and B (EC 3.1.6.1), acid alpha-mannosidase (EC 3.2.1.24), acid beta-mannosidase (EC 3.2.1.25), and N-acetyl-D-galactosamine-6-sulfate sulfatase (EC 3.1.6.-).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Beta-glucuronidase deficiency in a dog: a model of human mucopolysaccharidosis VII. 643 80

This study reports a case of type VII mucopolysaccharidosis (beta-glucuronidase deficiency) presenting as lethal hydrops fetalis. Skin fibroblast cultures established postmortem revealed deficient beta-glucuronidase activity. Mucopolysaccharides were stored in various cells of the brain, heart, kidney, liver, and spleen. The stages of maturation of the bones, kidneys, and brain were discrepant, the brain being the least mature organ. A delay in central nervous system maturation may account for psychomotor retardation in some patients with this enzyme deficiency.
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PMID:Postmortem observations on beta-glucuronidase deficiency presenting as hydrops fetalis. 668 50

A beta-glucuronidase deficiency found in serum, leukocytes and fibroblasts and an increased [35S]sulphate incorporation in fibroblasts led us to diagnose two cases of type VII mucopolysaccharidosis in one family. In spite of the wide distribution of activities in serum from controls, decreased beta-glucuronidase activity allowed us to demonstrate the heterozygous status of the parents and two other children. Following these studies, and antenatal diagnosis was performed when the mother was pregnant again; amniotic fluid and cultured amniotic cells were used for enzyme activity determination. A heterozygous fetus was suspected and confirmed after birth. The reliability of various biological materials for enzymatic diagnosis and existence of genetic variants in the normal population are discussed.
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PMID:Beta-glucuronidase deficiency: enzyme studies in an affected family and prenatal diagnosis. 679 58

The morphologic, cytochemical, and ultrastructural pathology of the blood and bone marrow of an infant with Mucopolysaccharidosis Type VII (MPS VII) is reported. The neutrophils, monocytes, basophils, and eosinophils contained prominent granulation of the Alder-Reilly type. The lymphocytes, plasma cells, osteoblasts, and macrophages contained cytoplasmic inclusions surrounded by clear vacuoles. Cytochemically, the granulocytes, monocytes, and lymphocytes were negative for beta-glucuronidase, negative or weakly metachromatic with toluidine blue, and positive for acid phosphatase. Macrophages were negative with toluidine blue. A normal staining pattern was present with myeloperoxidase and periodic acid-Schiff (PAS). Ultrastructural studies showed abnormal vacuoles in neutrophils, basophils, eosinophils, monocytes, lymphocytes, plasma cells, and macrophages. Occasional vacuoles contained Ruthenium Red positive material and confirmed the presence of acid mucopolysaccharide in these cells. This report confirms previously described abnormalities in peripheral blood cells in MPS VII, demonstrates additional abnormalities in bone marrow, and reports cytochemical reactions in leukocytes in MPS VII.
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PMID:Mucopolysaccharidosis type VII. A morphologic, cytochemical, and ultrastructural study of the blood and bone marrow. 681 36

We present evidence that a 480G-->A transition in the coding region of the beta-glucuronidase gene, which results in an aspartic-acid-to-asparagine substitution at amino acid position 152 (D152N), produces a pseudodeficiency allele (GUSBp) that leads to greatly reduced levels of beta-glucuronidase activity without apparent deleterious consequences. The 480G-->A mutation was found initially in the pseudodeficient mother of a child with mucopolysaccharidosis VII (MPSVII), but it was not on her disease-causing allele, which carried the L176F mutation. The 480G-->A change was also present in an unrelated individual with another MPSVII allele who had unusually low beta-glucuronidase activity, but whose clinical symptoms were probably unrelated to beta-glucuronidase deficiency. This individual also had an R357X mutation, probably on his second allele. We screened 100 unrelated normal individuals for the 480G-->A mutation with a PCR method and detected one carrier. Reduced beta-glucuronidase activity following transfection of COS cells with the D152N cDNA supported the causal relationship between the D152N allele and pseudodeficiency. The mutation reduced the fraction of expressed enzyme that was secreted. Pulse-chase experiments indicated that the reduced activity in COS cells was due to accelerated intracellular turnover of the D152N enzyme. They also suggested that a potential glycosylation site created by the mutation is utilized in approximately 50% of the enzyme expressed.
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PMID:A pseudodeficiency allele (D152N) of the human beta-glucuronidase gene. 757 38


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