PubMed:10561464 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":73},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":74,"end":338},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":339,"end":451},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":452,"end":607},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":608,"end":758},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":759,"end":862},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":863,"end":1016},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1017,"end":1113},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1114,"end":1278},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1279,"end":1467},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":73},"obj":"Sentence"},{"id":"T2","span":{"begin":74,"end":338},"obj":"Sentence"},{"id":"T3","span":{"begin":339,"end":451},"obj":"Sentence"},{"id":"T4","span":{"begin":452,"end":607},"obj":"Sentence"},{"id":"T5","span":{"begin":608,"end":758},"obj":"Sentence"},{"id":"T6","span":{"begin":759,"end":862},"obj":"Sentence"},{"id":"T7","span":{"begin":863,"end":1016},"obj":"Sentence"},{"id":"T8","span":{"begin":1017,"end":1113},"obj":"Sentence"},{"id":"T9","span":{"begin":1114,"end":1278},"obj":"Sentence"},{"id":"T10","span":{"begin":1279,"end":1467},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":73},"obj":"Sentence"},{"id":"T2","span":{"begin":74,"end":338},"obj":"Sentence"},{"id":"T3","span":{"begin":339,"end":451},"obj":"Sentence"},{"id":"T4","span":{"begin":452,"end":607},"obj":"Sentence"},{"id":"T5","span":{"begin":608,"end":758},"obj":"Sentence"},{"id":"T6","span":{"begin":759,"end":862},"obj":"Sentence"},{"id":"T7","span":{"begin":863,"end":1016},"obj":"Sentence"},{"id":"T8","span":{"begin":1017,"end":1113},"obj":"Sentence"},{"id":"T9","span":{"begin":1114,"end":1278},"obj":"Sentence"},{"id":"T10","span":{"begin":1279,"end":1467},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":231,"end":246},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"T2","span":{"begin":863,"end":878},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"T3","span":{"begin":1154,"end":1169},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":452,"end":457},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":831,"end":838},"obj":"http://purl.obolibrary.org/obo/MAT_0000122"},{"id":"T3","span":{"begin":893,"end":898},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"T4","span":{"begin":903,"end":908},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T5","span":{"begin":1034,"end":1039},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T6","span":{"begin":1044,"end":1049},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":74,"end":95},"obj":"HP_0008155"},{"id":"T2","span":{"begin":151,"end":170},"obj":"HP_0000007"},{"id":"T3","span":{"begin":843,"end":861},"obj":"HP_0001433"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":18,"end":39},"obj":"http://purl.bioontology.org/ontology/ICD10/E76.3"},{"id":"T2","span":{"begin":74,"end":95},"obj":"http://purl.bioontology.org/ontology/ICD10/E76.3"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":151,"end":160},"obj":"FMAID:74406"},{"id":"_T2","span":{"begin":151,"end":160},"obj":"FMAID:176862"},{"id":"_T3","span":{"begin":161,"end":170},"obj":"FMAID:211293"},{"id":"_T4","span":{"begin":172,"end":181},"obj":"FMAID:63836"},{"id":"_T5","span":{"begin":172,"end":181},"obj":"FMAID:162299"},{"id":"_T6","span":{"begin":231,"end":238},"obj":"FMAID:67110"},{"id":"_T7","span":{"begin":231,"end":238},"obj":"FMAID:165191"},{"id":"_T8","span":{"begin":231,"end":246},"obj":"FMAID:63023"},{"id":"_T9","span":{"begin":231,"end":246},"obj":"FMAID:167405"},{"id":"_T10","span":{"begin":247,"end":259},"obj":"FMAID:55654"},{"id":"_T11","span":{"begin":247,"end":259},"obj":"FMAID:198193"},{"id":"_T12","span":{"begin":286,"end":295},"obj":"FMAID:63836"},{"id":"_T13","span":{"begin":286,"end":295},"obj":"FMAID:162299"},{"id":"_T14","span":{"begin":303,"end":310},"obj":"FMAID:67110"},{"id":"_T15","span":{"begin":303,"end":310},"obj":"FMAID:165191"},{"id":"_T16","span":{"begin":452,"end":457},"obj":"FMAID:146514"},{"id":"_T17","span":{"begin":452,"end":457},"obj":"FMAID:50801"},{"id":"_T18","span":{"begin":476,"end":483},"obj":"FMAID:54527"},{"id":"_T19","span":{"begin":476,"end":483},"obj":"FMAID:166033"},{"id":"_T20","span":{"begin":476,"end":483},"obj":"FMAID:150783"},{"id":"_T21","span":{"begin":499,"end":508},"obj":"FMAID:63836"},{"id":"_T22","span":{"begin":499,"end":508},"obj":"FMAID:162299"},{"id":"_T23","span":{"begin":521,"end":531},"obj":"FMAID:167608"},{"id":"_T24","span":{"begin":521,"end":531},"obj":"FMAID:93573"},{"id":"_T25","span":{"begin":521,"end":531},"obj":"FMAID:30322"},{"id":"_T26","span":{"begin":521,"end":531},"obj":"FMAID:7145"},{"id":"_T27","span":{"begin":591,"end":595},"obj":"FMAID:256134"},{"id":"_T28","span":{"begin":591,"end":595},"obj":"FMAID:256135"},{"id":"_T29","span":{"begin":647,"end":656},"obj":"FMAID:162299"},{"id":"_T30","span":{"begin":647,"end":656},"obj":"FMAID:63836"},{"id":"_T31","span":{"begin":647,"end":665},"obj":"FMAID:226190"},{"id":"_T32","span":{"begin":647,"end":665},"obj":"FMAID:226191"},{"id":"_T33","span":{"begin":660,"end":665},"obj":"FMAID:169002"},{"id":"_T34","span":{"begin":660,"end":665},"obj":"FMAID:68646"},{"id":"_T35","span":{"begin":680,"end":687},"obj":"FMAID:256050"},{"id":"_T36","span":{"begin":804,"end":807},"obj":"FMAID:276692"},{"id":"_T58","span":{"begin":1191,"end":1209},"obj":"FMAID:167395"},{"id":"_T37","span":{"begin":831,"end":838},"obj":"FMAID:106284"},{"id":"_T38","span":{"begin":863,"end":870},"obj":"FMAID:67110"},{"id":"_T39","span":{"begin":863,"end":870},"obj":"FMAID:165191"},{"id":"_T40","span":{"begin":863,"end":878},"obj":"FMAID:63023"},{"id":"_T41","span":{"begin":863,"end":878},"obj":"FMAID:167405"},{"id":"_T42","span":{"begin":893,"end":898},"obj":"FMAID:226785"},{"id":"_T43","span":{"begin":903,"end":908},"obj":"FMAID:50801"},{"id":"_T44","span":{"begin":903,"end":908},"obj":"FMAID:146514"},{"id":"_T45","span":{"begin":929,"end":940},"obj":"FMAID:82797"},{"id":"_T46","span":{"begin":929,"end":940},"obj":"FMAID:196792"},{"id":"_T47","span":{"begin":1034,"end":1039},"obj":"FMAID:93672"},{"id":"_T48","span":{"begin":1034,"end":1039},"obj":"FMAID:7197"},{"id":"_T49","span":{"begin":1044,"end":1049},"obj":"FMAID:146514"},{"id":"_T50","span":{"begin":1044,"end":1049},"obj":"FMAID:50801"},{"id":"_T51","span":{"begin":1044,"end":1058},"obj":"FMAID:206963"},{"id":"_T52","span":{"begin":1120,"end":1129},"obj":"FMAID:63836"},{"id":"_T53","span":{"begin":1120,"end":1129},"obj":"FMAID:162299"},{"id":"_T54","span":{"begin":1154,"end":1161},"obj":"FMAID:67110"},{"id":"_T55","span":{"begin":1154,"end":1161},"obj":"FMAID:165191"},{"id":"_T56","span":{"begin":1154,"end":1169},"obj":"FMAID:63023"},{"id":"_T57","span":{"begin":1154,"end":1169},"obj":"FMAID:167405"},{"id":"_T59","span":{"begin":1191,"end":1209},"obj":"FMAID:63011"},{"id":"_T60","span":{"begin":1383,"end":1390},"obj":"FMAID:178661"},{"id":"_T61","span":{"begin":1454,"end":1458},"obj":"FMAID:198663"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":151,"end":160},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/150701"},{"id":"T2","span":{"begin":399,"end":403},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T3","span":{"begin":442,"end":450},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/525814"},{"id":"T4","span":{"begin":536,"end":545},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/144547"},{"id":"T5","span":{"begin":660,"end":665},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T6","span":{"begin":669,"end":673},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T7","span":{"begin":680,"end":687},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T8","span":{"begin":794,"end":800},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/23017"},{"id":"T9","span":{"begin":1353,"end":1363},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0051235"},{"id":"T2","span":{"begin":608,"end":615},"obj":"http://purl.obolibrary.org/obo/GO_0051235"},{"id":"T3","span":{"begin":182,"end":189},"obj":"http://purl.obolibrary.org/obo/GO_0035732"},{"id":"T4","span":{"begin":608,"end":615},"obj":"http://purl.obolibrary.org/obo/GO_0035732"},{"id":"T5","span":{"begin":239,"end":246},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T6","span":{"begin":871,"end":878},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T7","span":{"begin":945,"end":952},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T8","span":{"begin":1162,"end":1169},"obj":"http://purl.obolibrary.org/obo/GO_0051923"},{"id":"T9","span":{"begin":804,"end":807},"obj":"http://purl.obolibrary.org/obo/GO_0007568"},{"id":"T10","span":{"begin":893,"end":898},"obj":"http://purl.obolibrary.org/obo/GO_0060073"},{"id":"T11","span":{"begin":972,"end":980},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T12","span":{"begin":1146,"end":1153},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T13","span":{"begin":1146,"end":1169},"obj":"http://purl.obolibrary.org/obo/GO_0030200"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":151,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0030849"},{"id":"T2","span":{"begin":172,"end":181},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T3","span":{"begin":286,"end":295},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T4","span":{"begin":499,"end":508},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T5","span":{"begin":647,"end":656},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T6","span":{"begin":521,"end":531},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T7","span":{"begin":660,"end":665},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":1433,"end":1437},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":680,"end":687},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T2","span":{"begin":893,"end":898},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"},{"id":"T3","span":{"begin":903,"end":908},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"T4","span":{"begin":1044,"end":1049},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"T5","span":{"begin":1034,"end":1039},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":172,"end":181},"obj":"http://edamontology.org/topic_0616"},{"id":"T2","span":{"begin":190,"end":197},"obj":"http://edamontology.org/topic_0634"},{"id":"T3","span":{"begin":286,"end":295},"obj":"http://edamontology.org/topic_0616"},{"id":"T4","span":{"begin":499,"end":508},"obj":"http://edamontology.org/topic_0616"},{"id":"T5","span":{"begin":647,"end":656},"obj":"http://edamontology.org/topic_0616"},{"id":"T6","span":{"begin":998,"end":1003},"obj":"http://edamontology.org/topic_2815"},{"id":"T7","span":{"begin":1120,"end":1129},"obj":"http://edamontology.org/topic_0616"},{"id":"T8","span":{"begin":1342,"end":1352},"obj":"http://edamontology.org/topic_0783"},{"id":"T9","span":{"begin":1367,"end":1374},"obj":"http://edamontology.org/topic_0634"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":411,"end":419},"obj":"http://edamontology.org/data_1255"},{"id":"T2","span":{"begin":953,"end":961},"obj":"http://edamontology.org/data_1756"},{"id":"T3","span":{"begin":1222,"end":1228},"obj":"http://edamontology.org/operation_3435"},{"id":"T4","span":{"begin":1342,"end":1352},"obj":"http://edamontology.org/data_3718"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":452,"end":457},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T2","span":{"begin":831,"end":838},"obj":"http://purl.obolibrary.org/obo/MAT_0000122"},{"id":"T3","span":{"begin":893,"end":898},"obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"T4","span":{"begin":903,"end":908},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"T5","span":{"begin":1034,"end":1039},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"T6","span":{"begin":1044,"end":1049},"obj":"http://purl.obolibrary.org/obo/MAT_0000098"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":231,"end":246},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":863,"end":878},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":1154,"end":1169},"obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":680,"end":687},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":452,"end":457},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":903,"end":908},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":1044,"end":1049},"obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":1034,"end":1039},"obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"PD-UBERON-AE-B_T6","span":{"begin":476,"end":483},"obj":"http://purl.obolibrary.org/obo/UBERON_2000602"},{"id":"PD-UBERON-AE-B_T7","span":{"begin":893,"end":898},"obj":"http://purl.obolibrary.org/obo/UBERON_0001088"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":18,"end":50},"obj":"Disease"},{"id":"T2","span":{"begin":18,"end":48},"obj":"Disease"},{"id":"T3","span":{"begin":52,"end":71},"obj":"Disease"},{"id":"T4","span":{"begin":74,"end":106},"obj":"Disease"},{"id":"T5","span":{"begin":74,"end":104},"obj":"Disease"},{"id":"T6","span":{"begin":108,"end":117},"obj":"Disease"},{"id":"T7","span":{"begin":119,"end":138},"obj":"Disease"},{"id":"T8","span":{"begin":172,"end":197},"obj":"Disease"},{"id":"T9","span":{"begin":429,"end":438},"obj":"Disease"},{"id":"T10","span":{"begin":1283,"end":1292},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0009655"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0018937"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0018937"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0009655"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0018937"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0009655"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0018937"},{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0002561"},{"id":"A9","pred":"mondo_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MONDO_0009655"},{"id":"A10","pred":"mondo_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MONDO_0009655"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":843,"end":861},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0001433"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":2,"end":7},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":370,"end":375},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":768,"end":772},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":998,"end":1003},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1293,"end":1298},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10088"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10090"},{"id":"A3","pred":"db_id","subj":"T3","obj":"10088"},{"id":"A4","pred":"db_id","subj":"T3","obj":"10090"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10088"},{"id":"A6","pred":"db_id","subj":"T6","obj":"9606"},{"id":"A7","pred":"db_id","subj":"T7","obj":"10088"},{"id":"A8","pred":"db_id","subj":"T7","obj":"10090"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":231,"end":246},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":863,"end":878},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":1154,"end":1169},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0086"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0086"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":452,"end":457},"obj":"Body_part"},{"id":"T2","span":{"begin":831,"end":838},"obj":"Body_part"},{"id":"T3","span":{"begin":893,"end":898},"obj":"Body_part"},{"id":"T4","span":{"begin":903,"end":908},"obj":"Body_part"},{"id":"T5","span":{"begin":1034,"end":1039},"obj":"Body_part"},{"id":"T6","span":{"begin":1044,"end":1049},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000122"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000058"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000098"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000097"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000098"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":452,"end":457},"obj":"Body_part"},{"id":"T3","span":{"begin":499,"end":508},"obj":"Body_part"},{"id":"T4","span":{"begin":647,"end":656},"obj":"Body_part"},{"id":"T5","span":{"begin":831,"end":838},"obj":"Body_part"},{"id":"T7","span":{"begin":893,"end":898},"obj":"Body_part"},{"id":"T8","span":{"begin":903,"end":908},"obj":"Body_part"},{"id":"T10","span":{"begin":1034,"end":1039},"obj":"Body_part"},{"id":"T11","span":{"begin":1044,"end":1049},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001255"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0018707"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0001088"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A9","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0000955"},{"id":"A12","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_6110636"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}

{"project":"Glycosmos15-CL","denotations":[{"id":"T1","span":{"begin":476,"end":483},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000540"}],"text":"A mouse model for mucopolysaccharidosis type III A (Sanfilippo syndrome).\nMucopolysaccharidosis type III A (MPS III A, Sanfilippo syndrome) is a rare, autosomal recessive, lysosomal storage disease characterized by accumulation of heparan sulfate secondary to defective function of the lysosomal enzyme heparan N- sulfatase (sulfamidase). Here we describe a spontaneous mouse mutant that replicates many of the features found in MPS III A in children. Brain sections revealed neurons with distended lysosomes filled with membranous and floccular materials with some having a classical zebra body morphology. Storage materials were also present in lysosomes of cells of many other tissues, and these often stained positively with periodic-acid Schiff reagent. Affected mice usually died at 7-10 months of age exhibiting a distended bladder and hepatosplenomegaly. Heparan sulfate isolated from urine and brain had nonreducing end glucosamine- N -sulfate residues that were digested with recombinant human sulfamidase. Enzyme assays of liver and brain extracts revealed a dramatic reduction in sulfamidase activity. Other lysosomal hydrolases that degrade heparan sulfate or other glycans and glycosaminoglycans were either normal, or were somewhat increased in specific activity. The MPS III A mouse provides an excellent model for evaluating pathogenic mechanisms of disease and for testing treatment strategies, including enzyme or cell replacement and gene therapy."}