PubMed:23811343 JSONTXT

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":2033,"end":2055},"obj":"gene:22856"},{"id":"T1","span":{"begin":2134,"end":2157},"obj":"disease:C0031117"},{"id":"T2","span":{"begin":2072,"end":2107},"obj":"gene:22856"},{"id":"T3","span":{"begin":2134,"end":2157},"obj":"disease:C0031117"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"Allie","denotations":[{"id":"SS1_23811343_0_0","span":{"begin":2,"end":24},"obj":"expanded"},{"id":"SS2_23811343_0_0","span":{"begin":26,"end":32},"obj":"abbr"}],"relations":[{"id":"AE1_23811343_0_0","pred":"abbreviatedTo","subj":"SS1_23811343_0_0","obj":"SS2_23811343_0_0"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"23811343-0#2#24#gene22856","span":{"begin":2,"end":24},"obj":"gene22856"},{"id":"23811343-0#26#32#gene22856","span":{"begin":26,"end":32},"obj":"gene22856"},{"id":"23811343-0#70#80#diseaseC0442874","span":{"begin":70,"end":80},"obj":"diseaseC0442874"},{"id":"23811343-11#103#125#gene22856","span":{"begin":2033,"end":2055},"obj":"gene22856"},{"id":"23811343-11#142#177#gene22856","span":{"begin":2072,"end":2107},"obj":"gene22856"},{"id":"23811343-11#204#227#diseaseC0031117","span":{"begin":2134,"end":2157},"obj":"diseaseC0031117"}],"relations":[{"id":"2#24#gene2285670#80#diseaseC0442874","pred":"associated_with","subj":"23811343-0#2#24#gene22856","obj":"23811343-0#70#80#diseaseC0442874"},{"id":"26#32#gene2285670#80#diseaseC0442874","pred":"associated_with","subj":"23811343-0#26#32#gene22856","obj":"23811343-0#70#80#diseaseC0442874"},{"id":"103#125#gene22856204#227#diseaseC0031117","pred":"associated_with","subj":"23811343-11#103#125#gene22856","obj":"23811343-11#204#227#diseaseC0031117"},{"id":"142#177#gene22856204#227#diseaseC0031117","pred":"associated_with","subj":"23811343-11#142#177#gene22856","obj":"23811343-11#204#227#diseaseC0031117"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"DisGeNET5_variant_disease","denotations":[{"id":"23811343-9#27#32#geners768947688","span":{"begin":1555,"end":1560},"obj":"geners768947688"},{"id":"23811343-9#60#70#diseaseC0442874","span":{"begin":1588,"end":1598},"obj":"diseaseC0442874"}],"relations":[{"id":"27#32#geners76894768860#70#diseaseC0442874","pred":"associated_with","subj":"23811343-9#27#32#geners768947688","obj":"23811343-9#60#70#diseaseC0442874"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":70,"end":80},"obj":"Disease"},{"id":"T2","span":{"begin":334,"end":344},"obj":"Disease"},{"id":"T3","span":{"begin":503,"end":513},"obj":"Disease"},{"id":"T4","span":{"begin":1588,"end":1598},"obj":"Disease"},{"id":"T5","span":{"begin":1831,"end":1854},"obj":"Disease"},{"id":"T6","span":{"begin":2134,"end":2157},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0003620"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0003620"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

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chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":2,"end":13},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":107,"end":118},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":147,"end":158},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":264,"end":275},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":405,"end":416},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":540,"end":551},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":573,"end":584},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":749,"end":760},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":808,"end":819},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":960,"end":971},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T11","span":{"begin":1081,"end":1092},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T12","span":{"begin":1133,"end":1144},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T13","span":{"begin":1179,"end":1190},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T14","span":{"begin":1285,"end":1296},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T15","span":{"begin":1370,"end":1381},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T16","span":{"begin":1402,"end":1413},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T17","span":{"begin":1453,"end":1464},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T18","span":{"begin":1532,"end":1543},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T19","span":{"begin":1625,"end":1636},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T20","span":{"begin":1726,"end":1737},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T21","span":{"begin":1757,"end":1768},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T22","span":{"begin":1948,"end":1959},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T23","span":{"begin":2033,"end":2044},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T24","span":{"begin":2060,"end":2071},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T25","span":{"begin":2208,"end":2219},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A11","pred":"glycoepitope_id","subj":"T11","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A12","pred":"glycoepitope_id","subj":"T12","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A13","pred":"glycoepitope_id","subj":"T13","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A14","pred":"glycoepitope_id","subj":"T14","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A15","pred":"glycoepitope_id","subj":"T15","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A16","pred":"glycoepitope_id","subj":"T16","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A17","pred":"glycoepitope_id","subj":"T17","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A18","pred":"glycoepitope_id","subj":"T18","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A19","pred":"glycoepitope_id","subj":"T19","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A20","pred":"glycoepitope_id","subj":"T20","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A21","pred":"glycoepitope_id","subj":"T21","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A22","pred":"glycoepitope_id","subj":"T22","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A23","pred":"glycoepitope_id","subj":"T23","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A24","pred":"glycoepitope_id","subj":"T24","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A25","pred":"glycoepitope_id","subj":"T25","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":70,"end":80},"obj":"Phenotype"},{"id":"T2","span":{"begin":334,"end":344},"obj":"Phenotype"},{"id":"T3","span":{"begin":503,"end":513},"obj":"Phenotype"},{"id":"T4","span":{"begin":1588,"end":1598},"obj":"Phenotype"},{"id":"T5","span":{"begin":1816,"end":1854},"obj":"Phenotype"},{"id":"T6","span":{"begin":2134,"end":2157},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0009830"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0009830"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0009830"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0009830"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0007133"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0009830"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":70,"end":80},"obj":"Disease"},{"id":"T2","span":{"begin":334,"end":344},"obj":"Disease"},{"id":"T3","span":{"begin":503,"end":513},"obj":"Disease"},{"id":"T4","span":{"begin":1588,"end":1598},"obj":"Disease"},{"id":"T5","span":{"begin":1831,"end":1854},"obj":"Disease"},{"id":"T6","span":{"begin":2134,"end":2157},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0005244"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0003620"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0003620"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":57,"end":64},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":490,"end":497},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1575,"end":1582},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":2111,"end":2129},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:2000032"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":2111,"end":2129},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_2000032"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":195},"obj":"Sentence"},{"id":"T2","span":{"begin":196,"end":207},"obj":"Sentence"},{"id":"T3","span":{"begin":208,"end":345},"obj":"Sentence"},{"id":"T4","span":{"begin":346,"end":469},"obj":"Sentence"},{"id":"T5","span":{"begin":470,"end":572},"obj":"Sentence"},{"id":"T6","span":{"begin":573,"end":776},"obj":"Sentence"},{"id":"T7","span":{"begin":777,"end":785},"obj":"Sentence"},{"id":"T8","span":{"begin":786,"end":874},"obj":"Sentence"},{"id":"T9","span":{"begin":875,"end":939},"obj":"Sentence"},{"id":"T10","span":{"begin":940,"end":948},"obj":"Sentence"},{"id":"T11","span":{"begin":949,"end":1112},"obj":"Sentence"},{"id":"T12","span":{"begin":1113,"end":1514},"obj":"Sentence"},{"id":"T13","span":{"begin":1515,"end":1527},"obj":"Sentence"},{"id":"T14","span":{"begin":1528,"end":1805},"obj":"Sentence"},{"id":"T15","span":{"begin":1806,"end":1907},"obj":"Sentence"},{"id":"T16","span":{"begin":1908,"end":1929},"obj":"Sentence"},{"id":"T17","span":{"begin":1930,"end":2235},"obj":"Sentence"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

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chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":2,"end":13},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":107,"end":118},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":147,"end":158},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":264,"end":275},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":405,"end":416},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":540,"end":551},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":573,"end":584},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":749,"end":760},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":808,"end":819},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":960,"end":971},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T11","span":{"begin":1081,"end":1092},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T12","span":{"begin":1133,"end":1144},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T13","span":{"begin":1179,"end":1190},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T14","span":{"begin":1285,"end":1296},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T15","span":{"begin":1370,"end":1381},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T16","span":{"begin":1402,"end":1413},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T17","span":{"begin":1453,"end":1464},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T18","span":{"begin":1532,"end":1543},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T19","span":{"begin":1625,"end":1636},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T20","span":{"begin":1726,"end":1737},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T21","span":{"begin":1757,"end":1768},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T22","span":{"begin":1948,"end":1959},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T23","span":{"begin":2033,"end":2044},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T24","span":{"begin":2060,"end":2071},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T25","span":{"begin":2208,"end":2219},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A11","pred":"glycoepitope_id","subj":"T11","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A12","pred":"glycoepitope_id","subj":"T12","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A13","pred":"glycoepitope_id","subj":"T13","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A14","pred":"glycoepitope_id","subj":"T14","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A15","pred":"glycoepitope_id","subj":"T15","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A16","pred":"glycoepitope_id","subj":"T16","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A17","pred":"glycoepitope_id","subj":"T17","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A18","pred":"glycoepitope_id","subj":"T18","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A19","pred":"glycoepitope_id","subj":"T19","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A20","pred":"glycoepitope_id","subj":"T20","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A21","pred":"glycoepitope_id","subj":"T21","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A22","pred":"glycoepitope_id","subj":"T22","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A23","pred":"glycoepitope_id","subj":"T23","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A24","pred":"glycoepitope_id","subj":"T24","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A25","pred":"glycoepitope_id","subj":"T25","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":57,"end":64},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":490,"end":497},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1575,"end":1582},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":2111,"end":2129},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_2000032"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":70,"end":80},"obj":"Phenotype"},{"id":"T2","span":{"begin":334,"end":344},"obj":"Phenotype"},{"id":"T3","span":{"begin":503,"end":513},"obj":"Phenotype"},{"id":"T4","span":{"begin":1588,"end":1598},"obj":"Phenotype"},{"id":"T5","span":{"begin":1816,"end":1854},"obj":"Phenotype"},{"id":"T6","span":{"begin":2134,"end":2157},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0009830"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0009830"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0009830"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"HP:0009830"},{"id":"A5","pred":"hp_id","subj":"T5","obj":"HP:0007133"},{"id":"A6","pred":"hp_id","subj":"T6","obj":"HP:0009830"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":2111,"end":2129},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:2000032"}],"text":"A chondroitin synthase-1 (ChSy-1) missense mutation in a patient with neuropathy impairs the elongation of chondroitin sulfate chains initiated by chondroitin N-acetylgalactosaminyltransferase-1.\nBACKGROUND: Previously, we identified two missense mutations in the chondroitin N-acetylgalactosaminyltransferase-1 gene in patients with neuropathy. These mutations are associated with a profound decrease in chondroitin N-acetylgalactosaminyltransferase-1 enzyme activity. Here, we describe a patient with neuropathy who is heterozygous for a chondroitin synthase-1 mutation. Chondroitin synthase-1 has two glycosyltransferase activities: it acts as a GlcUA and a GalNAc transferase and is responsible for adding repeated disaccharide units to growing chondroitin sulfate chains.\nMETHODS: Recombinant wild-type chondroitin synthase-1 enzyme and the F362S mutant were expressed. These enzymes and cells expressing them were then characterized.\nRESULTS: The mutant chondroitin synthase-1 protein retained approximately 50% of each glycosyltransferase activity relative to the wild-type chondroitin synthase-1 protein. Furthermore, unlike chondroitin polymerase comprised of wild-type chondroitin synthase-1 protein, the non-reducing terminal 4-O-sulfation of GalNAc residues synthesized by chondroitin N-acetylgalactosaminyltransferase-1 did not facilitate the elongation of chondroitin sulfate chains when chondroitin polymerase that consists of the mutant chondroitin synthase-1 protein was used as the enzyme source.\nCONCLUSIONS: The chondroitin synthase-1 F362S mutation in a patient with neuropathy resulted in a decrease in chondroitin polymerization activity and the mutant protein was defective in regulating the number of chondroitin sulfate chains via chondroitin N-acetylgalactosaminyltransferase-1. Thus, the progression of peripheral neuropathies may result from defects in these regulatory systems.\nGENERAL SIGNIFICANCE: The elongation of chondroitin sulfate chains may be tightly regulated by the cooperative expression of chondroitin synthase-1 and chondroitin N-acetylgalactosaminyltransferase-1 in peripheral neurons and peripheral neuropathies may result from synthesis of abnormally truncated chondroitin sulfate chains."}