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Information on EC 2.4.1.225 - N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase
for references in articles please use BRENDA:EC2.4.1.225
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.225 N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase
IUBMB Comments
Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.4.1.225
- exostoses
- proteoglycans
- osteochondroma
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hspgs
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thsd7a
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ext-like
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extls
- tout-velu
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nell-1
- medicine
Reaction Schemes
showSynonyms
extl3, exostosin, rib-1, rib-2, ext-1, ext-2, tout velu, heparan sulfate co-polymerase, ext-3, glucuronic acid/n-acetylglucosamine co-polymerase-1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diphosphoglucuronate:oligosaccharide uridine glucuronosyltransferase
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exostosin glycosyltransferase 1
exostosin-1
exostosin-2
exotose-2
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EXT-1
EXT1
EXT2
EXTL3
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the EXTL proteins exhibit overlapping glycosyltransferase activities in vitro, so it is not apparent what reactions they catalyze in vivo
gene EXTL1 glycosyltransferase
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gene EXTL2 glycosyltransferase
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glucuronosyltransferase
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heparan glucuronosyltransferase II
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heparan sulfate co-polymerase
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heparan sulfate glucuronosyltransferase
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N-acetylglucosaminylproteoglycan beta-1,4-glucuronosyltransferase
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sotv
ttv
UDP-glucuronate:oligosaccharide
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exostosin-1
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exostosin-2
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EXT1
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EXT1 and EXT2 form a Golgi-located hetero-oligomeric complex that catalyzes the chain elongation step in heparan sulfate biosynthesis
EXT2
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EXT1 and EXT2 form a Golgi-located hetero-oligomeric complex that catalyzes the chain elongation step in heparan sulfate biosynthesis
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
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PATHWAY SOURCE
PATHWAYS
MetaCyc
heparan sulfate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucuronate:N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase
Involved in the biosynthesis of heparin and heparan sulfate. Some forms of the human enzyme (particularly the enzyme complex encoded by the EXT1 and EXT2 genes) act as bifunctional glycosyltransferases, which also have the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase (EC 2.4.1.224) activity required for the synthesis of the heparan sulfate disaccharide repeats.
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CAS REGISTRY NUMBER
COMMENTARY
145539-84-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
K5 heptasaccharide + UDP-alpha-D-glucuronate
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K5 heptasaccharide + UDP-alpha-D-glucuronate
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K5 heptasaccharide + UDP-alpha-D-glucuronate
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
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UDP-N-acetyl-D-glucosamine + alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
UDP + alpha-N-acetyl-D-glucosaminyl-alpha-D-glucuronosyl-(1-4)-N-acetylglucoside
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additional information
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Substrates: formation of homo- and heterooligomeric complexes of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 alone
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additional information
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Substrates: EXT1 has both GlcNAc transferase activity of EC 2.4.1.224 and GlcA transferase activity of EC 2.4.1.225, EXT2 only has low activity of EC 2.4.1.225, coexpression of EXT1 and EXT2 yields high activity of EC 2.4.1.225 and low activity of EC 2.4.1.224
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additional information
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Substrates: formation of homo- and heterooligomeric complexes of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 has alone
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additional information
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Substrates: the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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additional information
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Substrates: the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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Substrates: -
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UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
UDP + beta-glucuronosyl-(1-4)-N-acetyl-alpha-D-glucosaminyl-(1-4)-beta-D-glucuronosyl-proteoglycan
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Substrates: -
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additional information
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Substrates: the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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additional information
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Substrates: the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Immunopathological analysis of the expression of glomerular exostosin 1 and exostosin 2 in Japanese patients with lupus nephritis.
Breast Neoplasms
Exostosin 1 regulates cancer cell stemness in doxorubicin-resistant breast cancer cells.
Breast Neoplasms
Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene family.
Breast Neoplasms
The exostosin family of glycosyltransferases: mRNA expression profiles and heparan sulphate structure in human breast carcinoma cell lines.
Carcinogenesis
REG3A/REG3B promotes acinar to ductal metaplasia through binding to EXTL3 and activating the RAS-RAF-MEK-ERK signaling pathway.
Cholangiocarcinoma
Increase of exostosin 1 in plasma as a potential biomarker for opisthorchiasis-associated cholangiocarcinoma.
Chondrosarcoma
Aberrant heparan sulfate proteoglycan localization, despite normal exostosin, in central chondrosarcoma.
Chondrosarcoma
Structural Features of Heparan Sulfate from Multiple Osteochondromas and Chondrosarcomas.
Colorectal Neoplasms
EXTL3 promoter methylation down-regulates EXTL3 and heparan sulphate expression in mucinous colorectal cancers.
Diabetes Mellitus, Type 2
Association between variants of EXT2 and type 2 diabetes: a replication and meta-analysis.
Diabetes Mellitus, Type 2
No correlation between the variants of exostosin 2 gene and type 2 diabetes in Burkina Faso population.
Endometriosis
EXTL3-interacting endometriosis-specific serum factors induce colony formation of endometrial stromal cells.
Exostoses
Structural analysis of glycosaminoglycans in animals bearing mutations in sugarless, sulfateless, and tout-velu. Drosophila homologues of vertebrate genes encoding glycosaminoglycan biosynthetic enzymes.
Exostoses
The molecular and cellular basis of exostosis formation in hereditary multiple exostoses.
Exostoses, Multiple Hereditary
A family with limb girdle muscular dystrophy type 1B and multiple exostoses.
Exostoses, Multiple Hereditary
Assessing the general population frequency of rare coding variants in the EXT1 and EXT2 genes previously implicated in hereditary multiple exostoses.
Exostoses, Multiple Hereditary
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Exostoses, Multiple Hereditary
Evaluation of the anatomic burden of patients with hereditary multiple exostoses.
Exostoses, Multiple Hereditary
Ext1 heterozygosity causes a modest effect on postprandial lipid clearance in humans.
Exostoses, Multiple Hereditary
Familial Solitary Chondrosarcoma Resulting from Germline EXT2 Mutation.
Exostoses, Multiple Hereditary
Functional conservation of the human EXT1 tumor suppressor gene and its Drosophila homolog tout velu.
Exostoses, Multiple Hereditary
Functional Requirements for Heparan Sulfate Biosynthesis in Morphogenesis and Nervous System Development in C. elegans.
Exostoses, Multiple Hereditary
Glycosaminoglycans in blood of hereditary multiple exostoses patients: Half reduction of heparan sulfate to chondroitin sulfate ratio and the possible diagnostic application.
Exostoses, Multiple Hereditary
Hereditary multiple osteochondromas in Jordanian patients: Mutational and immunohistochemical analysis of EXT1 and EXT2 genes.
Exostoses, Multiple Hereditary
Identification of Two Novel Frameshift Mutations in Exostosin 1 in Two Families with Multiple Osteochondromas.
Exostoses, Multiple Hereditary
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.
Exostoses, Multiple Hereditary
Mutation spectrum of EXT1 and EXT2 in the Saudi patients with hereditary multiple exostoses.
Exostoses, Multiple Hereditary
Mutational Analysis of Exostosin 1 and 2 Genes in Multiple Osteochondroma.
Exostoses, Multiple Hereditary
Mutational spectrum and clinical signatures in 114 families with hereditary multiple osteochondromas: insights into molecular properties of selected exostosin variants.
Exostoses, Multiple Hereditary
Novel mutation in the EXT-1 gene in an Iranian family affected with hereditary multiple exostoses.
Exostoses, Multiple Hereditary
Regulation of zebrafish skeletogenesis by ext2/dackel and papst1/pinscher.
Exostoses, Multiple Hereditary
Whole?exome sequencing identifies a novel mutation of SLC20A2 (c.C1849T) as a possible cause of hereditary multiple exostoses in a Chinese family.
Genetic Diseases, Inborn
Mutation spectrum of EXT1 and EXT2 in the Saudi patients with hereditary multiple exostoses.
Giant Cell Tumors
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Glomerulonephritis, Membranous
A Target Antigen-Based Approach to the Classification of Membranous Nephropathy.
Glomerulonephritis, Membranous
Immunopathological analysis of the expression of glomerular exostosin 1 and exostosin 2 in Japanese patients with lupus nephritis.
Glomerulonephritis, Membranous
In Patients with Membranous Lupus Nephritis, Exostosin-Positivity and Exostosin-Negativity Represent Two Different Phenotypes.
Glomerulonephritis, Membranous
Primary Membranous Nephropathy With Enhanced Staining of Exostosin 1/Exostosin 2 in the Glomeruli: A Report of 2 Cases.
Glomerulonephritis, Membranous
The Exostosin Immunohistochemical Status Differentiates Lupus Membranous Nephropathy Subsets With Different Outcomes.
Hypercholesterolemia
Ext1 heterozygosity causes a modest effect on postprandial lipid clearance in humans.
Lupus Nephritis
Immunopathological analysis of the expression of glomerular exostosin 1 and exostosin 2 in Japanese patients with lupus nephritis.
Lupus Nephritis
Treatment of exostosin 1-associated membranous lupus nephritis with multiple low doses of rituximab: A case report.
Mucopolysaccharidoses
Gene silencing of EXTL2 and EXTL3 as a substrate deprivation therapy for heparan sulphate storing mucopolysaccharidoses.
Muscular Diseases
A family with limb girdle muscular dystrophy type 1B and multiple exostoses.
Neoplasms
A tumorigenic cell line derived from a hamster cholangiocarcinoma associated with Opisthorchis felineus liver fluke infection.
Neoplasms
Case Report of the positive exostosin-1 without B-cell lymphoma-2 gene expression of giant cell tumor lesion in hereditary multiple exostosis.
Neoplasms
Chondroitin sulfate synthase 1 expression is associated with malignant potential of soft tissue sarcomas with myxoid substance.
Neoplasms
Exostosin 1 regulates cancer cell stemness in doxorubicin-resistant breast cancer cells.
Neoplasms
Expression of rib-1, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes, is indispensable for heparan sulfate synthesis and embryonic morphogenesis.
Neoplasms
Functional conservation of the human EXT1 tumor suppressor gene and its Drosophila homolog tout velu.
Neoplasms
Hedgehog movement is regulated through tout velu-dependent synthesis of a heparan sulfate proteoglycan.
Neoplasms
Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode alpha 1,4- N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/ heparin biosynthesis.
Neoplasms
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.
Neoplasms
Mutation spectrum of EXT1 and EXT2 in the Saudi patients with hereditary multiple exostoses.
Neoplasms
rib-2, a Caenorhabditis elegans homolog of the human tumor suppressor EXT genes encodes a novel alpha1,4-N-acetylglucosaminyltransferase involved in the biosynthetic initiation and elongation of heparan sulfate.
Neoplasms
Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor suppressors, affects heparan sulfate in vivo.
Neoplasms
Systematic interactome mapping of acute lymphoblastic leukemia cancer gene products reveals EXT-1 tumor suppressor as a Notch1 and FBWX7 common interactor.
Neoplasms
Tout-velu is a Drosophila homologue of the putative tumour suppressor EXT-1 and is needed for Hh diffusion.
Osteochondroma
Cell biology of osteochondromas: bone morphogenic protein signalling and heparan sulphates.
Osteochondroma
Detection of exostosin glycosyltransferase gene mutations in patients with non-hereditary osteochondromas of the mandibular condyle.
Osteochondroma
Differentiation-induced loss of heparan sulfate in human exostosis derived chondrocytes.
Osteochondroma
Structural Features of Heparan Sulfate from Multiple Osteochondromas and Chondrosarcomas.
Osteochondroma
The use of Bcl-2 and PTHLH immunohistochemistry in the diagnosis of peripheral chondrosarcoma in a clinicopathological setting.
Osteochondromatosis
A de novo mutation in the EXT2 gene associated with osteochondromatosis in a litter of American Staffordshire Terriers.
Osteosarcoma
Functional Requirements for Heparan Sulfate Biosynthesis in Morphogenesis and Nervous System Development in C. elegans.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Systematic interactome mapping of acute lymphoblastic leukemia cancer gene products reveals EXT-1 tumor suppressor as a Notch1 and FBWX7 common interactor.
Sarcoma
Chondroitin sulfate synthase 1 expression is associated with malignant potential of soft tissue sarcomas with myxoid substance.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
EXT1, NDST1, and NDST2 differentially regulate heparan sulfate biosynthesis in human tooth germ
brenda
additional information
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loss of one copy of either the EXT1 or EXT2 gene product compromises the perichondrial chondrocytes ability to differentiate normally and to survive in a differentiated state in vitro
brenda
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FBJ, highly metastatic mouse osteosarcoma FBJ-LL cells and the poorly metastatic FBJ-S1 cells are produced from a FBJ virus-induced osteosarcoma
brenda
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FBJ, highly metastatic mouse osteosarcoma FBJ-LL cells and the poorly metastatic FBJ-S1 cells are produced from a FBJ virus-induced osteosarcoma
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brenda
additional information
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zebrafish ext2 gene is ubiquitously expressed during zebrafish development
brenda
additional information
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kidney extract is devoid of EXT2 in EXT2-overexpressing mice
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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identical localization of sotv and ttv
brenda
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Ext1 and Ext2 are type II transmembrane glycoproteins
brenda
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Ext1 and Ext2 are type II transmembrane glycoproteins
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brenda
EXT isozymes are localized mainly in the cis- and middle-Golgi stacks. Rotini, Rti, mediates the retrograde transport of EXT enzymes within the Golgi complex. Rotini regulates the sub-compartmental distribution of EXTs in the Golgi
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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slight change in the number of developing B cells in B-cell Ext1-deficient mice, but alteration does not cause a change in antibody production
malfunction
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EXT1 influences fibroblast matrix interactions. Essential role of EXT1 in providing specific binding sites for growth factors and extracellular matrix proteins. Phosphorylation of ERK1/2 in response to FGF2 stimulation is markedly decreased in the Ext1 mutant fibroblasts, whereas neither PDGF-BB nor FGF10 signaling is significantly affected. Ext1 mutants display reduced ability to attach to collagen I and to contract collagen lattices. Reintroduction of Ext1 in Ext1 mutant fibroblasts rescues heparan sulfate chain length, FGF2 signaling, and the ability of the fibroblasts to contract collagen
malfunction
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Fgf targeted gene expression is reduced in ext2 mutants and the remaining expression is readily inhibited by SU5402, an FGF receptor inhibitor. In the ext2 mutants, Fgf signaling is affected during nervous system development, mechanism, overview, and reduction of Fgf ligands in the mutants affects tail development. Wnt signaling is also affected in the ext2 mutants, while Hh dependent signaling is apparently unaffected in the ext2 mutants, Hh targeted gene expression is not reduced, the Hh inhibitor cyclopamine is not more affective in the mutants and Hh-dependent cell differentiation in the retina and in the myotome are normal in ext2 mutants, ext2 mutant phenotypes, overview
malfunction
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a reduction in either Ext1 or Ext2 can cause a reduction in heparan sulfate biosynthesis, overview. Suppression of Ext1 by siRNA in FBJ-S1 cells results in the decreased expression of heparan sulfate and enhanced motility
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo. Silencing of microvascular endothelial cell EXT1 and EXT2 under flow led to significant upregulation of endothelial nitric oxide synthesis and phospho-endothelial nitric oxide synthesis protein expression. Brachial artery flow-mediated dilation is significantly increased in hereditary multiple exostoses patients. In humans, heterozygous loss of function mutation in EXT1 and EXT2 are known to be involved in the development of HME syndrome, a disorder associated with bony tumor formation. In these humans, the loss-of-function mutations lead to alterations in the structure of tissue and plasma heparan sulfate composition, phenotype, overview
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo. Silencing of microvascular endothelial cell EXT1 and EXT2 under flow led to significant upregulation of endothelial nitric oxide synthesis and phospho-endothelial nitric oxide synthesis protein expression. Brachial artery flow-mediated dilation is significantly increased in hereditary multiple exostoses (HME) patients. In humans, heterozygous loss of function mutation in EXT1 and EXT2 are known to be involved in the development of HME syndrome, a disorder associated with bony tumor formation. In these humans, the loss-of-function mutations lead to alterations in the structure of tissue and plasma heparan sulfate composition, phenotype, overview
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo, phenotype, overview
malfunction
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo, phenotype, overview
malfunction
deletion of Ext1 in the mesoderm induces a cardiac phenotype similar to that of a mutant with conditional deletion of UDP-glucose dehydrogenase, a key enzyme responsible for synthesis of all glycosaminoglycans. The outflow tract defect in conditional Ext1 knockout (Ext1f/f:Mesp1Cre) mice is attributable to the reduced contribution of second heart field and neural crest cells. Ext1 deletion leads to downregulation of FGF signaling in the pharyngeal mesoderm. Exogenous FGF8 ameliorates the defects in the outflow tract and pharyngeal explants. Phenotype, detailed overview
malfunction
ectopic cartilage forms in Ext1-deficient mouse embryo long bones, phenotype overview. perichondrium phenotype and border function regulation is deregulated in hereditary multiple exostoses. Ext1 deficiency stimulates cartilage formation
malfunction
mutations in the tumor suppressor genes EXT1 and EXT2 disturb heparan sulfate proteoglycan biosynthesis and cause multiple osteochondroma. A reduction in Rti shifts the steady-state distribution of EXTs to the trans-Golgi. These accumulated EXTs tend to be degraded and their re-entrance towards the route for polymerizing GAG chains is disengaged. Conversely, EXTs are mislocalized towards the transitional endoplasmic reticulum/cis-Golgi when Rti is overexpressed. Both loss of function and overexpression of rti result in incomplete heparan sulfate proteoglycans and perturb Hedgehog signaling
malfunction
phenotype of four patients showing clinical seizures-scoliosis-macrocephaly syndrome with seizures and macrocephaly due to decreased EXT2 expression and mutations M87R and R95C. SSM syndrome is characterised by seizures, intellectual disability, hypotonia, scoliosis, macrocephaly, hypertelorism and renal dysfunction. Phenotype, overview
malfunction
screening and identifying the gene mutation of EXT1 associated with multiple exostosis and the expression in tumor tissues
malfunction
Ext1 knock-down reduces heparan sulfate, and increases chondrogenic markers and proteoglycan accumulation. Ext1 knock-down reduces active Wnt/beta-catenin signaling
malfunction
-
a reduction in either Ext1 or Ext2 can cause a reduction in heparan sulfate biosynthesis, overview. Suppression of Ext1 by siRNA in FBJ-S1 cells results in the decreased expression of heparan sulfate and enhanced motility
-
metabolism
Exostosin glycosyltransferases exclusively catalyze heparan sulfate polymerization. Heparan sulfate/heparin, chondroitin sulfate, dermatan sulfate, and keratan sulfate form glycosaminoglycans, long linear polysaccharide chains consisting of repeat disaccharide units. Glycosaminoglycans are the major components of the extracellular matrix and play critical roles in regulating transport and signaling of numerous growth factors during embryonic development
metabolism
the enzymes is involved in heparan sulfate biosynthesis. EXT1, NDST1, and NDST2 differentially regulate heparan sulfate biosynthesis in human tooth germ
physiological function
-
the level of expression of EXT1 and EXT2 affects the amount of glucosaminyl N-deacetylase/N-sulfotransferase 1 (NDST1) present in the cell, which, in turn, greatly influences heparan sulfate structure. Overexpression of EXT2 in HEK 293 cells enhances NDST1 expression, increases NDST1 N-glycosylation, and results in elevated heparan sulfate sulfation, overexpression of EXT1 has opposite effects. Heart tissue from transgenic mice overexpressing EXT2 shows increased NDST activity. NDST1 interacts with EXT2, NDST1 may compete with EXT1 for binding to EXT2
physiological function
-
Ext1 and Ext2 together form a copolymerase which is responsible for the polymerization process where repeating units of N-acetylglucosamine and glucuronic acid are incorporated in the growing linear polysaccharide chain, see also EC 2.4.1.224. Gene ext2 is involved in Fgf and Wnt signaling but not in Hh signaling, ext2 is a general enhancer of Fgf target gene expression, ext2 interacts genetically with Fgf signaling during tail development, specificity for gene ext2 in signaling pathways during embryonic development, overview
physiological function
-
Ext1 and Ext2 are tumor suppressors. In the biosynthesis of heparan sulfate, after the attachment of a GlcNAc residue to GlcA-Gal-Gal-Xyl, Ext1 and Ext2 catalyze the subsequent elongation of glycosaminoglycans by alternately adding GlcA and GlcNAc to the end of the growing chain. Involvement of Ext1 and heparanase in migration of FBJ osteosarcoma cells, overview
physiological function
heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability
physiological function
heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability
physiological function
Ext1 is a glycosyltransferase responsible for heparan sulfate synthesis. Function of Ext1 in heart development, overview. Ext1 expression in second heart field and neural crest cells is required for outflow tract remodeling. Ext1 is crucial for outflow tract formation in distinct progenitor cells, and heparan sulfate modulates FGF signaling during early heart development. Proper expression of Ext1 is required for cardiogenesis, heparan sulfate is required for heart development
physiological function
perichondrium phenotype and border function are deranged by Ext1 and heparan sulfate in developing long bones, and in ectopic cartilage formation
physiological function
exostosin (EXT) genes encode glycosyltransferases required for glycosaminoglycan chain polymerization in the biosynthesis of heparan sulfate proteoglycans. Synthesis of heparan sulfate proteoglycans requires sequential enzymatic modifications of glycoproteins in the Golgi. Drosophila Golgi phosphoprotein 3, GOLPH3 or rotini, Rti, regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins. Rti regulates the stability of EXTs. Proper function of EXTs depends not only on their enzymatic activities but also on their sub-compartmental distributions
physiological function
key enzyme contributing to the generation of heparan sulfate chains. EXT1, with tumour suppressor properties, is involved in the initiation and polymerisation of the growing heparan sulfate chain. The study may suggest that no association exists between EXT1 and multiple sclerosis
physiological function
the enzyme is involved in heparan sulfate biosynthesis
physiological function
key enzymes contributing to the generation of heparan sulfate chains. EXT1, with documented tumour suppressor properties, is involved in the initiation and polymerisation of the growing heparan sulfate chain
physiological function
the enzyme is required for heparan sulfate chain elongation in heparan sulfate-proteoglycan biosynthesis. EXT1 affects chondrogenic differentiation of precursor cells, in part via changes in the activity of Wnt/beta-catenin signaling. Wnt/beta-catenin signaling controls Ext1 expression, suggesting a regulatory loop between EXT1 and Wnt/beta-catenin signaling during chondrogenesis
physiological function
-
EXT1 knockdown promotes infection by porcine reproductive and respiratory syndrome virus (PRRSV), its overexpression inhibits virus infection. EXT1 restricts viral RNA replication and interacts with viral nonstructural proteins nsp3 and nsp5 via its N-terminal cytoplasmic tail and enhances their K48-linked polyubiquitination. The C-terminal glycosyltransferase activity domain of EXT1 is necessary for nsp3 and nsp5 degradation. EXT1 effectively restricts porcine epidemic diarrhea virus and porcine enteric alphacoronavirus infection in Vero cells
physiological function
knocking out EXT1 dramatically restricts ZIKV infection, mediated by the downregulation of autophagy. Overexpressing EXT1 results in the reduction of ZIKV production by targeting the viral envelope protein and non-structural protein NS3 in a proteasome-dependent degradation manner. Knocking down EXT1 at the early stage of ZIKV infection represses viral infection, an increase of ZIKV infection is observed when knocking down EXT1 at the late stage of viral infection
physiological function
-
Ext1 and Ext2 are tumor suppressors. In the biosynthesis of heparan sulfate, after the attachment of a GlcNAc residue to GlcA-Gal-Gal-Xyl, Ext1 and Ext2 catalyze the subsequent elongation of glycosaminoglycans by alternately adding GlcA and GlcNAc to the end of the growing chain. Involvement of Ext1 and heparanase in migration of FBJ osteosarcoma cells, overview
-
Show AA Sequence and Transmembrane Helices (614 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 80000, EXT1, calculated, 1 * 80000 + 1 * 80000, EXT1/EXT2 heterodimer, calculated
monomer
additional information
additional information
-
formation of homo- and heterooligomeric complexes of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 alone
additional information
-
formation of heterooligomers of ttv and sotv, co-immunoprecipitation experiments
additional information
-
formation of homo- and heterooligomeric complexes of EXT1 and EXT2, heterooligomeric complexes have substantially higher glycosyltransferase activity than EXT1 or EXT2 has alone
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C333R
naturally occuring mutation in hereditary multiple exostoses syndrome
L462W
naturally occuring mutation in hereditary multiple exostoses syndrome
L46F
naturally occuring mutation in hereditary multiple exostoses syndrome
M87R
naturally occuring mutation from a patient with clinical seizures-scoliosis-macrocephaly syndrome
medicine
the mutation status of patients with multiple osteochondromas correlates with decreased EXT1 or EXT2 expression, loss of EXT expression disrupts the function of the EXT1/2 complex in heparan sulfate proteoglycan biosynthesis, resulting in the intracellular accumulation of heparan sulfate proteoglycan core proteins in tumo tissues
N288K
naturally occuring mutation in hereditary multiple exostoses syndrome
R227D
naturally occuring mutation in hereditary multiple exostoses syndrome
R340H
naturally occuring mutation in hereditary multiple exostoses syndrome
R95C
naturally occuring mutation from a patient with clinical seizures-scoliosis-macrocephaly syndrome
S344F
naturally occuring mutation in hereditary multiple exostoses syndrome
S478L
naturally occuring mutation in hereditary multiple exostoses syndrome
V68G
naturally occuring mutation in hereditary multiple exostoses syndrome
additional information
additional information
-
enzyme null mutant, dramatically reduced levels of heparan sulfate, impaired Hedgehog, Wingless and Decapentaplegic signalling, alterations in chondroitin sulfate composition and levels
additional information
-
enzyme null mutants, defects in Hedgehog and Decapentaplegic signalling, abnormal distribution of Wingless morphogen
additional information
in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
in vitro EXT2 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
in vitro EXT2 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
in vitro EXT2 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
generation of Ext2+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext2+/- mice compared to wild-type littermates
additional information
generation of Ext2+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext2+/- mice compared to wild-type littermates
additional information
generation of Ext2+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext2+/- mice compared to wild-type littermates
additional information
generation of Ext1+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext1+/- mice compared to wild-type littermates
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
EXT1 and EXT2 cDNA, alone or in combination, cloned into the pBudCE4.1 vector, which contains two multiple cloning sites for simultaneous expression of two proteins. EXT1 cloned into the multiple cloning sites with the cytomegalovirus (CMV) immediate-early promotor and EXT2 into the multiple cloning sites with the human elongation factor 1alpha promotor. Constructs transfected into HEK-293 cells stably expressing NDST1 from the pCDNA3 vector. Mutated EXT2 cDNA cloned into the pBudCE4.1 vector and transfected into HEK-93 cells overexpressing NDST1. EXT2 cDNA inserted into the pCAGGS expression vector under the control of the CMV immediate-early enhancer and the chicken beta-actin promoter (CAG) for constitutively high tissue expression from fertilized eggs and early embryonic stage through adulthood. The cDNA construct cloned into the unique EcoR1 site between the CAG promoter and the rabbit beta-globin sequence. Vector linearized with BamH1 and SalI and injected into mice B6CBAF1 oocytes
-
full-length Ext1 cDNA cloned into the pBudCE4.1 vector and transfected into Ext1Gt/Gt fibroblasts
-
gene EXT1, creation of loxP-modified Ext1 allele and establishment of the Ext1 floxed mouse line (Ext1flox/flox), expression of the enzyme in Gdf-5-Cre transgenic mice, semiquantitative real-time PCR enzyme expression analysis
gene EXT1, recombinant expression of Myc-DKK-tagged enzyme in S2 cells, interaction analysis with GOLPH3 via yeast two-hybrid assay
gene EXT2, recombinant expression of Myc-DKK-tagged enzyme in S2 cells, interaction analysis with GOLPH3 via yeast two-hybrid assay
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is upregulated upon infection by porcine reproductive and respiratory syndrome virus (PRRSV)
-
EXT1 is significantly decreased in MCF7 cells compared with the non-tumorigenic MCF10A cells, while no significant difference is observed between the two triple-negative cell lines, MDA-MB-231 and HCC38, and the ER- and PR-positive MCF10A cells
EXT2 is down-regulated in MDA-MB-231 and HCC38 epithelial breast carcinoma cell lines
the overall transcriptional activity of the main heparan sulfate biosynthesis-involved genes (EXT1, EXT2, NDST1,NDST2, GLCE, HS2ST1, HS3ST1, HS3ST2, HS6ST1, HS6ST2, SULF1, SULF2, HPSE) is decreased by 1.5-2fold in Grade II-III glioma (p < 0.01) and by 3-fold in Grade IV glioma (glioblastoma multiforme, GBM) (p < 0.05), as compared with the para-tumourous tissue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
analysis of enzyme mutations in patients with hereditary multiple exostoses, mutation spectrum
medicine
-
there is deficiency of heparan sulfate and perlecan, together with accumulation of collagens in the matrix of EXT1-associated osteosarcomas
medicine
knocking out EXT1 dramatically restricts ZIKV infection, mediated by the downregulation of autophagy. Overexpressing EXT1 results in the reduction of ZIKV production by targeting the viral envelope protein and non-structural protein NS3 in a proteasome-dependent degradation manner. Knocking down EXT1 at the early stage of ZIKV infection represses viral infection, an increase of ZIKV infection is observed when knocking down EXT1 at the late stage of viral infection
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lind, T.; Tufaro, F.; McCormick, C.; Lindahl, U.; Lidholt, K.
The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate
J. Biol. Chem.
273
26265-26268
1998
Bos taurus (O77783)
brenda
Lind, T.; Lindahl, U.; Lidholt, K.
Biosynthesis of heparin/heparan sulfate. Identification of a 70-kDa protein catalyzing both the D-glucuronosyl- and the N-acetyl-D-glucosaminyltransferase reactions
J. Biol. Chem.
268
20705-20708
1993
Bos taurus
brenda
Lidholt, K.; Fjelstad, M.; Jann, K.; Lindahl, U.
Biosynthesis of heparin. XXV. Substrate specificities of glucosyltransferases involved in formation of heparin precursor and E. coli K5 capsular polysaccharides
Carbohydr. Res.
255
87-101
1994
Escherichia coli, Escherichia coli K5, Mus musculus
brenda
Wei, G.; Bai, X.; Gabb, M.M.G.; Bame, K.J.; Koshy, T.I.; Spear, P.G.; Esko, J.D.
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants
J. Biol. Chem.
275
27733-27740
2000
Oncorhynchus mykiss
brenda
Han, C.; Belenkaya, T.Y.; Khodoun, M.; Tauchi, M.; Lin, X.; Lin, X.
Distinct and collaborative roles of Drosophila EXT family proteins in morphopgen signalling and gradient formation
Development
131
1563-1575
2005
Drosophila melanogaster
brenda
Bornemann, D.J.; Duncan, J.E.; Staatz, W.; Selleck, S.; Warrior, R.
Abrogation of heparan sulfate synthesis in Drosophila disrupts the Wingless, Hedgehog and Decapentaplegic signaling pathways
Development
131
1927-198
2004
Drosophila melanogaster
brenda
Wuyts, W.; van Hul, W.
Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes
Hum. Mutat.
15
220-227
2000
Homo sapiens
brenda
Busse, M.; Kusche-Gullberg, M.
In vitro polymerization of heparan sulfate backbone by the EXT proteins
J. Biol. Chem.
278
41333-41337
2003
Homo sapiens
brenda
McCormick, C.; Duncan, G.; Goutsos, K.T.; Tufaro, F.
The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heapran sulfate
Proc. Natl. Acad. Sci. USA
97
668-673
2000
Homo sapiens, Bos taurus
brenda
Hecht, J.T.; Hayes, E.; Haynes, R.; Cole, W.G.; Long, R.J.; Farach-Carson, M.C.; Carson, D.D.
Differentiation-induced loss of heparan sulfate in human exostosis derived chondrocytes
Differentiation
73
212-221
2005
Homo sapiens
brenda
Dasgupta, U.; Dixit, B.L.; Rusch, M.; Selleck, S.; The, I.
Functional conservation of the human EXT1 tumor suppressor gene and its Drosophila homolog tout velu
Dev. Genes Evol.
217
555-561
2007
Drosophila melanogaster, Homo sapiens
brenda
Roberts, I.S.; Gleadle, J.M.
Familial nephropathy and multiple exostoses with exostosin-1 (EXT1) gene mutation
J. Am. Soc. Nephrol.
19
450-453
2008
Homo sapiens
brenda
Nadanaka, S.; Kitagawa, H.
Heparan sulphate biosynthesis and disease
J. Biochem.
144
7-14
2008
Caenorhabditis elegans, Drosophila melanogaster (Q9Y169), Drosophila melanogaster (Q9V730), Homo sapiens, Homo sapiens (Q93063), Homo sapiens (Q16394)
brenda
Busse, M.; Feta, A.; Presto, J.; Wilen, M.; Gronning, M.; Kjellen, L.; Kusche-Gullberg, M.
Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongation
J. Biol. Chem.
282
32802-32810
2007
Homo sapiens
brenda
Nadanaka, S.; Ishida, M.; Ikegami, M.; Kitagawa, H.
Chondroitin 4-O-sulfotransferase-1 modulates Wnt-3a signaling through control of E disaccharide expression of chondroitin sulfate
J. Biol. Chem.
283
27333-27343
2008
Mus musculus (P97464)
brenda
Hameetman, L.; David, G.; Yavas, A.; White, S.J.; Taminiau, A.H.; Cleton-Jansen, A.; Hogendoom, P.C.; Bovee, J.V.
Decreased EXT expression and intracellular accumulation of heparan sulphate proteoglycan in osteochondromas and peripheral chondrosarcomas
J. Pathol.
211
399-409
2007
Homo sapiens (Q93063), Homo sapiens (Q16394)
brenda
Garner, O.B.; Yamaguchi, Y.; Esko, J.D.; Videm, V.
Small changes in lymphocyte development and activation in mice through tissue-specific alteration of heparan sulphate
Immunology
125
420-429
2008
Mus musculus
brenda
Osterholm, C.; Barczyk, M.M.; Busse, M.; Gronning, M.; Reed, R.K.; Kusche-Gullberg, M.
Mutation in the heparan sulfate biosynthesis enzyme EXT1 influences growth factor signaling and fibroblast interactions with the extracellular matrix
J. Biol. Chem.
284
34935-34943
2009
Mus musculus
brenda
Presto, J.; Thuveson, M.; Carlsson, P.; Busse, M.; Wilen, M.; Eriksson, I.; Kusche-Gullberg, M.; Kjellen, L.
Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression and heparan sulfate sulfation
Proc. Natl. Acad. Sci. USA
105
4751-4756
2008
Mus musculus
brenda
Fischer, S.; Filipek-Gorniok, B.; Ledin, J.
Zebrafish Ext2 is necessary for Fgf and Wnt signaling, but not for Hh signaling
BMC Dev. Biol.
11
53
2011
Danio rerio
brenda
Wang, Y.; Yang, X.; Yamagata, S.; Yamagata, T.; Sato, T.
Involvement of Ext1 and heparanase in migration of mouse FBJ osteosarcoma cells
Mol. Cell. Biochem.
373
63-72
2013
Mus musculus, Mus musculus BALB/c
brenda
Huegel, J.; Mundy, C.; Sgariglia, F.; Nygren, P.; Billings, P.C.; Yamaguchi, Y.; Koyama, E.; Pacifici, M.
Perichondrium phenotype and border function are regulated by Ext1 and heparan sulfate in developing long bones: a mechanism likely deranged in hereditary multiple exostoses
Dev. Biol.
377
100-112
2013
Mus musculus (P97464)
brenda
Chang, W.L.; Chang, C.W.; Chang, Y.Y.; Sung, H.H.; Lin, M.D.; Chang, S.C.; Chen, C.H.; Huang, C.W.; Tung, K.S.; Chou, T.B.
The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan sulfate proteoglycans by modulating the retrograde trafficking of exostosins
Development
140
2798-2807
2013
Drosophila melanogaster (Q9Y169), Drosophila melanogaster (Q9V730)
brenda
Mooij, H.L.; Cabrales, P.; Bernelot Moens, S.J.; Xu, D.; Udayappan, S.D.; Tsai, A.G.; van der Sande, M.A.; de Groot, E.; Intaglietta, M.; Kastelein, J.J.; Dallinga-Thie, G.M.; Esko, J.D.; Stroes, E.S.; Nieuwdorp, M.
Loss of function in heparan sulfate elongation genes EXT1 and EXT 2 results in improved nitric oxide bioavailability and endothelial function
J. Am. Heart Assoc.
3
e001274
2014
Homo sapiens (Q93063), Homo sapiens (Q16394), Homo sapiens (P70428), Mus musculus (P97464)
brenda
Farhan, S.M.; Wang, J.; Robinson, J.F.; Prasad, A.N.; Rupar, C.A.; Siu, V.M.; Siu, V.M.; Hegele, R.A.
Old gene, new phenotype: mutations in heparan sulfate synthesis enzyme, EXT2 leads to seizure and developmental disorder, no exostoses
J. Med. Genet.
52
666-675
2015
Homo sapiens (Q93063), Homo sapiens
brenda
Zhang, R.; Cao, P.; Yang, Z.; Wang, Z.; Wu, J.L.; Chen, Y.; Pan, Y.
Heparan sulfate biosynthesis enzyme, Ext1, contributes to outflow tract development of mouse heart via modulation of FGF signaling
PLoS ONE
10
e0136518
2015
Mus musculus (P97464)
brenda
Wu, Z.; Wang, Y.; Wang, J.; Chen, Y.; Guo, Y.
The role of EXT1 gene mutation and its high expression of calcitonin gene-related peptide in the development of multiple exostosis
Biochem. Biophys. Res. Commun.
505
959-965
2018
Homo sapiens (Q16394)
brenda
Sembajwe, L.; Katta, K.; Gronning, M.; Kusche-Gullberg, M.
The exostosin family of glycosyltransferases MRNA expression profiles and heparan sulphate structure in human breast carcinoma cell lines
Biosci. Rep.
38
1-12
2018
Homo sapiens (Q93063), Homo sapiens (Q16394), Homo sapiens
brenda
Kero, D.; Bilandzija, T.; Arapovic, L.; Vukojevic, K.; Saraga-Babic, M.
Syndecans and enzymes involved in heparan sulfate biosynthesis and degradation are differentially expressed during human dontogenesis
Front. Physiol.
9
732
2018
Homo sapiens (Q16394)
brenda
Okolicsanyi, R.K.; Bluhm, J.; Miller, C.; Griffiths, L.R.; Haupt, L.M.
An investigation of genetic polymorphisms in heparan sulfate proteoglycan core proteins and key modification enzymes in an Australian Caucasian multiple sclerosis population
Hum. Genomics
14
18
2020
Homo sapiens (Q16394)
brenda
Ushakov, V.; Tsidulko, A.; De La Bourdonnaye, G.; Kazanskaya, G.; Volkov, A.; Kiselev, R.; Kobozev, V.; Kostromskaya, D.; Gaytan, A.; Krivoshapkin, A.; Aidagulova, S.; Grigorieva, E.
Heparan sulfate biosynthetic system is inhibited in human glioma due to EXT1/2 and HS6ST1/2 down-regulation
Int. J. Mol. Sci.
18
2301
2017
Homo sapiens (Q93063), Homo sapiens (Q16394)
brenda
Wang, X.; Cornelis, F.M.F.; Lories, R.J.; Monteagudo, S.
Exostosin-1 enhances canonical Wnt signaling activity during chondrogenic differentiation
Osteoarthritis Cartilage
27
1702-1710
2019
Homo sapiens (Q16394)
brenda
Zhang, X.; Dong, W.; Wang, X.; Zhu, Z.; He, S.; Zhang, H.; Chen, Y.; Liu, X.; Guo, C.
Exostosin glycosyltransferase 1 reduces porcine reproductive and respiratory syndrome virus infection through proteasomal degradation of nsp3 and nsp5
J. Biol. Chem.
298
101548
2022
Sus scrofa
brenda
Ling, J.; Khan, A.; Denkewitz, M.; Maccarana, M.; Lundkvist, A.; Li, J.P.; Li, J.
Dual roles of exostosin glycosyltransferase 1 in Zika virus infection
Virulence
16
2458681
2025
Homo sapiens (Q16394)
brenda
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