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metabolism
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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
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
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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; 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
effect of heterozygous mutations in heparan sulfate elongation genes EXT1 and EXT2 on endothelial function in vitro as well as in vivo, phenotype, overview; 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; 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
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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
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
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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
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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
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physiological function

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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
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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
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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
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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; 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
heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability; heparan sulfate elongation genes EXT1 and EXT2 are involved in heparan sulfate elongation and in maintaining endothelial homeostasis, presumably via increased nitric oxide bioavailability; 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
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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
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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
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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
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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
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
additional information
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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
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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-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-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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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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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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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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the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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additional information
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the Ext1/Ext2 complex possesses higher glycosyltransferase activity than Ext1 or Ext2 alone
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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
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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; 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
Y419X
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the EXT2 mutation results in a truncated protein
additional information

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enzyme null mutants, defects in Hedgehog and Decapentaplegic signalling, abnormal distribution of Wingless morphogen
additional information
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enzyme null mutant, dramatically reduced levels of heparan sulfate, impaired Hedgehog, Wingless and Decapentaplegic signalling, alterations in chondroitin sulfate composition and levels
additional information
generation of Ext2+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext2+/- mice compared to wild-type littermates; in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow; 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; in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow; 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; in vitro EXT1 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow; in vitro EXT2 silencing, suppressed with siRNA, in microvascular endothelial cells under laminar flow
additional information
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generation of Ext1+/- mice, endothelial glycocalyx and maximal arteriolar dilatation are significantly altered in Ext1+/- mice compared to wild-type littermates
additional information
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generation of EXT1 knockout mice
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Breast Neoplasms
Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene family.
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.
Colorectal Neoplasms
EXTL3 promoter methylation down-regulates EXTL3 and heparan sulphate expression in mucinous colorectal cancers.
Colorectal Neoplasms
EXTL3/EXTR1 alterations in colorectal cancer cell lines.
Diabetes Mellitus, Type 2
Association between variants of EXT2 and type 2 diabetes: a replication and meta-analysis.
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
Assessing the general population frequency of rare coding variants in the EXT1 and EXT2 genes previously implicated in hereditary multiple exostoses.
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
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.
Exostoses, Multiple Hereditary
Mutational Analysis of Exostosin 1 and 2 Genes in Multiple Osteochondroma.
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.
Herpes Zoster
Effect of sperm diluents on the acrosome reaction in canine sperm.
Hypercholesterolemia
Ext1 heterozygosity causes a modest effect on postprandial lipid clearance in humans.
Mucopolysaccharidoses
Gene silencing of EXTL2 and EXTL3 as a substrate deprivation therapy for heparan sulphate storing mucopolysaccharidoses.
Neoplasm Metastasis
Effect of REG I? protein on angiogenesis in gastric cancer tissues.
Neoplasms
Chondroitin sulfate synthase 1 expression is associated with malignant potential of soft tissue sarcomas with myxoid substance.
Neoplasms
Effect of REG I? protein on angiogenesis in gastric cancer tissues.
Neoplasms
Exostosin 1 is expressed in human odontoblasts.
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
EXTL3/EXTR1 alterations in colorectal cancer cell lines.
Neoplasms
Familial Solitary Chondrosarcoma Resulting from Germline EXT2 Mutation.
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
Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene family.
Neoplasms
Location of the glucuronosyltransferase domain in the heparan sulfate copolymerase EXT1 by analysis of Chinese hamster ovary cell mutants.
Neoplasms
Overexpression of EXTL3/EXTR1 enhances NF-kappaB activity induced by TNF-alpha.
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
The use of Bcl-2 and PTHLH immunohistochemistry in the diagnosis of peripheral chondrosarcoma in a clinicopathological setting.
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.
Stomach Neoplasms
Effect of REG I? protein on angiogenesis in gastric cancer tissues.
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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
Bos taurus, Homo sapiens
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 (Q9V730), Drosophila melanogaster (Q9Y169), Homo sapiens, Homo sapiens (Q16394), Homo sapiens (Q93063)
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 (Q16394), Homo sapiens (Q93063)
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 (Q9V730), Drosophila melanogaster (Q9Y169)
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 (P70428), Homo sapiens (Q16394), Homo sapiens (Q93063), 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, Homo sapiens (Q93063)
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