| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The importance of proteoglycans for proliferation increases during development in parallel with increasing expression of the glycosyltransferase genes , exostosin 1 and exostosin 2 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutations in either exostosin 1 ( EXT 1 ) or exostosin 2 ( EXT 2 ) gene cause the HME syndrome and also some isolated osteochondromas . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Three different exostosis ( EXT ) loci on chromosomes 8q ( exostosin 1 , EXT 1 ) , 11p ( exostosin 2 , EXT 2 ) and 19p ( exostosin 3 , EXT 3 ) have been reported . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The Ext 2 animals received the same 10 ray dose , 2 , 4 , 6 , 8 weeks after the transfer to long days and were sampled 10 weeks postirradiation . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Refinement of the multiple exostoses locus ( EXT 2 ) to a 3 cM interval on chromosome 11 . ^^^ EXT is genetically heterogeneous , with at least three loci involved : one ( EXT 1 ) in the Langer Giedion region on 8q23 q 24 , a second ( EXT 2 ) in the pericentromeric region of chromosome 11 , and a third ( EXT 3 ) on chromosome 19p . ^^^ In this study , linkage analysis in seven extended EXT families , all linked to the EXT 2 locus , refined the localization of the EXT 2 gene to a 3 cM region flanked by D11S1355 and D11S1361 / D11S554 . ^^^ This implies that the EXT 2 gene is located at the short arm of chromosome 11 , in band 11p11 p 12 . ^^^ The refined localization of EXT 2 excludes a number of putative candidate genes located in the pericentromeric region of chromosome 11 and facilitates the process of isolating the EXT 2 gene . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Linkage studies have recently suggested that there are three chromosomal locations for EXT genes , 8q24 . 1 ( EXT 1 ) , the pericentric region of 11 ( EXT 2 ) , and 19p ( EXT 3 ) . ^^^ These results indicate that the EXT 2 gene maps to the region containing marker D11S903 , which is flanked by markers D11S1355 and D11S1361 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Four of 17 sporadic tumors showed LOH for markers linked to EXT 1 , and 7 showed LOH for markers linked to EXT 2 on chromosome 11 . ^^^ In all , LOH was observed for markers linked to EXT 1 or EXT 2 in 44 % of the 18 tumors , whereas heterozygosity was retained for markers on 19p linked to EXT 3 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Here , we report on the genetic mapping of a second locus ( EXT 2 ) to the short arm of chromosome 19 by linkage to a microsatellite DNA marker at the D19S221 locus , which gives additional support to the view that EXT is a genetically heterogeneous condition . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The EXT 2 multiple exostoses gene defines a family of putative tumour suppressor genes . ^^^ Here , we report the isolation and characterization of the EXT 2 gene . ^^^ Both EXT 1 and EXT 2 show significant homology with one additional expressed sequence tag , defining a new multigene family of proteins with potential tumour suppressor activity . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Three different EXT loci on chromosomes 8q ( EXT 1 ) , 11p ( EXT 2 ) and 19p ( EXT 3 ) have been reported , and recently the EXT 1 gene was identified by positional cloning . ^^^ To isolate the EXT 2 gene , we constructed a contig of yeast artificial chromosomes ( YAC ) and P 1 clones covering the complete EXT 2 candidate region on chromosome 11p11 p 12 . ^^^ This indicates that this gene is the EXT 2 gene . ^^^ EXT 2 has an open reading frame encoding 718 amino acids with an overall homology of 30 . 9 % with EXT 1 , suggesting that a family of related genes might be responsible for the development of EXT . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| One sporadic chondrosarcoma demonstrated LOH for EXT 1 and EXT 3 , while a second underwent LOH for EXT 2 and chromosome 10 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Genetic linkage of this disorder has been described to three independent loci on chromosomes 8q24 . 1 ( EXT 1 ) , 11p11 13 ( EXT 2 ) , and 19p ( EXT 3 ) . ^^^ The EXT 1 and EXT 2 genes were isolated recently and show extensive sequence homology to each other . ^^^ We have identified a third gene that shows striking sequence similarity to both EXT 1 and EXT 2 at the nucleotide and amino acid sequence levels , and have derived its entire coding sequence . ^^^ Although the mRNA transcribed from this gene is similar in size to that from EXT 1 and EXT 2 , its pattern of expression is quite different . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The a posteriori probability of linkage of the disease to EXT 1 , EXT 2 and EXT 3 was greater than 80 % for 8 / 29 , 5 / 29 and 3 / 29 families , respectively , and did not give evidence of a fourth locus for the disease . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Alterations in at least three genes ( EXT 1 , EXT 2 , and EXT 3 ) can cause this disorder . ^^^ Two of these have been isolated ( EXT 1 and EXT 2 ) and encode related members of a putative tumor suppressor family . ^^^ We report here the genomic structure of the human EXT 2 gene consisting of 14 exons ( plus 2 alternative exons ) covering an estimated 108 kb of chromosome 11p11 13 . ^^^ We have derived the DNA sequences at all exon / intron boundaries throughout this gene information that is important for the detailed study of mutations in EXT 2 . ^^^ We have also characterized the mouse EXT 2 cDNA and have mapped the mouse locus to chromosome 2 between D2Mit15 and Pax 6 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple exostoses ( EXT ) is a genetically heterogeneous bone disorder caused by genes segregating on human chromosomes 8 , 11 , and 19 and designated EXT 1 , EXT 2 and EXT 3 , respectively . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The putative tumor suppressors EXT 1 and EXT 2 are glycosyltransferases required for the biosynthesis of heparan sulfate . ^^^ This protein was identified as EXT 2 . ^^^ Expression of EXT 2 yielded a protein with both glycosyltransferase activities . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Isolation and characterization of the murine homolog of the human EXT 2 multiple exostoses gene . ^^^ To investigate the evolutionary relatedness of EXT genes across species we isolated the mouse EXT 2 cDNA . ^^^ As in the human counterpart , the mouse EXT 2 cDNA contains an open reading frame of 2154 bp encoding a predicted protein of 718 amino acids . ^^^ The nucleic acid sequence is 87 % identical to the human EXT 2 transcript , resulting in an amino acid sequence which is 95 % identical to the human protein . ^^^ The mouse EXT 2 gene also shows significant sequence similarity to the mouse and human EXT 1 gene . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Recently , two homologous genes , EXT 1 and EXT 2 , with a putative tumor suppressor function have been described . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutations in the EXT 1 and EXT 2 genes in hereditary multiple exostoses . ^^^ EXT is genetically heterogeneous , and three loci have been identified so far : EXT 1 , on chromosome 8q23 q 24 ; EXT 2 , on 11p11 p 12 ; and EXT 3 , on the short arm of chromosome 19 . ^^^ The EXT 1 and EXT 2 genes were cloned recently , and they were shown to be homologous . ^^^ We have now analyzed the EXT 1 and EXT 2 genes , in 26 EXT families originating from nine countries , to identify the underlying disease causing mutation . ^^^ Of the 26 families , 10 families had an EXT 1 mutation , and 10 had an EXT 2 mutation . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Genetical heterogeneities have segregated at least on chromosome 8 , 11 , and 19 and been designated EXT 1 , EXT 2 , and EXT 3 , respectively . ^^^ Recently , the responsible genes for EXT 1 and EXT 2 have been isolated and appeared to define a structurally related gene family . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Two homologous genes , EXT 1 and EXT 2 , responsible for the development of benign multiple cartilagenous bone tumors ( exostoses ) on the long bones , have been identified in the past 2 years . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Three chromosomal loci have been implicated in this genetically heterogeneous disease : EXT 1 at 8q24 , EXT 2 at 11p13 , and EXT 3 on 19p . ^^^ EXT 1 and EXT 2 were recently cloned . ^^^ We evaluated 34 families with EXT to estimate the proportion of disease attributable to EXT 1 , EXT 2 , and EXT 3 and to investigate the spectrum of EXT 1 mutations . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Germline mutations in the EXT 1 and EXT 2 genes in Korean patients with hereditary multiple exostoses . ^^^ Recently , EXT 1 and EXT 2 genes were cloned and germline mutations of EXT 1 and EXT 2 were identified in EXT families . ^^^ In this study , we performed a mutational analysis of EXT 1 and EXT 2 genes in eight unrelated Korean EXT families by polymerase chain reaction ( PCR ) single strand conformation polymorphism ( SSCP ) analysis followed by direct DNA sequencing . ^^^ As a result , we were able to identify one family ( SNU OC 3 ) with the EXT 1 mutation and another family ( SNU OC 15 ) with the EXT 2 mutation . ^^^ The EXT 2 mutation identified in the SNU OC 15 family was a missense mutation at codon 85 of exon 2 ( TGC > CGC ) , resulting in an amino acid change from cysteine to arginine . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Identification of mutations in the human EXT 1 and EXT 2 genes ] . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| EXT is genetically heterogeneous , and two genes , EXT 1 and EXT 2 , located on 8q24 and 11p11 p 12 , respectively , have been cloned . ^^^ EXT 1 and EXT 2 mutation analysis was performed in a total of 34 sporadic and hereditary osteochondromas and secondary peripheral chondrosarcomas . ^^^ No mutations were found in the EXT 2 gene . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| It is genetically heterogeneous with at least three chromosomal loci : EXT 1 on 8q24 . 1 , EXT 2 on 11p11 , and EXT 3 on 19p . ^^^ EXT 1 and EXT 2 , the two genes responsible for EXT 1 and EXT 2 , respectively , have been cloned . ^^^ EXT 1 , EXT 2 , and the three EXTLs are homologous with one another . ^^^ We have identified the intron exon boundaries of EXTL 1 and EXTL 3 and analyzed EXT 1 , EXT 2 , EXTL 1 , and EXTL 3 , in 36 Chinese families with EXT , to identify underlying disease related mutations in the Chinese population . ^^^ Of the 36 families , five and 12 family groups have mutations in EXT 1 and EXT 2 , respectively . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| HME is usually caused by defects in either one of two genes , EXT 1 and EXT 2 , which encode enzymes that catalyse the biosynthesis of heparan sulphate , an important component of the extracellular matrix . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| HME results from mutations in one of two homologous genes , EXT 1 and EXT 2 . ^^^ We performed two hybrid screens with a fragment of EXT 2 from the region that is most highly conserved in the gene family and identified two interacting proteins : the tumor necrosis factor type 1 associated protein and a novel UDP GalNAc : poly peptide N acetylgalactosaminyltransferase . ^^^ The EXT 2 GalNAc T 5 interaction provides the first direct physical link between EXT proteins and known components of glycosamino glycan synthesis . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The putative tumor suppressors EXT 1 and EXT 2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate . ^^^ Hereditary multiple exostoses , a dominantly inherited genetic disorder characterized by multiple cartilaginous tumors , is caused by mutations in members of the EXT gene family , EXT 1 or EXT 2 . ^^^ The proteins encoded by these genes , EXT 1 and EXT 2 , are endoplasmic reticulum localized type 2 transmembrane glycoproteins that possess or are tightly associated with glycosyltransferase activities involved in the polymerization of heparan sulfate . ^^^ Here , by testing a cell line with a specific defect in EXT 1 in in vivo and in vitro assays , we show that EXT 2 does not harbor significant glycosyltransferase activity in the absence of EXT 1 . ^^^ Instead , it appears that EXT 1 and EXT 2 form a hetero oligomeric complex in vivo that leads to the accumulation of both proteins in the Golgi apparatus . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| A novel splice site mutation of the EXT 2 gene in a Finnish hereditary multiple exostoses family . ^^^ Using 2 point linkage analysis the EXT phenotype was shown to be linked to the recently cloned EXT 2 gene on chromosome 11p11 . ^^^ The described change is considered to be a novel disease causing mutation in the EXT 2 gene . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Association of EXT 1 and EXT 2 , hereditary multiple exostoses gene products , in Golgi apparatus . ^^^ We prepared the specific antibodies for EXT 1 and EXT 2 , hereditary multiple exostoses ( HME ) gene products , and characterized their expression , subcellular localization , and protein association among EXT members . ^^^ Biochemical analyses indicate that EXT 1 and EXT 2 can associate and form homo / hetero oligomers in vivo with or without HME linked mutations , EXT 1 ( R340C ) and EXT 2 ( D227N ) , when exogenously expressed in COS 7 cells . ^^^ An immunocytochemical analysis showed that both EXT 1 and EXT 2 localized in Golgi apparatus , irrespective of HME mutations . ^^^ An immunohistochemical analysis on developing bones further showed that both EXT 1 and EXT 2 were concomitantly expressed in hypertrophic chondrocytes of forelimb bones from 1 day old neonatal mouse , but down regulated in maturing chondrocytes of developing cartilage from 21 day old mouse . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Molecular basis of multiple exostoses : mutations in the EXT 1 and EXT 2 genes . ^^^ Two genes , EXT 1 and EXT 2 , and at least one other unidentified gene , are known to be involved in the formation of exostoses . ^^^ To date , 49 different EXT 1 and 25 different EXT 2 mutations have been found in EXT patients , and there is evidence that mutations in these two genes are responsible for over 70 % of the EXT cases . ^^^ For EXT 2 , 8 nonsense , 11 frameshift , 3 splice site and 3 missense mutations are described . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Cytoskeletal abnormalities in chondrocytes with EXT 1 and EXT 2 mutations . ^^^ Two HME disease genes , EXT 1 and EXT 2 , have been identified and are expressed ubiquitously . ^^^ In this study , we have characterized exostosis chondrocytes from three patients with HME ( one with EXT 1 and two with EXT 2 germline mutations ) and from one individual with a non HME , isolated exostosis . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Molecular cloning of EXT 2 and EXT 4 gene ] . ^^^ Three genetic loci have been identified at 8q24 . 1 ( EXT 1 ) , 11p11 ( EXT 2 ) and 19p ( EXT 3 ) respectively . ^^^ In this paper , EXT 2 gene was cloned with positional cloning and homologous screening . ^^^ This confirmed that the gene cloned in this paper was EXT 2 gene which locus at 11p11 . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Genetic analyses have revealed HME to be a multigenic disorder linked to three loci on chromosomes 8q24 ( EXT 1 ) , 11p11 13 ( EXT 2 ) , and 19p ( EXT 3 ) . ^^^ The EXT 1 and EXT 2 genes have been cloned and defined as glycosyltransferases involved in the synthesis of heparan sulfate . ^^^ The mouse homologs of EXT 1 and EXT 2 have also been cloned and shown to be 99 % and 95 % identical to their human counterparts , respectively . ^^^ However , in situ hybridization of sectioned embryos revealed remarkable differences in expression profiles of EXT 1 , EXT 2 , and EXTL 1 . ^^^ The identical expression patterns found for the EXT 1 and EXT 2 genes support the recent observation that both proteins form a glycosyltransferase complex . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple exostoses ( HME ) , an autosomal skeletal disorder characterized by cartilage capped excrescences , has been ascribed to mutations in EXT 1 and EXT 2 , two tumor suppressor related genes encoding glycosyltransferases involved in the heparan sulfate proteoglycan ( HSPG ) biosynthesis . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The proteins encoded by the EXT 1 , EXT 2 , and EXTL 2 genes , members of the hereditary multiple exostoses gene family of tumor suppressors , are glycosyltransferases required for the heparan sulfate biosynthesis . ^^^ In the present study , the substrate specificity of a soluble recombinant form of the rib 2 protein was determined and compared with those of the recombinant forms of the mammalian EXT 1 , EXT 2 , and EXTL 2 proteins . ^^^ In contrast , the findings confirmed the previous observations that both the EXT 1 and EXT 2 proteins were heparan sulfate copolymerases with both alpha 1 , 4 N acetylglucosaminyltransferase and beta 1 , 4 glucuronyltransferase activities , which are involved only in the elongation step of the heparan sulfate chain , and that the EXTL 2 protein was an alpha 1 , 4 N acetylglucosaminyltransferase involved only in the initiation of heparan sulfate synthesis . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| For hereditary multiple osteochondromas , two responsible genes , EXT 1 and EXT 2 , have been cloned . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Diminished levels of the putative tumor suppressor proteins EXT 1 and EXT 2 in exostosis chondrocytes . ^^^ The EXT family of putative tumor suppressor genes affect endochondral bone growth , and mutations in EXT 1 and EXT 2 genes cause the autosomal dominant disorder Hereditary Multiple Exostoses ( HME ) . ^^^ We also determined subcellular localization and quantitation of EXT 1 and EXT 2 proteins by immunocytochemistry using antibodies raised against unique peptide epitopes . ^^^ Diminished levels of EXT 1 and EXT 2 protein were found in 9 ( 82 % ) and 5 ( 45 % ) exostosis chondrocyte strains , respectively , and 4 ( 36 % ) were deficient in levels of both proteins . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutation frequencies of EXT 1 and EXT 2 in 43 Japanese families with hereditary multiple exostoses . ^^^ Among the four loci , the exostosis type 1 gene ( EXT 1 ) and type 2 gene ( EXT 2 ) have been cloned . ^^^ Seventeen ( 40 % ) of the 23 families had a mutation in EXT 1 and six ( 14 % ) had a mutation in EXT 2 , suggesting that the former mutations are more frequent than the latter in Japanese EXT families . ^^^ Of the 17 families with EXT 1 mutations , 13 had those causing premature termination of the EXT 1 protein and four showed missense mutations , whereas five of the six families with EXT 2 mutations had those causing premature termination and one showed missense mutation . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The D glucuronyltransferase and N acetyl D glucosaminyltransferase reactions in heparan sulfate biosynthesis have been associated with two genes , EXT 1 and EXT 2 , which are also implicated in the inherited bone disorder , multiple exostoses . ^^^ We therefore expressed EXT 1 and EXT 2 in yeast , which does not synthesize heparan sulfate . ^^^ The recombinant EXT 1 and EXT 2 were both found to catalyze both glycosyltransferase reactions in vitro . ^^^ Coexpression of the two proteins , but not mixing of separately expressed recombinant EXT 1 and EXT 2 , yields hetero oligomeric complexes in yeast and mammalian cells , with augmented glycosyltransferase activities . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The tumor suppressors EXT 1 and EXT 2 are associated with hereditary multiple exostoses and encode bifunctional glycosyltransferases essential for chain polymerization of heparan sulfate ( HS ) and its analog , heparin ( Hep ) . ^^^ Thus , their acceptor specificities of the five family members are overlapping but distinct from each other , except for EXT 1 and EXT 2 with the same specificity . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple exostoses ( HME ) , a dominantly inherited genetic disorder characterized by multiple cartilaginous tumors , is caused by mutations in members of the EXT gene family , EXT 1 or EXT 2 . ^^^ The corresponding gene products , exostosin 1 ( EXT 1 ) and exostosin 2 ( EXT 2 ) , are type 2 transmembrane glycoproteins which form a Golgi localized heterooligomeric complex that catalyzes the polymerization of heparan sulfate ( HS ) . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| A novel deletion mutation of the EXT 2 gene in a large Chinese pedigree with hereditary multiple exostosis . ^^^ Among them , EXT 1 and EXT 2 , which encode enzymes that catalyse the biosynthesis of heparan sulfate , an important component of the extracellular matrix , are responsible for over 70 % of the EXT cases . ^^^ The EXT phenotype was shown to be linked to the EXT 2 gene by using 2 point linkage analysis . ^^^ After polymerase chain reaction ( PCR ) single strand conformation polymorphism ( SSCP ) analysis and DNA sequencing , a previously unreported deletion of a G in exon 3 of EXT 2 gene was observed . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| OBJECTIVES : To identify possible mutations in our previously cloned candidate gene for hereditary multiple exostoses type 2 ( EXT 2 ) in affected members of EXT families so as to confirm that it is the disease causing gene . ^^^ CONCLUSIONS : The identification of the mutation in the candidate gene indicates that this novel gene is responsible for EXT 2 ( one of the disease causing gene of EXT ) . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| EXT is genetically heterogeneous with at least 3 chromosomal loci : EXT 1 ( 8q24 . 1 ) , EXT 2 ( 11p11 p 13 ) , and EXT 3 ( 19p ) . ^^^ We have analyzed the EXT 1 and EXT 2 genes in 9 unrelated EXT families and in a patient with a sporadic osteochondroma , all originating from Italy . ^^^ Three families presented EXT 2 mutations consisting of nucleotide substitutions leading to alterations of the third intron splice site , to an amino acid substitution and to a nonsense mutation . ^^^ The sporadic osteochondroma patient carried a novel missense mutation in exon 11 of EXT 2 gene , leading to an amino acid substitution . ^^^ EXT 2 missense mutations were also confirmed by amino acids conservation between human and mouse and by analysis of a healthy control population . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The EXT 1 and EXT 2 genes from lymphocytes of the affected individuals were analyzed by using denaturing high performance liquid chromatography and direct sequencing . ^^^ EXT 1 is expressed in the brain , and both EXT 1 and EXT 2 proteins are associated with glycosyltransferase activities required for the biosynthesis of heparan sulfate , which also has activity in the brain . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| HME is caused by mutations in the EXT 1 and EXT 2 genes , which have glycosyltransferase activity . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| To test the hypothesis that adjusting semen extender composition and dilution ratio increases sperm quality after thawing , three extenders ( Ext 1 , Ext 2 , Ext 3 ; all with DMSO as a cryoprotectant ) and three dilution ratios ( semen / extender : 1 : 5 , 1 : 9 , 1 : 15 ) were screened . ^^^ This method resulted in 46 + / 3 % motility of the thawed spermatozoa and a mortality rate of 39 + / 4 % whereas Ext 2 and Ext 3 resulted in motility rates of only 10 and 5 % . respectively . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| EXT 1 and EXT 2 function as glycosyltransferases that participate in the biosynthesis of heparan sulfate ( HS ) to modify proteoglycans . ^^^ DNA from the HME exostoses demonstrated heterozygous germline EXT 1 or EXT 2 mutations , and DNA from one solitary exostosis demonstrated a somatic EXT 1 mutation . ^^^ These results indicate that , although multiple mutational events do not occur in the EXT 1 or EXT 2 genes , a complete loss of HS was found in the exostosis growth plates . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| At least 3 loci identified as EXT 1 , EXT 2 and EXT 3 are involved in this skeletal disease . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| EXT 1 and EXT 2 are genes that have been shown to cause hereditary multiple exostosis ( HME ) , a syndrome marked by the formation of bony growths juxtaposed to the growth plate . ^^^ We and others have previously suggested that a two hit mutational model applies to the development of an exostosis where a germline mutation coupled with a somatic mutation results in the loss of EXT 1 or EXT 2 function and subsequent tumor formation . ^^^ This provides limited support for the two hit hypothesis involving the EXT 1 and EXT 2 genes for the development of an exostosis . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple exostoses ( HME , OMIM 133700 , 133701 ) results from mutations in EXT 1 and EXT 2 , genes encoding the copolymerase responsible for heparan sulfate ( HS ) biosynthesis . ^^^ EXT 1 and EXT 2 encode the copolymerase , whereas the roles of the other EXT family members ( EXTL 1 , L 2 , and L 3 ) are less clearly defined . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| This genetically heterozygous disease comprises three chromosomal loci : the EXT 1 gene on chromosome 8q23 q 24 , EXT 2 on 11p11 p 13 , and EXT 3 on 19p . ^^^ Both EXT 1 and EXT 2 have been cloned and defined as a new family of potential tumor suppressor genes in previous work . ^^^ Our results showed that one proband is linked to the EXT 1 locus and three are linked to the EXT 2 locus ; the sporadic case was subsequently found to involve EXT 1 . ^^^ We then identified four new mutations that have not been found in other races : two in EXT 1 frameshift ( K218fsX247 ) and nonsense ( Y468X ) mutations and two in EXT 2 missense ( R223P ) and nonsense ( Y394X ) mutations . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| EXT gene family members including EXT 1 , EXT 2 , and EXTL 2 are glycosyltransferases required for heparan sulfate biosynthesis . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Multiple exosotoses is a dominantly inherited bone disorder caused by defects in EXT 1 and EXT 2 , genes encoding glycosyltransferases involved in heparan sulfate chain elongation . ^^^ EXT 1 and EXT 2 are suggested to be dual glucuronyl / N acetylglucosaminyltransferases , and a heterooligomeric complex of EXT 1 and EXT 2 ( EXT1 / 2 ) is considered to be the biological functional polymerization unit . ^^^ Here , we have investigated the in vitro polymerization capacities of recombinant soluble EXT 1 , EXT 2 , and EXT1 / 2 complex on exogenous oligosaccharide acceptors derived from Escherichia coli K 5 capsular polysaccharide . ^^^ In contrast , incubations with recombinant EXT 2 resulted in the addition of a single glucuronic acid but no further polymerization . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| These advances are reviewed and used as the basis for a revised theory for pathogenesis : A clone of proliferating chondrocytes without functional EXT 1 ( or EXT 2 ) expression fails to produce heparan sulfate ; lack of heparan sulfate at the cell surface disrupts fibroblast growth factor signaling and Indian hedgehog diffusion , leading to focal overproliferation and adjacent bone collar deficiency , respectively ; together these effects are proposed to contribute to osteochondroma pathogenesis . . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple and isolated sporadic exostoses in the same kindred : identification of the causative gene ( EXT 2 ) and detection of a new mutation , nt112delAT , that distinguishes the two phenotypes . ^^^ Both conditions are potentially malignant and both are associated with genetic alterations in either EXT 1 or EXT 2 genes . ^^^ Linkage analysis aimed to discern one of the known EXT genes demonstrated linkage of the HME phenotype to the EXT 2 gene . ^^^ |
|
| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| We have identified and isolated the other two members of the Drosophila EXT family genes , which are named sister of tout velu ( sotv ) and brother of tout velu ( botv ) , and encode Drosophila homologues of vertebrate EXT 2 and EXT like 3 ( EXTL 3 ) , respectively . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Methylation status of EXT 1 and EXT 2 promoters and two mutations of EXT 2 in chondrosarcoma . ^^^ Germline mutation and functional loss of EXT 1 or EXT 2 are commonly found in multiple osteochondromas and predispose to the development of chondrosarcoma . ^^^ Mutations of EXT 1 and EXT 2 have rarely been detected in sporadic secondary chondrosarcomas from osteochondroma ; these frequently display loss of heterozygosity at the EXT 1 and EXT 2 loci , but primary chondrosarcomas typically do not . ^^^ To evaluate promoter methylation ( which is an epigenetic gene silencing mechanism ) of EXT 1 and EXT 2 , we performed methylation specific polymerase chain reaction ( PCR ) for 20 chondrosarcoma cases ( 12 primary , 3 secondary to osteochondroma , 2 secondary to enchondromatosis , 2 extraskeletal ordinary , and 1 clear cell ) and in five cell lines . ^^^ In addition , mutation analysis of the EXT 1 and EXT 2 coding regions was performed using PCR single strand conformation polymorphism and sequencing analysis for 12 of the 20 chondrosarcoma cases ( 8 primary , 1 secondary to enchondromatosis , 1 secondary to osteochondroma , and 2 extraskeletal ordinary ) and five cell lines . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Genetic screening for mutations affecting morphogen signaling pathways in Drosophila has identified three genes , tout velu ( ttv ) , sister of tout velu ( sotv ) , and brother of toutvelu ( botv ) , which encode homologues of human EXT 1 , EXT 2 , and EXTL 3 , respectively . ^^^ In contrast to human , TTV SOTV exhibited no GlcNAcT 1 activity , indicating that BOTV / DEXT3 , which is an EXT Like gene and possesses GlcNAcT 1 activity required for the initiation of HS , is indispensable for the biosynthesis of HS chains in Drosophila . ^^^ Thus , all three EXT members in Drosophila , TTV , SOTV , and BOTV , are required for the biosynthesis of full length HS in Drosophila . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutations were determined by sequencing the EXT 1 and EXT 2 genes . ^^^ There were seven subjects with an EXT 1 mutation and 16 with an EXT 2 mutation . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutation screening of the EXT 1 and EXT 2 genes in patients with hereditary multiple exostoses . ^^^ HME is genetically heterogeneous , with at least three loci , on 8q24 . 1 ( EXT 1 ) , 11p11 p 13 ( EXT 2 ) , and 19p ( EXT 3 ) . ^^^ Both the EXT 1 and EXT 2 genes have been cloned recently and define a new family of potential tumor suppressor genes . ^^^ This is the first study in which mutation screening has been performed for both the EXT 1 and EXT 2 genes prior to any linkage analysis . ^^^ We have screened 17 probands with the HME phenotype , for alterations in all translated exons and flanking intronic sequences , in the EXT 1 and EXT 2 genes , by conformation sensitive gel electrophoresis . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Clonal karyotypic abnormalities of the hereditary multiple exostoses chromosomal loci 8q24 . 1 ( EXT 1 ) and 11p11 12 ( EXT 2 ) in patients with sporadic and hereditary osteochondromas . ^^^ HME is genetically heterogeneous with association of three loci including 8q24 . 1 ( EXT 1 ) , 11p11 12 ( EXT 2 ) , and 19p ( EXT 3 ) . ^^^ CONCLUSIONS : These findings : 1 ) confirm previous observations of 8q24 . 1 karyotypic anomalies in sporadic osteochondroma , 2 ) reveal the presence of somatic chromosomal anomalies in hereditary osteochondromata , 3 ) suggest that similar to hereditary lesions , sporadic osteochondromas also are genetically heterogeneic ( involvement of both 8q24 . 1 and 11p11 12 ) , and 4 ) support the hypothesis that loss or mutation of EXT 1 and EXT 2 , two putative tumor suppressor genes , may be important in the pathogenesis of sporadic as well as hereditary osteochondromata . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Linkage analyses have identified three different genes for HME , EXT 1 on 8q24 . 1 , EXT 2 on 11p11 13 and EXT 3 on 19p ( refs 6 9 ) . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The EXTL 3 ( also called EXTR 1 ) gene was selected as a candidate because of its homology to EXT 1 and EXT 2 , putative tumor suppressor genes . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Comparison of fluorescent single strand conformation polymorphism analysis and denaturing high performance liquid chromatography for detection of EXT 1 and EXT 2 mutations in hereditary multiple exostoses . ^^^ EXT 1 and EXT 2 are two genes responsible for the majority of cases of hereditary multiple exostoses ( HME ) , a dominantly inherited bone disorder . ^^^ In order to develop an efficient screening strategy for mutations in these genes , we performed two independent blind screens of EXT 1 and EXT 2 in 34 unrelated patients with HME , using denaturing high performance liquid chromatography ( DHPLC ) and fluorescent single strand conformation polymorphism analysis ( F SSCP ) . ^^^ The mutation likely to cause HME was found in 29 ( 85 % ) of the 34 probands : in 22 of these ( 76 % ) , the mutation was in EXT 1 ; seven patients ( 24 % ) had EXT 2 mutations . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| After 6 h of incubation , ejaculates diluted in media with a high Ca2+ concentration showed a significantly higher percentage ( means + / SD ) of acrosome reacted spermatozoa [ 64 + / 7 and 58 + / 9 in sperm capacitation medium with ( SP TALP 1 ) and without BSA ( SP TALP 2 ) , respectively ] than those diluted in media with a low Ca2+ concentration [ 36 + / 5 , 39 + / 4 , 18 + / 2 and 20 + / 4 in Canine Capacitation Medium ( CCM ) , Egg Yolk Tris dog semen extender ( EXT 1 ) , Modified Egg Yolk Tris extender ( EXT 2 ) and Modified CCM ( MCCM ) , respectively ] . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The condition is genetically heterogeneous , and at least three genes , ext 1 , ext 2 and ext 3 are involved . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Recent studies have shown that these reactions are catalyzed by a copolymerase encoded by EXT 1 and EXT 2 , members of the exostosin family of putative tumor suppressors linked to hereditary multiple exostoses . ^^^ Expression of EXT 1 corrects the deficiencies in the mutants , whereas EXT 2 and the related EXT like cDNAs do not . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Genetic linkage has identified three different loci for this disease : EXT 1 on 8q , EXT 2 on 11p , and EXT 3 on 19p . ^^^ The EXT 1 and EXT 2 genes were recently isolated and mutation analyses have been performed in a number of patients with different ethnic backgrounds . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Three genetic loci have been identified , of which two ( EXT 1 and EXT 2 ) have tumor suppressor activity . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| It is a genetically heterogeneous condition for which two genes , EXT 1 and EXT 2 , have been isolated . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Although no mutations were found in the EXT 1 and EXT 2 genes , the genes involved in HME , or in exons 5 8 of the p 53 gene , the development of three malignancies before the age of 40 suggests that this patient is genetically prone to malignant transformation . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Hereditary multiple exostoses ( HME ) , a dominantly inherited disorder characterized by multiple cartilaginous tumors , is caused by mutations in the gene for , EXT 1 or EXT 2 . ^^^ Recent studies have revealed that EXT 1 and EXT 2 are required for the biosynthesis of heparan sulfate and exert maximal transferase activity as a complex . ^^^ The expression of EXT 1 is concomitantly upregulated in EXT 2 transgenic and even mutant EXT 2 transgenic mice , suggesting an interactive regulation of EXT 1 and EXT 2 expression . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Various germline mutations of two putative tumor suppressor genes , EXT 1 localized to 8q24 . 1 and EXT 2 localized to 11p11 approximately p 12 , have been demonstrated in HME families . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| After equilibration , the same volume of three different second extenders was added , respectively , to each of the three aliquots : ( A ) Ext 2A ( same composition as Ext 1 except that it contained 7 % glycerol and 1 % Equex STM Paste ) , ( B ) Ext 2B ( same composition as that of Ext 1 except that it contained 7 % glycerol and 1 % Equex Pasta ) , and ( C ) Ext 2 ( Control : same composition as that of Ext 1 except that it contained 7 % glycerol ) . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Gene expression of EXT 1 and EXT 2 during mouse brain development . ^^^ Among them , two enzymes , EXT 1 and EXT 2 , catalyze polymerization of glucuronic acid and N acetylglucosamine , the crucial step of HS synthesis . ^^^ To obtain insight into the roles of HS in neural development , we examined the spatiotemporal expression patterns of EXT 1 and EXT 2 during mice brain development . ^^^ RT PCR analyses showed that expression of EXT 1 and EXT 2 peaks during early postnatal period in the cerebrum and around birth in the cerebellum . ^^^ In situ hybridization revealed that in the embryonic brain , EXT 1 and EXT 2 were localized primarily in the neuroepithelial cells surrounding the lateral ventricles , the mesencephalic vesicle , and the fourth ventricle . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Heparan , the common unsulfated precursor of heparan sulfate ( HS ) and heparin , is synthesized on the glycosaminoglycan protein linkage region tetrasaccharide GlcUA Gal Gal Xyl attached to the respective core proteins presumably by HS co polymerases encoded by EXT 1 and EXT 2 , the genetic defects of which result in hereditary multiple exostoses in humans . ^^^ Although both EXT 1 and EXT 2 exhibit GlcNAc transferase and GlcUA transferase activities required for the HS synthesis , no HS chain polymerization has been demonstrated in vitro using recombinant enzymes . ^^^ Recombinant soluble enzymes expressed by co transfection of EXT 1 and EXT 2 synthesized heparan polymers with average molecular weights greater than 1 . 7 10 105 using UDP [ 3H ] GlcNAc and UDP GlcUA as donors on the recombinant glypican 1 core protein and also on the synthetic linkage region analog GlcUA Gal O C2H4NH benzyloxycarbonyl . ^^^ In contrast , no polymerization was achieved with a mixture of individually expressed EXT 1 and EXT 2 or with acceptor substrates such as N acetylheparosan oligosaccharides or the linkage region tetrasaccharide Ser , which are devoid of a hydrophobic aglycon , suggesting the critical requirement of core protein moieties in addition to the interaction between EXT 1 and EXT 2 for HS polymerization . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Our results may contribute to understanding the biological basis of hereditary multiple exostoses ( HME ) , a disease associated with bone overgrowth that results from mutations in EXT 1 and EXT 2 , the human orthologs of ttv and sotv . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutational defects in either EXT 1 or EXT 2 genes cause multiple exostoses , an autosomal hereditary human disorder . ^^^ The EXT 1 and EXT 2 genes encode glycosyltransferases that play an essential role in heparan sulfate chain elongation . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Screening 18 patients without detectable point mutations in the EXT 1 and EXT 2 genes revealed five cases with deletions of one or more exons : four in EXT 1 and one in EXT 2 . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutations EXT 1 and EXT 2 were almost equally common , and were identified in 83 % of individuals . ^^^ The sites of mutation affected the severity of disease with patients with EXT 1 mutations having a significantly worse condition than those with EXT 2 mutations in three of five parameters of severity ( stature , deformity and functional parameters ) . ^^^ A single sarcoma developed in an EXT 2 mutation carrier , compared with seven in EXT 1 mutation carriers . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Mutation screening of EXT 1 and EXT 2 by direct sequence analysis and MLPA in patients with multiple osteochondromas : splice site mutations and exonic deletions account for more than half of the mutations . ^^^ Multiple osteochondromas ( MO ) is an autosomal dominant condition , caused by mutations in either the EXT 1 or the EXT 2 gene . ^^^ In total , 10 mutations were detected in the EXT 1 and 12 in the EXT 2 gene . ^^^ In patients suspected to be affected by MO , we recommend a quantitative analysis such as MLPA , followed by direct sequence analysis for the screening of the EXT 1 and EXT 2 genes . . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| The most common underlying cause of the disease involves mutations in either the EXT 1 or the EXT 2 gene . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| HME is usually caused by mutations of EXT 1 or EXT 2 . ^^^ OBJECTIVE : The objective of this study was to investigate a three generation Austrian kindred with HME for EXT 1 and EXT 2 mutations and for abnormalities of bone mineral density ( BMD ) . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| Novel EXT 1 and EXT 2 mutations identified by DHPLC in Italian patients with multiple osteochondromas . ^^^ We describe the results of an optimised DHPLC based mutation screening of the EXT 1 and EXT 2 genes in Italian patients affected by multiple osteochondromas [ MO ; also referred to as hereditary multiple exostoses ( HME ) in the literature ] , using a multistep approach . ^^^ In patients who tested normal at DHPLC screening , all EXT 1 and EXT 2 exons and splice site junctions were directly sequenced . ^^^ In 7 informative families , we also performed a pre screening linkage analysis to selectively focus the DHPLC testing on the EXT 1 or EXT 2 gene . ^^^ Twenty four mutations ( 77 % ) were found in EXT 1 and 7 ( 23 % ) in EXT 2 . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| HME results from mutations in EXT 1 and EXT 2 , genes that encode glycosyltransferases that synthesize heparan sulfate chains . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| An optimized DHPLC protocol for molecular testing of the EXT 1 and EXT 2 genes in hereditary multiple osteochondromas . ^^^ MO is caused by mutations in the EXT 1 or EXT 2 genes , which encode glycosyltransferases implicated in heparan sulfate biosynthesis . ^^^ Standard mutation analysis performed by sequencing analysis of all coding exons of the EXT 1 and EXT 2 genes reveals a mutation in approximately 80 % of the MO patients . ^^^ We have now optimized and validated a denaturing high performance liquid chromatography ( DHPLC ) based protocol for screening of all EXT 1 and EXT 2 coding exons in a set of 49 MO patients with an EXT 1 or EXT 2 mutation . ^^^ These include 20 previously described mutations and 29 new mutations 20 new EXT 1 and nine new EXT 2 mutations . ^^^ |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16394 and Q93063 |
Pubmed |
SVM Score :0.0 |
| NA |
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