Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II. Götting, C., Kuhn, J., Zahn, R., Brinkmann, T., & Kleesiek, K. Journal of Molecular Biology, 304(4):517-528, Academic Press, 12, 2000. ![Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II [pdf]](https://bibbase.org/img/filetypes/pdf.svg "pdf")
Paper abstract bibtex Human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading flame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94 % identity to the corresponding human enzyme. (C) 2000 Academic Press.
@article{
title = {Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II},
type = {article},
year = {2000},
identifiers = {[object Object]},
keywords = {Chondroitin sulfate,Glycosyltransferase,Heparan sulfate,Proteoglycan,Xylosyltransferase},
pages = {517-528},
volume = {304},
month = {12},
publisher = {Academic Press},
day = {8},
id = {26168b49-55eb-327b-9cb2-ec1210dc11d3},
created = {2020-04-06T15:50:59.618Z},
accessed = {2020-03-10},
file_attached = {true},
profile_id = {f2cdae9b-bb24-326a-a6de-4643b6dd80bc},
group_id = {b4569066-6232-3efc-bd6a-2e69a994cdae},
last_modified = {2020-04-06T15:50:59.900Z},
read = {false},
starred = {false},
authored = {false},
confirmed = {false},
hidden = {false},
folder_uuids = {eef7c586-4fee-4bcb-a7e6-090f8b72d2c9},
private_publication = {false},
abstract = {Human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading flame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94 % identity to the corresponding human enzyme. (C) 2000 Academic Press.},
bibtype = {article},
author = {Götting, Christian and Kuhn, Joachim and Zahn, Roland and Brinkmann, Thomas and Kleesiek, Knut},
journal = {Journal of Molecular Biology},
number = {4}
}
Downloads: 0
{"_id":"pwYK3mKvrF6nzh3s7","bibbaseid":"gtting-kuhn-zahn-brinkmann-kleesiek-molecularcloningandexpressionofhumanudpdxyloseproteoglycancoreproteindxylosyltransferaseanditsfirstisoformxtii-2000","authorIDs":[],"author_short":["Götting, C.","Kuhn, J.","Zahn, R.","Brinkmann, T.","Kleesiek, K."],"bibdata":{"title":"Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II","type":"article","year":"2000","identifiers":"[object Object]","keywords":"Chondroitin sulfate,Glycosyltransferase,Heparan sulfate,Proteoglycan,Xylosyltransferase","pages":"517-528","volume":"304","month":"12","publisher":"Academic Press","day":"8","id":"26168b49-55eb-327b-9cb2-ec1210dc11d3","created":"2020-04-06T15:50:59.618Z","accessed":"2020-03-10","file_attached":"true","profile_id":"f2cdae9b-bb24-326a-a6de-4643b6dd80bc","group_id":"b4569066-6232-3efc-bd6a-2e69a994cdae","last_modified":"2020-04-06T15:50:59.900Z","read":false,"starred":false,"authored":false,"confirmed":false,"hidden":false,"folder_uuids":"eef7c586-4fee-4bcb-a7e6-090f8b72d2c9","private_publication":false,"abstract":"Human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading flame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94 % identity to the corresponding human enzyme. (C) 2000 Academic Press.","bibtype":"article","author":"Götting, Christian and Kuhn, Joachim and Zahn, Roland and Brinkmann, Thomas and Kleesiek, Knut","journal":"Journal of Molecular Biology","number":"4","bibtex":"@article{\n title = {Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II},\n type = {article},\n year = {2000},\n identifiers = {[object Object]},\n keywords = {Chondroitin sulfate,Glycosyltransferase,Heparan sulfate,Proteoglycan,Xylosyltransferase},\n pages = {517-528},\n volume = {304},\n month = {12},\n publisher = {Academic Press},\n day = {8},\n id = {26168b49-55eb-327b-9cb2-ec1210dc11d3},\n created = {2020-04-06T15:50:59.618Z},\n accessed = {2020-03-10},\n file_attached = {true},\n profile_id = {f2cdae9b-bb24-326a-a6de-4643b6dd80bc},\n group_id = {b4569066-6232-3efc-bd6a-2e69a994cdae},\n last_modified = {2020-04-06T15:50:59.900Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n folder_uuids = {eef7c586-4fee-4bcb-a7e6-090f8b72d2c9},\n private_publication = {false},\n abstract = {Human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase (EC 2.4.2.26, XT-I) initiates the biosynthesis of glycosaminoglycan chains in proteoglycans by transferring xylose from UDP-xylose to specific serine residues of the core protein. Based on the partial amino acid sequence of the purified enzyme from human JAR choriocarcinoma cell culture supernatant we isolated a cDNA encoding XT-I using the degenerate reverse transcriptase-polymerase chain reaction method. This enzyme, which is involved in chondroitin sulfate, heparan sulfate, heparin and dermatan sulfate biosynthesis, belongs to a novel family of glycosyltransferases with no homology to proteins known so far. 5' and 3'-RACE were performed to isolate a novel cDNA fragment of 3726 bp with a single open reading flame encoding at least 827 amino acid residues with a molecular mass of 91 kDa. The human XT-I gene was located on chromosome 16p13.1 using radiation hybrid mapping, and extracts from CHO-K1 cells transfected with the XT-I cDNA in an expression vector exhibited marked XT activity. A new 3608 bp cDNA fragment encoding a protein of 865 amino acid residues was also isolated by PCR using degenerate primers based on the amino acid sequence of human XT-I. The amino acid sequence of this XT-II isoform displayed 55% identity to the human XT-I. The XT-II gene was located on chromosome 17q21.3-17q22, and the exon/intron structure of the 15 kb gene was determined. RT-PCR analyses of XT-I and XT-II mRNA from various tissues confirmed that both XT-I and XT-II transcripts are ubiquitously expressed in the human tissues, although with different levels of transcription. Furthermore, the cDNAs encoding XT-I and XT-II from rat were cloned. The deduced amino acid sequences of rat xylosyltransferases displayed 94 % identity to the corresponding human enzyme. (C) 2000 Academic Press.},\n bibtype = {article},\n author = {Götting, Christian and Kuhn, Joachim and Zahn, Roland and Brinkmann, Thomas and Kleesiek, Knut},\n journal = {Journal of Molecular Biology},\n number = {4}\n}","author_short":["Götting, C.","Kuhn, J.","Zahn, R.","Brinkmann, T.","Kleesiek, K."],"urls":{"Paper":"https://bibbase.org/service/mendeley/f2cdae9b-bb24-326a-a6de-4643b6dd80bc/file/68d18406-d3e3-930f-21d7-31dd61072bb2/full_text.pdf.pdf"},"bibbaseid":"gtting-kuhn-zahn-brinkmann-kleesiek-molecularcloningandexpressionofhumanudpdxyloseproteoglycancoreproteindxylosyltransferaseanditsfirstisoformxtii-2000","role":"author","keyword":["Chondroitin sulfate","Glycosyltransferase","Heparan sulfate","Proteoglycan","Xylosyltransferase"],"downloads":0},"bibtype":"article","creationDate":"2020-04-07T17:42:59.933Z","downloads":0,"keywords":["chondroitin sulfate","glycosyltransferase","heparan sulfate","proteoglycan","xylosyltransferase"],"search_terms":["molecular","cloning","expression","human","udp","xylose","proteoglycan","core","protein","xylosyltransferase","first","isoform","götting","kuhn","zahn","brinkmann","kleesiek"],"title":"Molecular cloning and expression of human UDP-D-xylose: Proteoglycan core protein β-D-xylosyltransferase and its first isoform XT-II","year":2000}