{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T12:54:00Z","timestamp":1789736040619,"version":"4.0.1"},"reference-count":30,"publisher":"Oxford University Press (OUP)","issue":"12","license":[{"start":{"date-parts":[[2006,12,1]],"date-time":"2006-12-01T00:00:00Z","timestamp":1164931200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Background: Xylosyltransferase I (XT-I), the key enzyme in the biosynthesis of glycosaminoglycan chains in proteoglycans, has increased activity in the blood serum of patients with connective tissue diseases. Therefore, the measurement of serum XT-I activity is useful to monitor disease activity in these patients.<\/jats:p><jats:p>Methods: We developed an HPLC electrospray ionization tandem mass spectrometry method to assay XT-I activity in serum by use of a synthetic peptide (Bio\u2013BIK-F) as the XT-I substrate. On the basis of XT-I-mediated transfer of D-xylose from UDP-D-xylose to the synthetic peptide to form Bio-BIK-F-Xyl, we determined XT-I activity in human serum samples.<\/jats:p><jats:p>Results: Multiple calibration curves for the analysis of Bio-BIK-F-Xyl exhibited consistent linearity and reproducibility in the range of 0.20\u201320 mg\/L, corresponding to XT-I activity of 1.14\u2013114 mU\/L under assay conditions. The mean (SD, range) XT-I activity values in 30 blood donor sera were 18.4 (3.0, 8.7\u201324.8) mU\/L. The limit of detection and lower limit of quantification were 8.5 \u03bcg\/L (0.05 mU\/L) and 163 \u03bcg\/L Bio-BIK-F-Xyl (0.93 mU\/L XT-I activity), respectively. Interassay imprecision (CV) was 5.4%\u201326.1% in the range of 0.64 to 129 mU\/L, and mean recovery was 107% (range, 96%\u2013129%). Method comparison with the radiochemical assay showed a moderate correlation (r = 0.79). The Passing\u2013Bablok regression line was: radiochemical assay = 0.045 LC-MS\/MS + 0.061 mU\/L, Sy|x = 0.186.<\/jats:p><jats:p>Conclusions: This simple and robust LC-MS\/MS assay permits the rapid and accurate determination of XT-I activity in human serum.<\/jats:p>","DOI":"10.1373\/clinchem.2006.071167","type":"journal-article","created":{"date-parts":[[2006,10,15]],"date-time":"2006-10-15T06:15:25Z","timestamp":1160892925000},"page":"2243-2249","source":"Crossref","is-referenced-by-count":31,"title":["Measurement of Fibrosis Marker Xylosyltransferase I Activity by HPLC Electrospray Ionization Tandem Mass Spectrometry"],"prefix":"10.1093","volume":"52","author":[{"given":"Joachim","family":"Kuhn","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Prante","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein\u2013Westfalen, Universita\u0308tsklinik der Ruhr-Universita\u0308t Bochum, Bad Oeynhausen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sylvia","family":"Scho\u0308n","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein\u2013Westfalen, Universita\u0308tsklinik der Ruhr-Universita\u0308t Bochum, Bad Oeynhausen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Go\u0308tting","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein\u2013Westfalen, Universita\u0308tsklinik der Ruhr-Universita\u0308t Bochum, Bad Oeynhausen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Knut","family":"Kleesiek","sequence":"first","affiliation":[{"name":"Institut fu\u0308r Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein\u2013Westfalen, Universita\u0308tsklinik der Ruhr-Universita\u0308t Bochum, Bad Oeynhausen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2006,12,1]]},"reference":[{"key":"2020022801320128300_R1","doi-asserted-by":"crossref","unstructured":"Stoolmiller AC, Horwitz AL, Dorfman A. Biosynthesis of the chondroitin sulfate proteoglycan: purification and properties of xylosyltransferase. J Biol Chem1972;247:3525-3532.","DOI":"10.1016\/S0021-9258(19)45172-7"},{"key":"2020022801320128300_R2","doi-asserted-by":"crossref","unstructured":"Kearns AE, Campbell SC, Westley J, Schwartz NB. Initiation of chondroitin sulfate biosynthesis: a kinetic analysis of UDP-D-xylose:core protein \u03b2-D-xylosyltransferase. Biochemistry1991;30:7477-7483.","DOI":"10.1021\/bi00244a016"},{"key":"2020022801320128300_R3","doi-asserted-by":"crossref","unstructured":"Kuhn J, Go\u0308tting C, Schno\u0308lzer M, Tore K, Brinkmann T, Kleesiek K. First isolation of human UDP-D-xylose: proteoglycan core protein \u03b2-D-xylosyltransferase secreted from cultured JAR choriocarcinoma cells. J Biol Chem2001;276:4940-4947.","DOI":"10.1074\/jbc.M005111200"},{"key":"2020022801320128300_R4","doi-asserted-by":"crossref","unstructured":"Go\u0308tting C, Kuhn J, Zahn R, Brinkmann T, Kleesiek K. Molecular cloning and expression of human UDP-D-xylose:proteoglycan core protein \u03b2-D-xylosyltransferase and its first isoform XT-II. J Mol Biol2000;304:517-528.","DOI":"10.1006\/jmbi.2000.4261"},{"key":"2020022801320128300_R5","doi-asserted-by":"crossref","unstructured":"Wilson IBH. The never-ending story of peptide O-xylosyltransferase. Cell Mol Life Sci2004;61:794-809.","DOI":"10.1007\/s00018-003-3278-2"},{"key":"2020022801320128300_R6","doi-asserted-by":"crossref","unstructured":"Go\u0308tting C, Sollberg S, Kuhn J, Weilke C, Huerkamp C, Brinkmann T, et al. Serum xylosyltransferase: a new biochemical marker of the sclerotic process in systemic sclerosis. J Invest Dermatol1999;112:919-924.","DOI":"10.1046\/j.1523-1747.1999.00590.x"},{"key":"2020022801320128300_R7","unstructured":"Ka\u0308hnert H, Paddenberg R, Kleesiek K. Simultaneous secretion of xylosyltransferase and chondroitin sulfate proteoglycans in chondrocyte culture. Eur J Clin Chem Clin Biochem1991;29:624-625."},{"key":"2020022801320128300_R8","doi-asserted-by":"crossref","unstructured":"Kitabatake M, Ishikawa H, Maeda H. Immunohistochemical demonstration of proteoglycans in the skin of patients with systemic sclerosis. Br J Dermatol1983;108:257-262.","DOI":"10.1111\/j.1365-2133.1983.tb03962.x"},{"key":"2020022801320128300_R9","doi-asserted-by":"crossref","unstructured":"Ishikawa H, Horiuchi R. Initial change of glycosaminoglycans in systemic scleroderma. Dermatologica1975;150:334-345.","DOI":"10.1159\/000251454"},{"key":"2020022801320128300_R10","doi-asserted-by":"crossref","unstructured":"Akimoto S, Hayashi H, Ishikawa H. Disaccharide analysis of the skin glycosaminoglycans in systemic sclerosis. Br J Dermatol1992;126:29-34.","DOI":"10.1111\/j.1365-2133.1992.tb08399.x"},{"key":"2020022801320128300_R11","doi-asserted-by":"crossref","unstructured":"Higuchi T, Ohnishi K, Hayashi H, Ishikawa O, Miyachi Y. Changes in skin disaccharide components correlate with the severity of sclerotic skin in systemic sclerosis. Acta Derm Venereol1994;74:179-182.","DOI":"10.2340\/0001555574188190"},{"key":"2020022801320128300_R12","doi-asserted-by":"crossref","unstructured":"Campbell P, Jacobsson I, Benzing-Purdie L, Roden L, Fessler JH. Silk\u2014a new substrate for UDP-D-xylose:proteoglycan core protein \u03b2-D-xylosyltransferase. Anal Biochem1984;137:505-516.","DOI":"10.1016\/0003-2697(84)90119-2"},{"key":"2020022801320128300_R13","doi-asserted-by":"crossref","unstructured":"Brinkmann T, Weilke C, Kleesiek K. Recognition of acceptor proteins by UDP-D-xylose proteoglycan core protein \u03b2-D-xylosyltransferase. J Biol Chem1997;272:11171-11175.","DOI":"10.1074\/jbc.272.17.11171"},{"key":"2020022801320128300_R14","doi-asserted-by":"crossref","unstructured":"Weilke C, Brinkmann T, Kleesiek K. Determination of xylosyltransferase activity in serum with recombinant human bikunin as acceptor. Clin Chem1997;43:45-51.","DOI":"10.1093\/clinchem\/43.1.45"},{"key":"2020022801320128300_R15","doi-asserted-by":"crossref","unstructured":"Wilson IBH. Functional characterization of Drosophila melanogaster peptide O-xylosyltransferase, the key enzyme for proteoglycan chain initiation and member of the core 2\/I N-acetylglucosaminyltransferase family. J Biol Chem2002;277:21207-21212.","DOI":"10.1074\/jbc.M201634200"},{"key":"2020022801320128300_R16","doi-asserted-by":"crossref","unstructured":"Kuhn J, Mo\u0308lle K, Brinkmann T, Go\u0308tting C, Kleesiek K. High-density tissue-like cultivation of JAR choriocarcinoma cells for the in vitro production of human xylosyltransferase. J Biotechnol2003;103:191-196.","DOI":"10.1016\/S0168-1656(03)00102-0"},{"key":"2020022801320128300_R17","doi-asserted-by":"crossref","unstructured":"Kuhn J, Mu\u0308ller S, Schno\u0308lzer M, Kempf T, Scho\u0308n S, Brinkmann T, et al. High-level expression and purification of human xylosyltransferase I in High Five insect cells as biochemical active form. Biochem Biophys Res Commun2003;312:537-544.","DOI":"10.1016\/j.bbrc.2003.10.157"},{"key":"2020022801320128300_R18","doi-asserted-by":"crossref","unstructured":"Shah VP, Midha KK, Findlay JW, Hill HM, Hulse JD, McGilveray IJ, et al. Bioanalytical method validation\u2014a revisit with a decade of progress. Pharm Res2000;17:1551-1557.","DOI":"10.1023\/A:1007669411738"},{"key":"2020022801320128300_R19","doi-asserted-by":"crossref","unstructured":"Bossuyt PM, Reitsma JB, Bruns DE, Gatsonis CA, Glasziou PP, Irwig LM, et al. Towards complete and accurate reporting of studies of diagnostic accuracy: the STARD initiative. Clin Chem2003;49:1-6.","DOI":"10.1373\/49.1.1"},{"key":"2020022801320128300_R20","doi-asserted-by":"crossref","unstructured":"Bossuyt PM, Reitsma JB, Bruns DE, Gatsonis CA, Glasziou PP, Irwig LM, et al. The STARD statement for reporting studies of diagnostic accuracy: explanation and elaboration. Clin Chem2003;49:7-18.","DOI":"10.1373\/49.1.7"},{"key":"2020022801320128300_R21","doi-asserted-by":"crossref","unstructured":"Scho\u0308ttler M, Mu\u0308ller S, Scho\u0308n S, Prante C, Kuhn J, Kleesiek K, et al. Serum xylosyltransferase I activity, the new biochemical fibrosis marker, is not affected by renal insufficiency. Clin Biochem2005;38:486-488.","DOI":"10.1016\/j.clinbiochem.2005.02.004"},{"key":"2020022801320128300_R22","doi-asserted-by":"crossref","unstructured":"Koslowski R, Pfeil U, Fehrenbach H, Kasper M, Skutelsky E, Wenzel KW. Changes in xylosyltransferase activity and in proteoglycan deposition in bleomycin-induced lung injury in rat. Eur Respir J2001;18:347-356.","DOI":"10.1183\/09031936.01.00085601"},{"key":"2020022801320128300_R23","doi-asserted-by":"crossref","unstructured":"Kuhn J, Schno\u0308lzer M, Scho\u0308n S, Mu\u0308ller S, Prante C, Go\u0308tting C, et al. Xylosyltransferase I acceptor properties of fibroblast growth factor and its fragment bFGF (1\u201324). Biochem Biophys Res Commun2005;333:156-166.","DOI":"10.1016\/j.bbrc.2005.05.087"},{"key":"2020022801320128300_R24","doi-asserted-by":"crossref","unstructured":"Go\u0308tting C, Hendig D, Adam A, Scho\u0308n S, Schulz V, Szliska C, et al. Elevated xylosyltransferase I activities in pseudoxanthoma elasticum (PXE) patients as a marker of stimulated proteoglycan biosynthesis. J Mol Med2005;83:984-992.","DOI":"10.1007\/s00109-005-0693-x"},{"key":"2020022801320128300_R25","doi-asserted-by":"crossref","unstructured":"Scho\u0308n S, Huep G, Prante C, Mu\u0308ller S, Christ R, Hagena FW, et al. Mutational and functional analyses of xylosyltransferases and their implication in osteoarthritis. Osteoarthritis Cartilage2006;14:442-448.","DOI":"10.1016\/j.joca.2005.11.004"},{"key":"2020022801320128300_R26","doi-asserted-by":"crossref","unstructured":"Kleesiek K, Reinards R, Okusi J, Wolf B, Greiling H. UDP-D-xylose: core protein \u03b2-D-xylosyltransferase: a new marker of cartilage destruction in chronic joint disease. J Clin Chem Clin Biochem1987;25:473-481.","DOI":"10.1515\/cclm.1987.25.8.473"},{"key":"2020022801320128300_R27","doi-asserted-by":"crossref","unstructured":"Keevil BG, Tierney DP, Cooper DP, Morris MR. Rapid liquid chromatography-tandem mass spectrometry method for routine analysis of cyclosporin over an extended concentration range. Clin Chem2002;48:69-76.","DOI":"10.1093\/clinchem\/48.1.69"},{"key":"2020022801320128300_R28","doi-asserted-by":"crossref","unstructured":"Streit F, Shipkova M, Armstrong VW, Oellerich M. Validation of a rapid and sensitive liquid chromatography-tandem mass spectrometry method for free and total mycophenolic acid. Clin Chem2004;50:152-159.","DOI":"10.1373\/clinchem.2003.024323"},{"key":"2020022801320128300_R29","doi-asserted-by":"crossref","unstructured":"Maunsell Z, Wright DJ, Rainbow SJ. Routine isotope-dilution liquid chromatography-tandem mass spectrometry assay for simultaneous measurement of the 25-hydroxy metabolites of vitamins D2 and D3. Clin Chem2005;51:1683-1690.","DOI":"10.1373\/clinchem.2005.052936"},{"key":"2020022801320128300_R30","doi-asserted-by":"crossref","unstructured":"Kuhn J, Go\u0308tting C, Kleesiek K. Rapid micro-scale assay for homocysteine by liquid chromatography-tandem mass spectrometry. Clin Biochem2006;39:164-166.","DOI":"10.1016\/j.clinbiochem.2005.11.009"}],"container-title":["Clinical Chemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/clinchem\/article-pdf\/52\/12\/2243\/32687246\/clinchem2243.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/clinchem\/article-pdf\/52\/12\/2243\/32687246\/clinchem2243.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,2,7]],"date-time":"2024-02-07T14:05:28Z","timestamp":1707314728000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/clinchem\/article\/52\/12\/2243\/5626700"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,12,1]]},"references-count":30,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2006,12,1]]},"published-print":{"date-parts":[[2006,12,1]]}},"URL":"https:\/\/doi.org\/10.1373\/clinchem.2006.071167","relation":{},"ISSN":["0009-9147","1530-8561"],"issn-type":[{"value":"0009-9147","type":"print"},{"value":"1530-8561","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2006,12,1]]},"published":{"date-parts":[[2006,12,1]]}}}