Show simple item record

Files in this item


Item metadata

dc.contributor.authorBrown, Sharon J.
dc.contributor.authorFuller, Heidi R.
dc.contributor.authorJones, Philip
dc.contributor.authorCaterson, Bruce
dc.contributor.authorShirran, Sally L.
dc.contributor.authorBotting, Catherine H.
dc.contributor.authorRoberts, Sally
dc.identifier.citationBrown , S J , Fuller , H R , Jones , P , Caterson , B , Shirran , S L , Botting , C H & Roberts , S 2017 , ' Contaminants in commercial preparations of ‘purified’ small leucine-rich proteoglycans may distort mechanistic studies ' , Bioscience Reports , vol. 37 , no. 1 .
dc.identifier.otherPURE: 248865743
dc.identifier.otherPURE UUID: 0915a54c-1b42-4918-b9b0-6df32afe7fa1
dc.identifier.otherScopus: 85011571452
dc.identifier.otherORCID: /0000-0003-3516-3507/work/32169102
dc.identifier.otherWOS: 000395096100017
dc.descriptionThe authors are grateful to Genodisc (EC’s 7th Framework Programme (FP7, 2007-2013) under grant agreement no. HEALTH-F2-2008-201626) and the Orthopaedic Institute Ltd for funding.en
dc.description.abstractThis paper reports the perplexing results that came about because of seriously impure commercially available reagents. Commercial reagents and chemicals are routinely ordered by scientists and are expected to have been rigorously assessed for their purity. Unfortunately, we found this assumption to be risky. Extensive work was carried out within our laboratory using commercially-sourced preparations of the small leucine-rich proteoglycans, decorin and biglycan, to investigate their influence on nerve cell growth. Unusual results compelled us to analyse the composition and purity of both preparations of these proteoglycans using both mass spectrometry and Western blotting, with and without various enzymatic deglycosylations. Commercial ‘decorin’ and ‘biglycan’ were found to contain a mixture of proteoglycans including not only both decorin and biglycan but also fibromodulin and aggrecan. The unexpected effects of ‘decorin’ and ‘biglycan’ on nerve cell growth could be explained by these impurities. Decorin and biglycan contain either chondroitin or dermatan sulphate glycosaminoglycan chains whilst fibromodulin only contains keratan sulphate and the large (>2,500 kDa), highly glycosylated aggrecan, contains both keratan and chondroitin sulphate. The different structure, molecular weights and composition of these impurities significantly affected our work and any conclusions that could be made. These findings beg the question as to whether scientists need to verify the purity of each commercially obtained reagent used in their experiments. The implications of these findings are vast, since the effects of these impurities may already have led to inaccurate conclusions and reports in the literature with concomitant loss of researchers’ funds and time.
dc.relation.ispartofBioscience Reportsen
dc.rights© 2017 The Authors. This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).en
dc.subjectCommercial preparationsen
dc.subjectSmall leucine-rich proteoglycans (SLRPs)en
dc.subjectMass spectrometryen
dc.subjectQD Chemistryen
dc.titleContaminants in commercial preparations of ‘purified’ small leucine-rich proteoglycans may distort mechanistic studiesen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

This item appears in the following Collection(s)

Show simple item record