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Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition

In a recent publication in Bioscience Reports “Contaminants in commercial preparations of ‘purified’ small leucine-rich proteoglycans may distort mechanistic studies”, Brown et al. identified by mass spectrometry and immunoblotting that certain commercial preparations of the small leucine-rich prote...

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Autor principal: Adams, Josephine C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5426283/
https://www.ncbi.nlm.nih.gov/pubmed/28356486
http://dx.doi.org/10.1042/BSR20170078
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author Adams, Josephine C.
author_facet Adams, Josephine C.
author_sort Adams, Josephine C.
collection PubMed
description In a recent publication in Bioscience Reports “Contaminants in commercial preparations of ‘purified’ small leucine-rich proteoglycans may distort mechanistic studies”, Brown et al. identified by mass spectrometry and immunoblotting that certain commercial preparations of the small leucine-rich proteoglycans (SLRPs) decorin and biglycan, in fact, contained a mix of several proteoglycans that also included fibromodulin and aggrecan. The preparations were thus not suitable to study specific activities of decorin or biglycan. Decorin and biglycan are widely studied SLRPs that are considered to have highly multi-functional effects on cells. Decorin is of interest as a transforming growth factor-β antagonist and is also finding use in tissue engineering materials. This Commentary discusses Brown et al.’s findings and general issues raised for researchers who work with commercially sourced purified proteoglycans.
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spelling pubmed-54262832017-05-24 Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition Adams, Josephine C. Biosci Rep Commentaries In a recent publication in Bioscience Reports “Contaminants in commercial preparations of ‘purified’ small leucine-rich proteoglycans may distort mechanistic studies”, Brown et al. identified by mass spectrometry and immunoblotting that certain commercial preparations of the small leucine-rich proteoglycans (SLRPs) decorin and biglycan, in fact, contained a mix of several proteoglycans that also included fibromodulin and aggrecan. The preparations were thus not suitable to study specific activities of decorin or biglycan. Decorin and biglycan are widely studied SLRPs that are considered to have highly multi-functional effects on cells. Decorin is of interest as a transforming growth factor-β antagonist and is also finding use in tissue engineering materials. This Commentary discusses Brown et al.’s findings and general issues raised for researchers who work with commercially sourced purified proteoglycans. Portland Press Ltd. 2017-05-11 /pmc/articles/PMC5426283/ /pubmed/28356486 http://dx.doi.org/10.1042/BSR20170078 Text en © 2017 The Author(s). http://creativecommons.org/licenses/by/4.0/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) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentaries
Adams, Josephine C.
Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title_full Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title_fullStr Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title_full_unstemmed Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title_short Caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
title_sort caveat emptor: for researchers, a rose will not smell sweet unless we know its composition
topic Commentaries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5426283/
https://www.ncbi.nlm.nih.gov/pubmed/28356486
http://dx.doi.org/10.1042/BSR20170078
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