{"id":233,"date":"2019-04-05T11:02:12","date_gmt":"2019-04-05T09:02:12","guid":{"rendered":"https:\/\/web.umons.ac.be\/smos\/?p=233"},"modified":"2022-05-24T11:04:30","modified_gmt":"2022-05-24T09:04:30","slug":"new-paper-in-the-collaboration-with-the-erasmus-university-medical-center","status":"publish","type":"post","link":"https:\/\/web.umons.ac.be\/smos\/2019\/04\/05\/new-paper-in-the-collaboration-with-the-erasmus-university-medical-center\/","title":{"rendered":"New paper in the collaboration with the Erasmus University Medical Center"},"content":{"rendered":"<figure id=\"attachment_234\" aria-describedby=\"caption-attachment-234\" style=\"width: 571px\" class=\"wp-caption alignnone\"><img loading=\"lazy\" decoding=\"async\" class=\"wp-image-234 size-full\" src=\"https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05.png\" alt=\"New paper in the collaboration with the Erasmus University Medical Center\" width=\"571\" height=\"418\" srcset=\"https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05.png 571w, https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05-300x220.png 300w, https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05-30x22.png 30w, https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05-60x44.png 60w, https:\/\/web.umons.ac.be\/app\/uploads\/sites\/80\/2022\/05\/article-2019-04-05-360x264.png 360w\" sizes=\"auto, (max-width: 571px) 100vw, 571px\" \/><figcaption id=\"caption-attachment-234\" class=\"wp-caption-text\">Figure : Ratio between the modified and unmodified peptides (GLHGEFGLP(4Hyp)GP(Pro)AGPR and GLHGEFGLP(4Hyp)GP(?xHyp)AGPR, respectively)<\/figcaption><\/figure>\n<p>&nbsp;<\/p>\n<p>A paper entitled \u201cIdentification of 4-Hydroxyproline at the Xaa Position in Collagen by Mass Spectrometry\u201d has just been accepted for publication in the Journal of Proteome Research, an ACS scientific journal.<\/p>\n<p>The paper concerns the identification of an enzymatic structural modification of the proline residues of collagen by mass spectrometry.<\/p>\n<p>Collagen has a triple helix form, structured by a [-Gly-Xaa-Yaa-] repetition, where Xaa and Yaa are amino acids. This repeating unit can be post-translationally modified by enzymes, where proline is often hydroxylated into hydroxyproline (Hyp). Two Hyp isomers occur in collagen: 4-hydroxyproline (4Hyp) and 3-hydroxyproline (3Hyp).<\/p>\n<p>We showed that proline, at position 584 in COL1A2, has a lower rate of modification in colorectal liver metastasis tissue than in healthy liver, but the isomeric identity of ?xHyp, i.e. 3- and\/or 4Hyp, remained unknown.<\/p>\n<p>We here present a proof of principle identification of ?xHyp. This identification is based on liquid chromatography retention time differences and mass spectrometry using ETD-HCD fragmentation, complemented by ab initio calculations.<\/p>\n<p>Both techniques identify ?xHyp at position 584 in COL1A2 as 4-hydroxyproline (4xHyp).<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>A paper entitled \u201cIdentification of 4-Hydroxyproline at the Xaa Position in Collagen by Mass Spectrometry\u201d has just been accepted for publication in the Journal of Proteome Research, an ACS scientific journal.<\/p>\n","protected":false},"author":157,"featured_media":234,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[47],"tags":[],"class_list":["post-233","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-recherche"],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v25.1 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>New paper in the collaboration with the Erasmus University Medical Center - 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