Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.

Collagen is the major protein in the extracellular matrix and plays vital roles in tissue development and function. Collagen is also one of the most processed proteins in its biosynthesis. The most prominent post-translational modification (PTM) of collagen is the hydroxylation of Pro residues in th...

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Autores principales:	Michele Kirchner, Haiteng Deng, Yujia Xu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e88d270fa2ff48a68be8772ddbe76c43
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spelling	oai:doaj.org-article:e88d270fa2ff48a68be8772ddbe76c432021-12-02T20:17:29ZHeterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.1932-620310.1371/journal.pone.0250544https://doaj.org/article/e88d270fa2ff48a68be8772ddbe76c432021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0250544https://doaj.org/toc/1932-6203Collagen is the major protein in the extracellular matrix and plays vital roles in tissue development and function. Collagen is also one of the most processed proteins in its biosynthesis. The most prominent post-translational modification (PTM) of collagen is the hydroxylation of Pro residues in the Y-position of the characteristic (Gly-Xaa-Yaa) repeating amino acid sequence of a collagen triple helix. Recent studies using mass spectrometry (MS) and tandem MS sequencing (MS/MS) have revealed unexpected hydroxylation of Pro residues in the X-positions (X-Hyp). The newly identified X-Hyp residues appear to be highly heterogeneous in location and percent occupancy. In order to understand the dynamic nature of the new X-Hyps and their potential impact on applications of MS and MS/MS for collagen research, we sampled four different collagen samples using standard MS and MS/MS techniques. We found considerable variations in the degree of PTMs of the same collagen from different organisms and/or tissues. The rat tail tendon type I collagen is particularly variable in terms of both over-hydroxylation of Pro in the X-position and under-hydroxylation of Pro in the Y-position. In contrast, only a few unexpected PTMs in collagens type I and type III from human placenta were observed. Some observations are not reproducible between different sequencing efforts of the same sample, presumably due to a low population and/or the unpredictable nature of the ionization process. Additionally, despite the heterogeneous preparation and sourcing, collagen samples from commercial sources do not show elevated variations in PTMs compared to samples prepared from a single tissue and/or organism. These findings will contribute to the growing body of information regarding the PTMs of collagen by MS technology, and culminate to a more comprehensive understanding of the extent and the functional roles of the PTMs of collagen.Michele KirchnerHaiteng DengYujia XuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 8, p e0250544 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Michele Kirchner Haiteng Deng Yujia Xu Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
description	Collagen is the major protein in the extracellular matrix and plays vital roles in tissue development and function. Collagen is also one of the most processed proteins in its biosynthesis. The most prominent post-translational modification (PTM) of collagen is the hydroxylation of Pro residues in the Y-position of the characteristic (Gly-Xaa-Yaa) repeating amino acid sequence of a collagen triple helix. Recent studies using mass spectrometry (MS) and tandem MS sequencing (MS/MS) have revealed unexpected hydroxylation of Pro residues in the X-positions (X-Hyp). The newly identified X-Hyp residues appear to be highly heterogeneous in location and percent occupancy. In order to understand the dynamic nature of the new X-Hyps and their potential impact on applications of MS and MS/MS for collagen research, we sampled four different collagen samples using standard MS and MS/MS techniques. We found considerable variations in the degree of PTMs of the same collagen from different organisms and/or tissues. The rat tail tendon type I collagen is particularly variable in terms of both over-hydroxylation of Pro in the X-position and under-hydroxylation of Pro in the Y-position. In contrast, only a few unexpected PTMs in collagens type I and type III from human placenta were observed. Some observations are not reproducible between different sequencing efforts of the same sample, presumably due to a low population and/or the unpredictable nature of the ionization process. Additionally, despite the heterogeneous preparation and sourcing, collagen samples from commercial sources do not show elevated variations in PTMs compared to samples prepared from a single tissue and/or organism. These findings will contribute to the growing body of information regarding the PTMs of collagen by MS technology, and culminate to a more comprehensive understanding of the extent and the functional roles of the PTMs of collagen.
format	article
author	Michele Kirchner Haiteng Deng Yujia Xu
author_facet	Michele Kirchner Haiteng Deng Yujia Xu
author_sort	Michele Kirchner
title	Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
title_short	Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
title_full	Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
title_fullStr	Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
title_full_unstemmed	Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
title_sort	heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/e88d270fa2ff48a68be8772ddbe76c43
work_keys_str_mv	AT michelekirchner heterogeneityinprolinehydroxylationoffibrillarcollagensobservedbymassspectrometry AT haitengdeng heterogeneityinprolinehydroxylationoffibrillarcollagensobservedbymassspectrometry AT yujiaxu heterogeneityinprolinehydroxylationoffibrillarcollagensobservedbymassspectrometry
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Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.

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