Potential implications of the glycosylation patterns in collagen α1(I) and α2(I) chains for fibril assembly and growth

[Display omitted] •Post-translational modifications of collagen from four animals are identified.•Nine new hydroxylysine glycosylation sites identified in collagen Type I.•Lysine oxidation patterns in collagen type I display species variation.•d-periodic axial distribution of glycosylated hydroxylys...

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Published inJournal of structural biology Vol. 215; no. 1; p. 107938
Main Authors Visser, D.R., Loo, T.S., Norris, G.E, Parry, David A.D.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.03.2023
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Abstract [Display omitted] •Post-translational modifications of collagen from four animals are identified.•Nine new hydroxylysine glycosylation sites identified in collagen Type I.•Lysine oxidation patterns in collagen type I display species variation.•d-periodic axial distribution of glycosylated hydroxylysines implies a structural role.•Glycosylated lysine residues may play a part in assembly and size limitation of fibrils. O-Glycosylation of hydroxylysine (Hyl) in collagen occurs at an early stage of biosynthesis before the triple-helix has formed. This simple post-translational modification (PTM) of lysine by either a galactosyl or glucosylgalactosyl moiety is highly conserved in collagens and depends on the species, type of tissue and the collagen amino acid sequence. The structural/functional reason why only specific lysines are modified is poorly understood, and has led to increased efforts to map the sites of PTMs on collagen sequences from different species and to ascertain their potential role in vivo. To investigate this, we purified collagen type I (Col1) from the skins of four animals, then used mass spectrometry and proteomic techniques to identify lysines that were oxidised, galactosylated, glucosylgalactosylated, or glycated in its mature sequence. We found 18 out of the 38 lysines in collagen type Iα1, (Col1A1) and 7 of the 30 lysines in collagen type Iα2 (Col1A2) were glycosylated. Six of these modifications had not been reported before, and included a lysine involved in crosslinking collagen molecules. A Fourier transform analysis of the positions of the glycosylated hydroxylysines showed they display a regular axial distribution with the same d-period observed in collagen fibrils. The significance of this finding in terms of the assembly of collagen molecules into fibrils and of potential restrictions on the growth of the collagen fibrils is discussed.
AbstractList [Display omitted] •Post-translational modifications of collagen from four animals are identified.•Nine new hydroxylysine glycosylation sites identified in collagen Type I.•Lysine oxidation patterns in collagen type I display species variation.•d-periodic axial distribution of glycosylated hydroxylysines implies a structural role.•Glycosylated lysine residues may play a part in assembly and size limitation of fibrils. O-Glycosylation of hydroxylysine (Hyl) in collagen occurs at an early stage of biosynthesis before the triple-helix has formed. This simple post-translational modification (PTM) of lysine by either a galactosyl or glucosylgalactosyl moiety is highly conserved in collagens and depends on the species, type of tissue and the collagen amino acid sequence. The structural/functional reason why only specific lysines are modified is poorly understood, and has led to increased efforts to map the sites of PTMs on collagen sequences from different species and to ascertain their potential role in vivo. To investigate this, we purified collagen type I (Col1) from the skins of four animals, then used mass spectrometry and proteomic techniques to identify lysines that were oxidised, galactosylated, glucosylgalactosylated, or glycated in its mature sequence. We found 18 out of the 38 lysines in collagen type Iα1, (Col1A1) and 7 of the 30 lysines in collagen type Iα2 (Col1A2) were glycosylated. Six of these modifications had not been reported before, and included a lysine involved in crosslinking collagen molecules. A Fourier transform analysis of the positions of the glycosylated hydroxylysines showed they display a regular axial distribution with the same d-period observed in collagen fibrils. The significance of this finding in terms of the assembly of collagen molecules into fibrils and of potential restrictions on the growth of the collagen fibrils is discussed.
O-Glycosylation of hydroxylysine (Hyl) in collagen occurs at an early stage of biosynthesis before the triple-helix has formed. This simple post-translational modification (PTM) of lysine by either a galactosyl or glucosylgalactosyl moiety is highly conserved in collagens and depends on the species, type of tissue and the collagen amino acid sequence. The structural/functional reason why only specific lysines are modified is poorly understood, and has led to increased efforts to map the sites of PTMs on collagen sequences from different species and to ascertain their potential role in vivo. To investigate this, we purified collagen type I (Col1) from the skins of four animals, then used mass spectrometry and proteomic techniques to identify lysines that were oxidised, galactosylated, glucosylgalactosylated, or glycated in its mature sequence. We found 18 out of the 38 lysines in collagen type Iα1, (Col1A1) and 7 of the 30 lysines in collagen type Iα2 (Col1A2) were glycosylated. Six of these modifications had not been reported before, and included a lysine involved in crosslinking collagen molecules. A Fourier transform analysis of the positions of the glycosylated hydroxylysines showed they display a regular axial distribution with the same d-period observed in collagen fibrils. The significance of this finding in terms of the assembly of collagen molecules into fibrils and of potential restrictions on the growth of the collagen fibrils is discussed.
ArticleNumber 107938
Author Parry, David A.D.
Visser, D.R.
Norris, G.E
Loo, T.S.
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Issue 1
Keywords Fibrillogenesis
Glycosylation
Collagen type I
Mass spectrometry
Periodicity
Language English
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Snippet [Display omitted] •Post-translational modifications of collagen from four animals are identified.•Nine new hydroxylysine glycosylation sites identified in...
O-Glycosylation of hydroxylysine (Hyl) in collagen occurs at an early stage of biosynthesis before the triple-helix has formed. This simple post-translational...
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StartPage 107938
SubjectTerms Animals
Collagen - metabolism
Collagen type I
Collagen Type I - metabolism
Fibrillogenesis
Glycosylation
Lysine - metabolism
Mass spectrometry
Periodicity
Proteomics
Title Potential implications of the glycosylation patterns in collagen α1(I) and α2(I) chains for fibril assembly and growth
URI https://dx.doi.org/10.1016/j.jsb.2023.107938
https://www.ncbi.nlm.nih.gov/pubmed/36641113
https://search.proquest.com/docview/2765778217
Volume 215
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