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Glycosylation Patterns on Collagen α1(I) and Collagen α2(I) resemble a lock and key arrangement

ABSTRACT: Col1 from the skins of 4 animals (cow, deer, goat and sheep) were purified, then used mass spectrometry and proteomic techniques to identify lysines that were oxidised, galactosylated, glucosylgalactosylated, or glycated in its ma-ture sequence. We found 18 out of the 38 lysines in collagen type 1α1, (Col1A1) and 7 of the 30 lysines in collagen type 1α2 (Col1A2) were glycosylated. Six of these modifications had not been reported before, and included a lysine involved in cross linking collagen molecules. Mapping the positions of these modifications on the ColA1 and Col1A2 sequences showed they were complimentary and resembled a lock and key arrangement.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Bos Taurus (bovine) Capra Hircus X Ovis Aries

TISSUE(S): Skin

SUBMITTER: Trevor Loo

LAB HEAD: Gill Norris

PROVIDER: PXD036507 | Pride | 2023-05-24

REPOSITORIES: Pride

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			Action	DRS
	20190311_Tryptic_ACN1_Researched.msf	Msf
	20190311_Tryptic_ACN1_Researched.msfView	Msf
	20190311_Tryptic_ACN1_Researched.pdResult	Other

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Project description:Collagen deposition is a key process during idiopathic pulmonary fibrosis (IPF); however, little is known about the dynamics of collagen formation during disease development. Tissue samples of early stages of human disease are not readily available and it is difficult to identify changes in collagen content, since standard collagen analysis does not distinguish between 'old' and 'new' collagen. Therefore, the current study aimed to (i) investigate the dynamics of new collagen formation in mice using bleomycin-induced lung fibrosis in which newly synthesized collagen was labelled with deuterated water and (ii) use this information to identify genes and processes correlated to new collagen formation from gene expression analysis. Lung fibrosis was induced in female C57BL/6 mice by bleomycin instillation and sacrificed. Animals were sacrificed at 1 to 5 weeks after fibrosis induction. Collagen synthesized during the week before sacrifice was labelled with deuterium by providing mice with deuterated drinking water. After sacrifice, lung tissue was collected for microarray analysis, determination of new collagen formation, and histology. Deuterated water labelling showed a strong increase in new collagen formation already during the first week after fibrosis induction and a complete return to baseline at five weeks. Correlation of new collagen formation data with gene expression data revealed fibrosis specific processes, of which proliferation was an unexpected one. This was confirmed by measuring cell proliferation and collagen synthesis simultaneously using deuterated water incorporation. Furthermore, new collagen formation strongly correlated with gene expression of e.g. elastin, tenascin C, MMP-14, lysyl oxidase, and type V collagen. These data demonstrate, using a novel combination of technologies, that proliferation and extracellular matrix production are correlated to the core process of fibrosis, i.e. the formation of new collagen. In addition, it identified genes directly correlated to fibrosis, thus providing more insight into the aetiology of IPF. Total RNA was obtained from mouse lungs at timepoint 0 as a control (n = 7) or timepoints 1 (n = 7), 2 (n = 6), 3 (n = 6), 4 (n = 6) or 5 (n = 6) weeks after bleomycin-instillation to induce lung fibrosis.

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Glycosylation Patterns on Collagen α1(I) and Collagen α2(I) resemble a lock and key arrangement

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