Dataset Information

A quantitative label-free analysis of the extracellular proteome of human supraspinatus reveals damage to the pericellular and elastic fibre niches in torn and aged tendons

ABSTRACT: Tears of the human supraspinatus tendon are common and often cause painful and debilitating loss of function. Progressive failure of the tendon leading to structural abnormality and tearing is accompanied by numerous cellular and extra-cellular matrix (ECM) changes in the tendon tissue. This proteomics study aimed to compare torn and aged rotator cuff tissue to young and healthy tissue, and provide the first ECM inventory of human supraspinatus tendon generated using label-free quantitative LC-MS/MS. Employing two digestion protocols (trypsin and elastase), we analysed grain-sized tendon supraspinatus biopsies from older patients with torn tendons and from young controls. Our findings confirm measurable degradation of collagen fibrils and associated proteins in old and torn tendons, suggesting a significant loss of tissue organisation. A particularly marked reduction of cartilage oligomeric matrix protein (COMP) raises the possibility of using changes in levels of this glycoprotein as a marker of abnormal tissue, as previously suggested in horse models. Surprisingly, and despite using an elastase digestion for validation, elastin was not detected, raising the possibility that it is not highly abundant in human supraspinatus tendon. Finally, we identified marked changes to the elastic fibre, fibrillin-rich niche and the pericellular matrix. Further investigation of these regions may yield other potential biomarkers and help to explain detrimental cellular processes associated with tendon ageing and tendinopathy.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Tendon

SUBMITTER: Philip Charles

LAB HEAD: Benedikt Kessler

PROVIDER: PXD006466 | Pride | 2018-07-03

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20130925_Osnat_PRG_elastase.mgf	Mgf
	20130925_Osnat_PRG_elastase.pride.mgf.gz	Mgf
	20130925_Osnat_PRG_trypsin.mgf	Mgf
	20130925_Osnat_PRG_trypsin.pride.mgf.gz	Mgf
	OTE0052_Osnat_elas_C1.raw	Raw

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A quantitative label-free analysis of the extracellular proteome of human supraspinatus tendon reveals damage to the pericellular and elastic fibre niches in torn and aged tissue.

Hakimi Osnat O Ternette Nicola N Murphy Richard R Kessler Benedikt M BM Carr Andrew A

PloS one 20170518 5

Tears of the human supraspinatus tendon are common and often cause painful and debilitating loss of function. Progressive failure of the tendon leading to structural abnormality and tearing is accompanied by numerous cellular and extra-cellular matrix (ECM) changes in the tendon tissue. This proteomics study aimed to compare torn and aged rotator cuff tissue to young and healthy tissue, and provide the first ECM inventory of human supraspinatus tendon generated using label-free quantitative LC-M ...[more]

PMID: 28542244

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