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Mass spectrometry detection of photodamage in human extracellular matrix assemblies

ABSTRACT: Photoageing in skin is commonly recognised by architectural remodelling of dermal extracellular matrix components. Mass spectrometry was previously used to identify tissue-specific patterns of fibrillin-1 and collagen VI peptide spectrum matches (PXD008450). This study aimed to determine if the same mass spectrometry-based approach could detect peptide spectrum match patterns and significantly differences in relative abundance of peptide sequences characteristic of damage following exposure to UVR of co-purified suspensions of fibrillin and collagen VI microfibrils. Human dermal fibroblast-derived suspensions of microfibrils were irradiated with either broadband UVB or solar simulated radiation (SSR). UVR-induced molecular damage was characterised by proteolytic peptide generation with elastase followed by liquid chromatography tandem mass spectrometry (LC-MS/MS). This allowed the molecular scale identification of UV-induced structural changes within two skin matrix assemblies. The proteomic approaches used have the potential to facilitate the rapid, protein-specific identification of differential molecular fingerprints of damage in key extracellular matrix proteins.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Alexander Eckersley

LAB HEAD: Michael Sherratt

PROVIDER: PXD015149 | Pride | 2020-01-30

REPOSITORIES: Pride

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