Quantitative Top-Down Mass Spectrometry Identifies Proteoforms Differentially Released during Mechanical Stimulation of Mouse Skin

Francie Moehring, Matthew Waas, Theodore R. Keppel, Deepali Rathore, Ashley M. Cowie, Cheryl L. Stucky, Rebekah L. Gundry

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Mechanotransduction refers to the processes whereby mechanical stimuli are converted into electrochemical signals that allow for the sensation of our surrounding environment through touch. Despite its fundamental role in our daily lives, the molecular and cellular mechanisms of mechanotransduction are not yet well-defined. Previous data suggest that keratinocytes may release factors that activate or modulate cutaneous sensory neuron terminals, including small molecules, lipids, peptides, proteins, and oligosaccharides. This study presents a first step toward identifying soluble mediators of keratinocyte-sensory neuron communication by evaluating the potential for top-down mass spectrometry to identify proteoforms released during 1 min of mechanical stimulation of mouse skin from nalve animals. Overall, this study identified 47 proteoforms in the secretome of mouse hind paw skin, of which 14 were differentially released during mechanical stimulation, and includes proteins with known and previously unknown relevance to mechanotransduction. Finally, this study outlines a bioinformatic workflow that merges output from two complementary analysis platforms for top-down data and demonstrates the utility of this workflow for integrating quantitative and qualitative data.

Original languageEnglish (US)
Pages (from-to)2635-2648
Number of pages14
JournalJournal of proteome research
Volume17
Issue number8
DOIs
StatePublished - Aug 3 2018

Keywords

  • keratinocytes
  • label-free quantitation
  • mechanotransduction
  • nociceptor
  • primary afferent
  • proteoforms
  • sensory neuron
  • top-down proteomics
  • touch

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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