Proteomic Profiling of the Extracellular Vesicle Chaperone in Cancer

Kisho Ono, Takanori Eguchi

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Citation (Scopus)

Abstract

Molecular chaperones are widely distributed intracellular proteins that play essential roles in maintaining proteome function by assisting in the folding of client proteins. Molecular chaperones, such as heat shock proteins (HSPs), are found intracellularly and extracellularly. Extracellular vesicles (EVs), such as exosomes, contain HSPs and horizontally transfer the functional chaperones into various recipient cells. Besides, mass spectrometry has enabled a comprehensive analysis of exosomal and EV proteins, which is useful in basic biomedical research to clinical biomarker search. We have performed deep proteome analysis of EVs, including exosomes, from metastatic tongue and prostate cancers and detected >700 protein types, including cytoplasmic, ER, mitochondrial, small, and large HSPs. Here, we provide protocols for isolating exosomes/EVs and deep proteome analysis to detect the EV chaperone.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages233-249
Number of pages17
DOIs
Publication statusPublished - 2023

Publication series

NameMethods in Molecular Biology
Volume2693
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Chaperone proteins
  • Exosome isolation methods
  • Extracellular vesicles
  • Heat shock protein
  • Mass spectrometry
  • Proteome analysis

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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