S100A8/A9 amyloidosis in the ageing prostate: Relating ex vivo and in vitro studies

Anna L. Gharibyan, Dina Raveh, Ludmilla A. Morozova-Roche

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

6 Scopus citations


The family of S100 proteins encompasses more than 20 members characterized by remarkable conformational and functional diversity. S100 proteins act as central regulators of various cellular processes, including cell survival, proliferation, differentiation, and motility. Many S100 proteins are implicated in various types of cancer as well as neurodegenerative, inflammatory, and autoimmune diseases. Recently, we have found that S100A8âA9 proteins are involved in amyloidogenic process in the ageing prostate, contributing to the formation of calcified corpora amylacea (CA) inclusions, which commonly accompany age-dependent prostate tissue remodelling and cancer. Amyloid formation by S100A8/A9 proteins can also be modelled in vitro. Amyloid assembly of S100A8/A9 proteins into oligomeric and fibrillar complexes is modulated by metal ions such as calcium and zinc. Here, we provide insights into the extraction procedures and review the common structural features of ex vivo and in vitro S100A8/A9 amyloids, showing that they share the same generic origin.

Original languageEnglish
Title of host publicationAmyloid Proteins
Subtitle of host publicationMethods and Protocols
EditorsEinar M. Sigurdsson, Maria Gasset, Miguel Calero
Number of pages15
StatePublished - 1 Dec 2012

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Amyloid
  • Corpora amylacea
  • Fibrils
  • Oligomers
  • Prostate
  • S100A8
  • S100A9

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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