Joining S100 proteins and migration: for better or for worse, in sickness and in health

Stephane R. Gross*, Connie G.T. Sin, Roger Barraclough, Philip S. Rudland

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract

The vast diversity of S100 proteins has demonstrated a multitude of biological correlations with cell growth, cell differentiation and cell survival in numerous physiological and pathological conditions in all cells of the body. This review summarises some of the reported regulatory functions of S100 proteins (namely S100A1, S100A2, S100A4, S100A6, S100A7, S100A8/S100A9, S100A10, S100A11, S100A12, S100B and S100P) on cellular migration and invasion, established in both culture and animal model systems and the possible mechanisms that have been proposed to be responsible. These mechanisms involve intracellular events and components of the cytoskeletal organisation (actin/myosin filaments, intermediate filaments and microtubules) as well as extracellular signalling at different cell surface receptors (RAGE and integrins). Finally, we shall attempt to demonstrate how aberrant expression of the S100 proteins may lead to pathological events and human disorders and furthermore provide a rationale to possibly explain why the expression of some of the S100 proteins (mainly S100A4 and S100P) has led to conflicting results on motility, depending on the cells used. © 2013 Springer Basel.

Original languageEnglish
Pages (from-to)1551-1579
Number of pages29
JournalCellular and Molecular Life Sciences
Volume71
Issue number9
Early online date30 Jun 2013
DOIs
Publication statusPublished - May 2014

Bibliographical note

The final publication is available at link.springer.com

Keywords

  • cancer
  • cytoskeleton
  • invasion
  • migration/motility
  • receptor
  • S100 proteins

Fingerprint Dive into the research topics of 'Joining S100 proteins and migration: for better or for worse, in sickness and in health'. Together they form a unique fingerprint.

Cite this