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


Autoria(s): Gross, Stephane R.; Sin, Connie G.T.; Barraclough, Roger; Rudland, Philip S.
Data(s)

01/05/2014

Resumo

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.

Formato

application/pdf

Identificador

http://eprints.aston.ac.uk/20924/1/Joining_S100_proteins_and_migration.pdf

Gross, Stephane R.; Sin, Connie G.T.; Barraclough, Roger and Rudland, Philip S. (2014). Joining S100 proteins and migration:for better or for worse, in sickness and in health. Cellular and Molecular Life Sciences, 71 (9), pp. 1551-1579.

Relação

http://eprints.aston.ac.uk/20924/

Tipo

Article

PeerReviewed