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Review
. 2014 May;71(9):1551-79.
doi: 10.1007/s00018-013-1400-7. Epub 2013 Jun 30.

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

Stephane R Gross  1 , Connie Goh Then Sin, Roger Barraclough, Philip S Rudland
Affiliations
Review

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

Stephane R Gross et al. Cell Mol Life Sci. 2014 May.

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.

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Figures

Fig. 1
Fig. 1
S100 protein amino acid sequence alignment. Amino acid sequences of S100 proteins were aligned with the EF-hands and central regions indicated (number 1–12 in the canonical EF-hand motif refers to the position of essential amino acids for the formation of the calcium-binding loop). All sequences are human, and the accession numbers are S100A1, AAH14392.1; S100A2, EAW53305.1; S100A3, EAW53306.1; S100A4, CAG29341.1; S100A5, EAW53317.1; S100A6, EAW53326.1; S100A7, EAW53327.1; S100A8, EAW53330.1; S100A9, EAW53334.1; S100A10, NP002957.1; S100A11, NP005611.1; S100A12, EAW53332.1; S100A13, CAA68188.1; S100A14, AAM19206.1; S100A15, AAO40033.1; S100A16, EAW53304.1; S100B, NP006263.1; S100G, EAW98916.1; S100P, EAW82384.1 and S100Z, EAW95784.1. Sequences were aligned using the multalin sequence comparison program (http://multalin.toulouse.inra.fr/multalin/) and the resulting data shaded and presented using the boxshade integrated programme (http://www.ch.embnet.org/software/BOX_form.html)
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