Review
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World J Biol Chem. Feb 26, 2013; 4(1): 1-12
Published online Feb 26, 2013. doi: 10.4331/wjbc.v4.i1.1
S100B protein in tissue development, repair and regeneration
Guglielmo Sorci, Francesca Riuzzi, Cataldo Arcuri, Claudia Tubaro, Roberta Bianchi, Ileana Giambanco, Rosario Donato
Guglielmo Sorci, Francesca Riuzzi, Cataldo Arcuri, Claudia Tubaro, Roberta Bianchi, Ileana Giambanco, Rosario Donato, Department of Experimental Medicine and Biochemical Sciences, University of Perugia, 06122 Perugia, Italy
Guglielmo Sorci, Francesca Riuzzi, Rosario Donato, Interuniversity Institute for Myology, University of Perugia, 06122 Perugia, Italy
Author contributions: All the authors contributed equally to this work.
Supported by Ministero dell’Università e della Ricerca, No. PRIN 2007LNKSYS, No. 2007AWZTHH_004 and No. 2009WBFZYM_002; Association Française contre les Myopathies, No. Project 12992; Associazione Italiana per la Ricerca sul Cancro, No. Project 6021; and Fondazione Cassa di Risparmio di Perugia, No. 2007.0218.020, No. 2009.020.0021 and No. 2012.0241.021
Correspondence to: Rosario Donato, MD, Professor, Department of Experimental Medicine and Biochemical Sciences, University of Perugia, 06122 Perugia, Italy. donato@unipg.it
Telephone: +39-75-5857453 Fax: +39-75-5857453
Received: December 5, 2012
Revised: January 26, 2013
Accepted: February 25, 2013
Published online: February 26, 2013
Processing time: 118 Days and 24 Hours
Abstract

The Ca2+-binding protein of the EF-hand type, S100B, exerts both intracellular and extracellular regulatory activities. As an intracellular regulator, S100B is involved in the regulation of energy metabolism, transcription, protein phosphorylation, cell proliferation, survival, differentiation and motility, and Ca2+ homeostasis, by interacting with a wide array of proteins (i.e., enzymes, enzyme substrates, cytoskeletal subunits, scaffold/adaptor proteins, transcription factors, ubiquitin E3 ligases, ion channels) in a restricted number of cell types. As an extracellular signal, S100B engages the pattern recognition receptor, receptor for advanced glycation end-products (RAGE), on immune cells as well as on neuronal, astrocytic and microglial cells, vascular smooth muscle cells, skeletal myoblasts and cardiomyocytes. However, RAGE may not be the sole receptor activated by S100B, the protein being able to enhance bFGF-FGFR1 signaling by interacting with FGFR1-bound bFGF in particular cell types. Moreover, extracellular effects of S100B vary depending on its local concentration. Increasing evidence suggests that at the concentration found in extracellular fluids in normal physiological conditions and locally upon acute tissue injury, which is up to a few nM levels, S100B exerts trophic effects in the central and peripheral nervous system and in skeletal muscle tissue thus participating in tissue homeostasis. The present commentary summarizes results implicating intracellular and extracellular S100B in tissue development, repair and regeneration.

Keywords: S100B; Cell proliferation; Cell differentiation; Cell survival; Cell motility; Development; Tissue homeostasis; Tissue repair; Tissue regeneration