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Author(s): Donato R (Donato, Rosario); Sorci G (Sorci, Guglielmo); Riuzzi F (Riuzzi, Francesca); Arcuri C (Arcuri, Cataldo); Bianchi R (Bianchi, Roberta); Brozzi F (Brozzi, Flora); Tubaro C (Tubaro, Claudia); Giambanco I (Giambanco, Ileana)
Title: S100B's double life: Intracellular regulator and extracellular signal
Source: BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 1793 (6): 1008-1022
Date: 2009 JUN
Document Type: Journal : Proceedings Paper
DOI: 10.1016/j.bbamcr.2008.11.009
Language: English
Comment:  
Address: Univ Perugia, Dept Expt Med & Biochem Sci, Sect Anat, I-06122 Perugia, Italy.
Reprint: Donato, R, Univ Perugia, Dept Expt Med & Biochem Sci, Sect Anat, Via
Giochetto,CP 81,Succ 3, I-06122 Perugia, Italy.
E-mail: donato@unipg.it
Author Keywords: S100B; Proliferation; Differentiation; Development; Inflammation; RAGE; Signaling
KeyWords Plus: GLYCATION END-PRODUCTS; CALCIUM-BINDING PROTEINS; CENTRAL-NERVOUS- SYSTEM; NF-KAPPA-B; INCREASES GLUTAMATE UPTAKE; SEROTONERGIC GROWTH- FACTOR; RAGE-INDEPENDENT MANNER; DELAYED NEURONAL INJURY; NITRIC-OXIDE SYNTHASE; SMOOTH-MUSCLE-CELLS
Abstract: The Ca2+-binding protein of the EF-hand type, S100B, exerts both intracellular and extracellular functions. Recent studies have provided more detailed information concerning the mechanism(s) of action of S100B as an intracellular regulator and an extracellular signal. Indeed, intracellular S100B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S100B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes (i.e. beneficial or detrimental, pro-proliferative or pro-differentiative) depending on the concentration attained by the protein, the cell type and the microenvironment. Yet, RAGE might not be the sole S100B receptor, and S100B's ability to engage RAGE might be regulated by its interaction with other extracellular factors. Future studies using S100B transgenic and S100B null mice might shed more light on the functional role(s) of the protein. (C) 2008 Elsevier B.V. All rights reserved.
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