Journal ArticleDOI
Intracellular and extracellular roles of S100 proteins.
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TLDR
Structural and extracellular data indicate that members of the S100 protein family are multifunctional proteins implicated in the regulation of a variety of cellular activities.Abstract:
S100, a multigenic family of non-ubiquitous Ca(2+)-modulated proteins of the EF-hand type expressed in vertebrates exclusively, has been implicated in intracellular and extracellular regulatory activities. Members of this protein family have been shown to interact with several effector proteins within cells thereby regulating enzyme activities, the dynamics of cytoskeleton constituents, cell growth and differentiation, and Ca(2+) homeostasis. Structural information indicates that most of S100 proteins exist in the form of antiparallelly packed homodimers (in some cases heterodimers), capable of functionally crossbridging two homologous or heterologous target proteins in a Ca(2+)-dependent (and, in some instances, Ca(2+)-independent) manner. In addition, extracellular roles have been described for several S100 members, although secretion (via an unknown mechanism) has been documented for a few of them. Extracellular S100 proteins have been shown to exert regulatory effects on inflammatory cells, neurons, astrocytes, microglia, and endothelial and epithelial cells, and a cell surface receptor, RAGE, has been identified as a potential S100A12 and S100B receptor transducing the effects of these two proteins on inflammatory cells and neurons. Other cell surface molecules with ability to interact with S100 members have been identified, suggesting that RAGE might not be a universal S100 protein receptor and/or that a single S100 protein might interact with more than one receptor. Collectively, these data indicate that members of the S100 protein family are multifunctional proteins implicated in the regulation of a variety of cellular activities.read more
Citations
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Satellite glial cells in sensory ganglia: from form to function
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References
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Journal ArticleDOI
RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides.
Marion A. Hofmann,Steven Drury,Caifeng Fu,Wu Qu,Akihiko Taguchi,Yan Lu,Cecilia Avila,Neeraja Kambham,Angelika Bierhaus,Peter P. Nawroth,Markus F. Neurath,Timothy Slattery,Dale L. Beach,John McClary,Mariko Nagashima,John Morser,David M. Stern,Ann Marie Schmidt +17 more
TL;DR: It is reported here that receptor for AGE (RAGE) is a central cell surface receptor for EN-RAGE (extracellular newly identified RAGE-binding protein) and related members of the S100/calgranulin superfamily.
Journal ArticleDOI
Annexins: from structure to function.
Volker Gerke,Stephen E. Moss +1 more
TL;DR: Although annexins lack signal sequences for secretion, some members of the family have also been identified extracellularly where they can act as receptors for serum proteases on the endothelium as well as inhibitors of neutrophil migration and blood coagulation.
Journal ArticleDOI
S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles.
TL;DR: The variety of intracellular target proteins of S100 proteins and, in some cases, of a single S100 protein, and the cell specificity of expression of certain S100 members suggest that these proteins might have a role in the fine regulation of effector proteins and/or specific steps of signaling pathways/cellular functions.
Journal ArticleDOI
The S100 family of EF-hand calcium-binding proteins: functions and pathology.
TL;DR: Some functional aspects of EF-hand proteins are described, which have been found recently in different cellular compartments, which share a common Ca(2+)-binding motif.
Journal ArticleDOI
The S100 protein family: History, function, and expression
TL;DR: Analysis of the function and expression of these proteins in both nervous and nonnervous tissues will provide important information regarding the role of altered S100 expression in nervous system development, function and disease.