Book ChapterDOI
Pathologies involving the S100 proteins and RAGE.
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TLDR
The most recent developments focussing on the biological functions of the S100 proteins are reviewed and the presently available S100-specific mouse models and their possible use as human disease models are discussed.Abstract:
The S100 proteins are exclusively expressed in vertebrates and are the largest subgroup within the superfamily of EF-hand Ca 2+ -binding proteinsread more
Citations
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Mechanisms of Diabetic Complications
TL;DR: The well validated, as well as putative mechanisms involved in the development of diabetic complications are discussed and new fields of research, which warrant further investigation as potential therapeutic targets of the future, will be highlighted.
Journal ArticleDOI
S100B's double life: Intracellular regulator and extracellular signal
Rosario Donato,Guglielmo Sorci,Francesca Riuzzi,Cataldo Arcuri,Roberta Bianchi,Flora Brozzi,Claudia Tubaro,Ileana Giambanco +7 more
TL;DR: The Ca2+-binding protein of the EF-hand type, S100B, exerts both intracellular and extracellular functions, 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.
Journal ArticleDOI
RAGE (Receptor for Advanced Glycation Endproducts), RAGE Ligands, and their role in Cancer and Inflammation
Louis J. Sparvero,Denise Asafu-Adjei,Rui Kang,Daolin Tang,Neilay Amin,Jaehyun Im,Ronnye Rutledge,Brenda Lin,Andrew A. Amoscato,Herbert J. Zeh,Michael T. Lotze +10 more
TL;DR: The Receptor for Advanced Glycation Endproducts [RAGE] is an evolutionarily recent member of the immunoglobulin super-family, encoded in the Class III region of the major histocompatability complex, and sits in a pivotal role, regulating metabolism, inflammation, and epithelial survival in the setting of stress.
Journal ArticleDOI
Binding of S100 proteins to RAGE: An update
TL;DR: Interestingly, many RAGE ligands appear to interact with distinct domains of the extracellular portion of RAGE and to trigger various cellular effects.
Journal ArticleDOI
Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease.
Velandai Srikanth,Annette Maczurek,Thanh G. Phan,Megan L. Steele,Bernadette Westcott,Damian Juskiw,Gerald Münch +6 more
TL;DR: In this paper, the authors revisited the hypothesis that advanced glycation endproducts (AGEs) and their receptor RAGE may play an important role in disease pathogenesis by influencing transport of β-amyloid into the brain or by manipulating inflammatory mechanisms.
References
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Journal ArticleDOI
p53 mutations in human cancers
TL;DR: The p53 mutational spectrum differs among cancers of the colon, lung, esophagus, breast, liver, brain, reticuloendothelial tissues, and hemopoietic tissues as mentioned in this paper.
Journal ArticleDOI
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
TL;DR: It is reported that Hmgb1-/- necrotic cells have a greatly reduced ability to promote inflammation, which proves that the release of HMGB1 can signal the demise of a cell to its neighbours, and cells undergoing apoptosis are programmed to withhold the signal that is broadcast by cells that have been damaged or killed by trauma.
Journal ArticleDOI
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Shi Du Yan,Xi Chen,Jin Fu,Ming Chen,Huaijie Zhu,Alex E. Roher,Timothy Slattery,Lei Zhao,Mariko Nagashima,John Morser,Antonio Migheli,Peter P. Nawroth,David I. Stern,Ann Marie Schmidt +13 more
TL;DR: Evidence is presented that the 'receptor for advanced glycation end products' (RAGE) is such a receptor, and that it mediates effects of the peptide on neurons and microglia and indicates that it is relevant to the pathogenesis of neuronal dysfunction and death.
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
Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease
W. S.T. Griffin,L. C. Stanley,C. Ling,L. White,V. MacLeod,L. J. Perrot,Charles L. White,C. Araoz +7 more
TL;DR: The data suggest that increased expression of S-100 in Down syndrome, resulting from duplication of the gene on chromosome 21 that encodes the beta subunit ofS-100, may be augmented by elevation of interleukin 1, which may promote the astrogliosis in Alzheimer disease.