Perinatal S100B Protein Assessment in Human Unconventional Biological Fluids: A Minireview and New Perspectives

Gazzolo, Diego; Michetti, Fabrizio

doi:10.1155/2010/703563

Cited by 23 publications

(11 citation statements)

References 53 publications

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“…Some, such as the S100A8/S100A9 complex and S100B are considered biomarkers for particular disease processes [74,105,141-147] (also see below). Secretion of some S100 proteins is stimulated by particular cell activators.…”

Section: Secretion and Release Of S100 Proteinsmentioning

confidence: 99%

Functions of S100 Proteins

Donato¹,

Cannon²,

Sorci³

et al. 2013

Current Molecular Medicine

1,095

709

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The S100 protein family consists of 24 members functionally distributed into three main subgroups: those that only exert intracellular regulatory effects, those with intracellular and extracellular functions and those which mainly exert extracellular regulatory effects. S100 proteins are only expressed in vertebrates and show cell-specific expression patterns. In some instances, a particular S100 protein can be induced in pathological circumstances in a cell type that does not express it in normal physiological conditions. Within cells, S100 proteins are involved in aspects of regulation of proliferation, differentiation, apoptosis, Ca2+ homeostasis, energy metabolism, inflammation and migration/invasion through interactions with a variety of target proteins including enzymes, cytoskeletal subunits, receptors, transcription factors and nucleic acids. Some S100 proteins are secreted or released and regulate cell functions in an autocrine and paracrine manner via activation of surface receptors (e.g. the receptor for advanced glycation end-products and toll-like receptor 4), G-protein-coupled receptors, scavenger receptors, or heparan sulfate proteoglycans and N-glycans. Extracellular S100A4 and S100B also interact with epidermal growth factor and basic fibroblast growth factor, respectively, thereby enhancing the activity of the corresponding receptors. Thus, extracellular S100 proteins exert regulatory activities on monocytes/macrophages/microglia, neutrophils, lymphocytes, mast cells, articular chondrocytes, endothelial and vascular smooth muscle cells, neurons, astrocytes, Schwann cells, epithelial cells, myoblasts and cardiomyocytes, thereby participating in innate and adaptive immune responses, cell migration and chemotaxis, tissue development and repair, and leukocyte and tumor cell invasion.

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Section: Secretion and Release Of S100 Proteinsmentioning

confidence: 99%

Functions of S100 Proteins

Donato¹,

Cannon²,

Sorci³

et al. 2013

Current Molecular Medicine

1,095

709

View full text Add to dashboard Cite

show abstract

“…237, 238, 239, 240 S100A8/A9, S100A12 and S100B are even considered biomarkers of specific diseases, such as cancer, atherosclerosis and stroke. 231, 241, 242, 243, 244, 245 …”

Section: S100mentioning

confidence: 99%

HMGB1, IL-1α, IL-33 and S100 proteins: dual-function alarmins

2016

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Our immune system is based on the close collaboration of the innate and adaptive immune systems for the rapid detection of any threats to the host. Recognition of pathogen-derived molecules is entrusted to specific germline-encoded signaling receptors. The same receptors have now also emerged as efficient detectors of misplaced or altered self-molecules that signal tissue damage and cell death following, for example, disruption of the blood supply and subsequent hypoxia. Many types of endogenous molecules have been shown to provoke such sterile inflammatory states when released from dying cells. However, a group of proteins referred to as alarmins have both intracellular and extracellular functions which have been the subject of intense research. Indeed, alarmins can either exert beneficial cell housekeeping functions, leading to tissue repair, or provoke deleterious uncontrolled inflammation. This group of proteins includes the high-mobility group box 1 protein (HMGB1), interleukin (IL)-1α, IL-33 and the Ca2+-binding S100 proteins. These dual-function proteins share conserved regulatory mechanisms, such as secretory routes, post-translational modifications and enzymatic processing, that govern their extracellular functions in time and space. Release of alarmins from mesenchymal cells is a highly relevant mechanism by which immune cells can be alerted of tissue damage, and alarmins play a key role in the development of acute or chronic inflammatory diseases and in cancer development.

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“…9 Therefore, S100B is regarded as a biomarker of activation of pathologic mechanisms after brain injury and neuroinflammatory/ neurodegenerative disorders. 11,12 The elevated levels of S100B in neurodegenerative models have been found to be associated with impairments in learning and memory function. 13,14 In addition, recently an association between elevated circulating S100B levels and impaired neurologic outcomes has been observed after clinical brain injury.…”

Section: Introductionmentioning

confidence: 99%

S100B Inhibition Reduces Behavioral and Pathologic Changes in Experimental Traumatic Brain Injury

Kabadi

Stoica

Zimmer

et al. 2015

J Cereb Blood Flow Metab

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Neuroinflammation following traumatic brain injury (TBI) is increasingly recognized to contribute to chronic tissue loss and neurologic dysfunction. Circulating levels of S100B increase after TBI and have been used as a biomarker. S100B is produced by activated astrocytes and can promote microglial activation; signaling by S100B through interaction with the multiligand advanced glycation end product-specific receptor (AGER) has been implicated in brain injury and microglial activation during chronic neurodegeneration. We examined the effects of S100B inhibition in a controlled cortical impact model, using S100B knockout mice or administration of neutralizing S100B antibody. Both interventions significantly reduced TBI-induced lesion volume, improved retention memory function, and attenuated microglial activation. The neutralizing antibody also significantly reduced sensorimotor deficits and improved neuronal survival in the cortex. However, S100B did not alter microglial activation in BV2 cells or primary microglial cultures stimulated by lipopolysaccharide or interferon gamma. Further, proximity ligation assays did not support direct interaction in the brain between S100B and AGER following TBI. Future studies are needed to elucidate specific pathways underlying S100B-mediated neuroinflammatory actions after TBI. Our results strongly implicate S100B in TBI-induced neuroinflammation, cell loss, and neurologic dysfunction, thereby indicating that it is a potential therapeutic target for TBI.

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Perinatal S100B Protein Assessment in Human Unconventional Biological Fluids: A Minireview and New Perspectives

Cited by 23 publications

References 53 publications

Functions of S100 Proteins

Functions of S100 Proteins

HMGB1, IL-1α, IL-33 and S100 proteins: dual-function alarmins

S100B Inhibition Reduces Behavioral and Pathologic Changes in Experimental Traumatic Brain Injury

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