Functions of S100 proteins.

  title={Functions of S100 proteins.},
  author={Rosario Donato and Brian R. Cannon and Guglielmo Sorci and Francesca Riuzzi and Kenneth J. Hsu and Dylan J Weber and Carolyn L. Geczy},
  journal={Current molecular medicine},
  volume={13 1},
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… 

The Calcium Binding Protein S100A11 and Its Roles in Diseases

This review focuses on the tissue and organ expression of S100A11, a member of the S100 family, which may mediate signal transduction in response to internal or external stimuli and play various roles in different diseases such as cancers, metabolic disease, neurological diseases, and vascular calcification.

S100 Proteins As an Important Regulator of Macrophage Inflammation

The multi-functional roles of S100 proteins are discussed, especially their potential roles associated with cell migration, differentiation, tissue repair, and inflammation.

[Ligands of RAGE-Proteins: Role in Intercellular Communication and Pathogenesis of Inflammation].

The review contains data on the diversity of endogenous ligands of RAGE receptors (receptor for advanced glycation end products) that play an important role in the signal transduction in (patho) physiological conditions and special attention is paid to the role of RAGES in pathogenesis of inflammation, particularly, in brain injury and neurodegeneration.

Multifunctional Role of S100 Protein Family in the Immune System: An Update

The present review compiled the vast majority of recent studies that focused on the multifunctionality of S 100 proteins in the complex immune system and its associated activities and shed light on the numerous molecular approaches and signaling cascades regulated by S100 proteins during immune response.

S100B protein in tissue development, repair and regeneration.

Results implicating intracellular and extracellular S100B in tissue development, repair and regeneration are summarized.

S100 proteins in cancer

Emerging in vivo evidence indicates that the biology of most S100 proteins is complex and multifactorial, and that these proteins actively contribute to tumorigenic processes such as cell proliferation, metastasis, angiogenesis and immune evasion.

S100 proteins and the skin: a review

This review is an attempt to comprehensively summarize the function and expression of S100 proteins selectively expressed in normal skin and/or involved in diseased skin.

S100 proteins as therapeutic targets

This review focuses on the development of S100 neutralizing antibodies and small molecule inhibitors and their potential therapeutic use in controlling disease progression and severity.

S100 proteins as therapeutic targets

This review focuses on the development of S100 neutralizing antibodies and small molecule inhibitors and their potential therapeutic use in controlling disease progression and severity.



S100B's double life: intracellular regulator and extracellular signal.

RAGE: a single receptor for several ligands and different cellular responses: the case of certain S100 proteins.

  • R. Donato
  • Biology
    Current molecular medicine
  • 2007
Oligomerization of S100 proteins under the non-reducing, high-Ca2+ conditions found extracellularly appears to play a relevant role in RAGE activation, and binding of at least S100A12 and S100B results in RAGES oligomerization.

S100B Protein, A Damage-Associated Molecular Pattern Protein in the Brain and Heart, and Beyond

S100B belongs to a multigenic family of Ca2+-binding proteins of the EF-hand type and is expressed in high abundance in the brain and exerts effects outside the brain; as an intracellular regulator, S100B inhibits the postinfarction hypertrophic response in cardiomyocytes, while as an extracellular signal, (high) S 100B causesCardiomyocyte death, activates endothelial cells, and stimulates vascular smooth muscle cell proliferation.

Natural and amyloid self‐assembly of S100 proteins: structural basis of functional diversity

The unique chemical and structural properties of S100 proteins that underlie the conformational changes resulting in their oligomerization upon metal ion binding and ultimately in functional control are reviewed.

Oxidative modifications of S100 proteins: functional regulation by redox

The mounting evidence from functional and gene regulation studies that these proteins may also play protective roles is summarized, based on emerging data that post–translational, oxidative modifications may act as a regulatory switch.

Calcium-dependent and -independent interactions of the S100 protein family.

This review highlights both the calcium-dependent and -independent interactions of the S100 proteins, with a focus on the structures of the complexes, differences and similarities in the strengths of the interactions, and preferences for homo- compared with hetero-dimeric S100 protein assembly.

S100A10/p11: family, friends and functions

  • U. RescherV. Gerke
  • Biology, Chemistry
    Pflügers Archiv - European Journal of Physiology
  • 2007
It is proposed that S100A10 functions as a linker tethering certain transmembrane proteins to annexin A2 thereby assisting their traffic to the plasma membrane and/or their firm anchorage at certain membrane sites.

The Calcium-Dependent Interaction of S100B with Its Protein Targets

The structural basis and physiological significance of increased Ca2+-binding affinity in the presence of protein targets is reviewed and new information regarding redundancy among family members and the structural domains that mediate the interaction of S100B, and other S100s, with their targets is presented.

S100B and S100A6 Differentially Modulate Cell Survival by Interacting with Distinct RAGE (Receptor for Advanced Glycation End Products) Immunoglobulin Domains*

Comparison of the interaction of two S100 proteins, S100B and S100A6, with RAGE by in vitro assay and in culture of human SH-SY5Y neuroblastoma cells suggests that the receptor for advanced glycation end products (RAGE) plays important roles in mediating S100 protein-induced cellular signaling.