Role of S100 proteins in health and disease

González, Laura López; Garrie, Karin; Turner, Martha

doi:10.1016/j.bbamcr.2020.118677

Cited by 220 publications

(214 citation statements)

References 179 publications

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“…While some inhibitors seem to be effective by inhibiting the transcription of S100 genes, others inhibit S100 protein activity by disturbing the interaction between S100 proteins and their targets. In addition, targeting covalent modifications, such as S-nitrosylation, S-glutathionylation, and phosphorylation, could be a promising strategy, as these modifications influence the function of S100 proteins [213]. In this review, S100 inhibitors are classified into small molecule inhibitors, neutralising antibodies, and microRNA (miRNA) mimics, and a summary is given in Table 1.…”

Section: Targeting S100 Proteins For Cancer Therapymentioning

confidence: 99%

Friend or Foe: S100 Proteins in Cancer

Allgöwer

Kretz

Karstedt

et al. 2020

Cancers

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S100 proteins are widely expressed small molecular EF-hand calcium-binding proteins of vertebrates, which are involved in numerous cellular processes, such as Ca2+ homeostasis, proliferation, apoptosis, differentiation, and inflammation. Although the complex network of S100 signalling is by far not fully deciphered, several S100 family members could be linked to a variety of diseases, such as inflammatory disorders, neurological diseases, and also cancer. The research of the past decades revealed that S100 proteins play a crucial role in the development and progression of many cancer types, such as breast cancer, lung cancer, and melanoma. Hence, S100 family members have also been shown to be promising diagnostic markers and possible novel targets for therapy. However, the current knowledge of S100 proteins is limited and more attention to this unique group of proteins is needed. Therefore, this review article summarises S100 proteins and their relation in different cancer types, while also providing an overview of novel therapeutic strategies for targeting S100 proteins for cancer treatment.

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Section: Targeting S100 Proteins For Cancer Therapymentioning

confidence: 99%

Friend or Foe: S100 Proteins in Cancer

Allgöwer

Kretz

Karstedt

et al. 2020

Cancers

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“…S100A6 is a Ca 2+ -binding protein belonging to the S100 family [1,2]. Members of this family are present in different cell and tissue types including the brain.…”

Section: Discussionmentioning

confidence: 99%

“…S100A6 is a low-molecular-weight Ca 2+ -binding protein of the S100 family [1,2]. It functions as a homodimer mainly formed by non-covalent interactions ( Figure 1) and binds two Ca 2+ per monomer, each through an EF-hand structure consisting of two α helices linked by a short loop region.…”

Section: Introductionmentioning

confidence: 99%

S100A6 and Its Brain Ligands in Neurodegenerative Disorders

Filipek

2020

IJMS

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The S100A6 protein is present in different mammalian cells and tissues including the brain. It binds Ca2+ and Zn2+ and interacts with many target proteins/ligands. The best characterized ligands of S100A6, expressed at high level in the brain, include CacyBP/SIP and Sgt1. Research concerning the functional role of S100A6 and these two ligands indicates that they are involved in various signaling pathways that regulate cell proliferation, differentiation, cytoskeletal organization, and others. In this review, we focused on the expression/localization of these proteins in the brain and on their possible role in neurodegenerative diseases. Published results demonstrate that S100A6, CacyBP/SIP, and Sgt1 are expressed in various brain structures and in the spinal cord and can be found in different cell types including neurons and astrocytes. When it comes to their possible involvement in nervous system pathology, it is evident that their expression/level and/or subcellular localization is changed when compared to normal conditions. Among diseases in which such changes have been observed are Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS), epileptogenesis, Parkinson’s disease (PD), Huntington’s disease (HD), and others.

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“…The S100 proteins were named because of their ability to dissolve in 100% neutral saturated ammonium sulfate solution and belong to a unique class of non-ubiquitous small molecular weight (10-12 kDa) (Bresnick et al, 2015), Ca 2+ -modulated proteins, which were first identified in nervous system by Moore (1965). The S100 family currently has 25 known different members (including S100A1-16, S100G, S100P, and S100B), which are highly similar in sequence and structure (Gonzalez et al, 2020), and they all contain calcium-binding protein motifs (Bresnick et al, 2015). Schafer and Heizmann (1996) reported that S100 proteins consist of two distinct helix-loop-helix elongation factor (EF) hands flanked by conserved hydrophobic regions at the C-and N-terminal and connected by a central hinge region.…”

Section: S100a8 and S100a9 Proteins: Important Members Of The S100 Prmentioning

confidence: 99%

“…There is growing experimental and clinical evidence that the S100 protein family has been implicated in the occurrence and development of multiple cardiovascular diseases, and these proteins are expected to become new targets for prevention (Gonzalez et al, 2020). For example, serum S100A levels increase after acute ischemic events, are highly sensitive in myocardial injury, and may be a candidate biomarker for the diagnosis of AMI (Aydin et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

S100A8/A9 in Myocardial Infarction: A Promising Biomarker and Therapeutic Target

Cai

Xie

et al. 2020

Front. Cell Dev. Biol.

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Myocardial infarction (MI), the main cause of cardiovascular-related deaths worldwide, has long been a hot topic because of its threat to public health. S100A8/A9 has recently attracted an increasing amount of interest as a crucial alarmin that regulates the pathogenesis of cardiovascular disease after its release from myeloid cells. However, the role of S100A8/A9 in the etiology of MI is not well understood. Here, we elaborate on the critical roles and potential mechanisms of S100A8/A9 driving the pathogenesis of MI. First, cellular source of S100A8/A9 in infarcted heart is discussed. Then we highlight the effect of S100A8/A9 heterodimer in the early inflammatory period and the late reparative period of MI as well as myocardial ischemia/reperfusion (I/R) injury. Moreover, the predictive value of S100A8/A9 for the risk of recurrence of cardiovascular events is elucidated. Therefore, this review focuses on the molecular mechanisms of S100A8/A9 in MI pathogenesis to provide a promising biomarker and therapeutic target for MI.

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Role of S100 proteins in health and disease

Cited by 220 publications

References 179 publications

Friend or Foe: S100 Proteins in Cancer

Friend or Foe: S100 Proteins in Cancer

S100A6 and Its Brain Ligands in Neurodegenerative Disorders

S100A8/A9 in Myocardial Infarction: A Promising Biomarker and Therapeutic Target

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