S100A12 in Digestive Diseases and Health: A Scoping Review

Carvalho, Alexandre; Lu, Jacky; Francis, Jamisha D.; Moore, Rebecca E.; Haley, Kathryn P.; Doster, Ryan S.; Townsend, Steven D.; Johnson, Jeff S.; Damo, Steven M.; Gaddy, Jennifer A.

doi:10.1155/2020/2868373

Cited by 35 publications

(34 citation statements)

References 85 publications

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“…The majority of extracellular S100 proteins interact with the receptor for advanced glycation end products (RAGE) and Toll-like receptor 4 (TLR4). The binding of S100A9, S100A8/S100A9, and S100A12 to these receptors stimulates nuclear factor "kappa-light-chain-enhancer" of activated B-cells (NF-kB) signalling, which results in the upregulated expression of cytokines and pro-inflammatory factors, such as interleukin-1β (IL-1β) or tumour necrosis factor α (TNFα) [29,40,41]. Further, it was shown that S100A7, S100A8, S100A9, and S100A15 have chemotactic features, attracting neutrophils and lymphocytes [23,28,40,42,43].…”

Section: Expression and Regulationmentioning

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: Expression and Regulationmentioning

confidence: 99%

Friend or Foe: S100 Proteins in Cancer

Allgöwer

Kretz

Karstedt

et al. 2020

Cancers

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“…S100A12 gene is usually highly expressed in neutrophils at acute phase of inflammation 29 . The serum soluble form of S100A12 protein is also elevated in many inflammation-related diseases 30 , 31 .…”

Section: Resultsmentioning

confidence: 99%

Serum proteins may facilitate the identification of Kawasaki disease and promote in vitro neutrophil infiltration

Huang

Weng

et al. 2020

Sci Rep

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Kawasaki disease (KD) usually affects the children younger than 5 years of age and subsequently causes coronary artery lesions (CALs) without timely identification and treatment. Developing a robust and fast prediction method may facilitate the timely diagnosis of KD, significantly reducing the risk of CALs in KD patients. The levels of inflammatory serum proteins dramatically vary during the onsets of many immune diseases, including in KD. However, our understanding of their pathogenic roles in KD is behind satisfaction. The purpose of this study was to evaluate candidate diagnostic serum proteins and the potential mechanism in KD using iTRAQ gel-free proteomics. We enrolled subjects and conducted iTRAQ gel-free proteomics to globally screen serum proteins followed by specific validation with ELISA. Further in vitro leukocyte trans-endothelial model was also applied to investigate the pathogenesis roles of inflammatory serum proteins. We identified six KD protein biomarkers, including Protein S100-A8 (S100A8), Protein S100-A9 (S100A9), Protein S100-A12 (S100A12), Peroxiredoxin-2 (PRDX2), Neutrophil defensin 1 (DEFA1) and Alpha-1-acid glycoprotein 1 (ORM1). They enabled us to develop a high-performance KD prediction model with an auROC value of 0.94, facilitating the timely identification of KD. Further assays concluded that recombinant S100A12 protein treatment activated neutrophil surface adhesion molecules responsible for adhesion to endothelial cells. Therefore, S100A12 promoted both freshly clinically isolated neutrophils and neutrophil-like cells to infiltrate through the endothelial layer in vitro. Finally, the antibody against S100A12 may attenuate the infiltration promoted by S100A12. Our result demonstrated that evaluating S100A8, S100A9, S100A12, PRDX2, DEFA1 and ORM1 levels may be a good diagnostic tool of KD. Further in vitro study implied that S100A12 could be a potential therapeutic target for KD.

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“…Since bacteria and hosts are aware of the significance of zinc, they have established a competitive relationship at the pathogen-host interface. Vertebrates employ multiple mechanisms to restrict zinc bioavailability to pathogens, which is generally termed “nutritional immunity” [ 9 , 23 , 24 ]. In particular, the host employs S100 family proteins, such as S100A7 protein psoriasis secreted by keratinocytes and S100A8/S100A9 dimer calprotectin secreted by neutrophil granulocytes to sequester zinc locally and extracellularly [ 4 , 25 ].…”

Section: Discussionmentioning

confidence: 99%

Zinc uptake system ZnuACB is essential for maintaining pathogenic phenotype of F4ac+ enterotoxigenic E. coli (ETEC) under a zinc restricted environment

Quan

Xia

Lian

et al. 2020

Vet Res

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Zinc is the second trace element of living organisms after iron. Given its crucial importance, mammalian hosts restrict the bioavailability of Zinc ions (Zn2+) to bacterial pathogens. As a countermeasure, pathogens utilize high affinity Zn2+ transporters, such as ZnuACB to compete with the host for zinc. It is essential for bacteria to maintain zinc homeostasis and thus maintain their physiology and pathogenesis. In an attempt to uncover the zinc transporter in F4+ enterotoxigenic E. coli (ETEC) C83902, we analyzed two RNA-seq data sets of bacteria samples when different zinc treatments (restriction or abundance) were applied. Considering data revealing that the high affinity zinc uptake system ZnuACB acts as the main transporter in ETEC C83902 to resist zinc deficiency, we deleted znuACB genes to study the role of them in ETEC C83902. The deletion of znuACB genes results in growth perturbation and a sharp decrease in the ability of biofilm formation and adhesion of bacteria in vitro. Taking the data together, this study demonstrates that the ZnuACB system is required for ETEC C83902 to acquire zinc, which highly contributes to ETEC pathogenicity as well.

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S100A12 in Digestive Diseases and Health: A Scoping Review

Cited by 35 publications

References 85 publications

Friend or Foe: S100 Proteins in Cancer

Friend or Foe: S100 Proteins in Cancer

Serum proteins may facilitate the identification of Kawasaki disease and promote in vitro neutrophil infiltration

Zinc uptake system ZnuACB is essential for maintaining pathogenic phenotype of F4ac+ enterotoxigenic E. coli (ETEC) under a zinc restricted environment

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