Multiple functions of S100A10, an important cancer promoter

Saiki, Yuriko; Horii, Akira

doi:10.1111/pin.12861

Cited by 38 publications

(36 citation statements)

References 62 publications

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“…An S100 homodimer is usually supplied with two symmetrical hydrophobic binding sites that recognise two identical target molecules [ 7 , 10 , 12 ]. S100A10 seems to be the only family member who is active in a calcium-independent manner, as it lacks a Ca 2+ -binding site and remains in an open conformation when calcium is absent [ 5 , 7 , 13 ]. Besides calcium, some S100 proteins, for example, S100A7, S100A12, and S100B are capable of binding other divalent metal ions such as zinc (Zn 2+ ), copper (Cu 2+ ), and manganese (Mn 2+ ), which is thought to play a role in the formation of oligomers [ 4 , 14 ].…”

Section: The S100 Familymentioning

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: The S100 Familymentioning

confidence: 99%

Friend or Foe: S100 Proteins in Cancer

Allgöwer

Kretz

Karstedt

et al. 2020

Cancers

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“…19 The expression level of S100A10 increased by the oncoproteins promyelocytic leukemia/retinoic acid receptor alpha (PML/RARα) and RAS, and its higher expression is linked to worse outcome in a number of cancer types including breast cancers. 20 In this study, we analyzed metastasized CD44 + breast cancer cells in breast cancer patient-derived tumor xenograft (PDX) mice to identify the intrinsic factors that were associated with cancer cell metastasis. S100 protein family genes were upregulated in the CD44 + PDX cancer cells metastasized to the liver.…”

Section: Introductionmentioning

confidence: 99%

Upregulation of S100A10 in metastasized breast cancer stem cells

et al. 2020

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Metastatic progression remains the major cause of death in human breast cancer. Cancer cells with cancer stem cell (CSC) properties drive initiation and growth of metastases at distant sites. We have previously established the breast cancer patient‐derived tumor xenograft (PDX) mouse model in which CSC marker CD44+ cancer cells formed spontaneous microscopic metastases in the liver. In this PDX mouse, the expression levels of S100A10 and its family proteins were much higher in the CD44+ cancer cells metastasized to the liver than those at the primary site. Knockdown of S100A10 in breast cancer cells suppressed and overexpression of S100A10 in breast cancer PDX cells enhanced their invasion abilities and 3D organoid formation capacities in vitro. Mechanistically, S100A10 regulated the matrix metalloproteinase activity and the expression levels of stem cell–related genes. Finally, constitutive knockdown of S100A10 significantly reduced their metastatic ability to the liver in vivo. These findings suggest that S100A10 functions as a metastasis promoter of breast CSCs by conferring both invasion ability and CSC properties in breast cancers.

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“…S100A10 could be an excellent target for cancer treatment. Diverse therapeutic strategies that have been used to target S100A10 include neutralizing antibodies, small molecule inhibitors, peptides, and all−trans retinoic acid (ATRA) (Bresnick, 2018;Saiki and Horii, 2019). S100A10 antibody plays an important role in reducing homing of leukemia cells to the bone marrow in vivo (Gopalakrishnapillai et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

S100A10 Accelerates Aerobic Glycolysis and Malignant Growth by Activating mTOR-Signaling Pathway in Gastric Cancer

et al. 2020

Front. Cell Dev. Biol.

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S100 calcium-binding protein A10 (S100A10) is crucially involved in the tumorigenesis of multiple malignant tumors. Reprogrammed glucose metabolism is emerging as a hallmark of various human cancers. However, the function of S100A10 in aerobic glycolysis is unclear. The expression of S100A10 was analyzed using the Oncomine database, Gene Expression Profiling Interactive Analysis (GEPIA), The Cancer Genome Atlas (TCGA), and the UALCAN cancer database. Prognostic analysis was performed using the Kaplan–Meier Plotter. The correlation between S100A10 and key glycolytic factors was assessed by GEPIA. The glycolysis level was examined by determining glucose consumption, lactate production, adenosine triphosphate production, cellular oxygen consumption rate, and extracellular acidification rate. Cell apoptosis was investigated by flow cytometry. Colony formation and BrdU assays were performed to detect cell proliferation. A subcutaneous xenograft mouse model was established to evaluate the effects of S100A10 in vivo. Gene Set Enrichment Analysis and western blotting were performed to explore the downstream signaling pathway. S100A10 was significantly upregulated in gastric cancer. Its expression was associated with poor survival. S100A10 increased glucose consumption, lactate production, and the switch from oxidative phosphorylation to aerobic glycolysis. S100A10 promoted malignant proliferation and suppressed cell apoptosis in gastric cancer. S100A10 activated the mTOR pathway by interacting with annexin A2 (ANXA2) to accelerate tumor glycolysis, resulting in tumor malignant progression. S100A10 contributed to aerobic glycolysis and accelerated malignant growth by modulating the Src/ANXA2/AKT/mTOR signaling pathway. Thus, S100A10 may have pivotal roles in gastric cancer.

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Multiple functions of S100A10, an important cancer promoter

Cited by 38 publications

References 62 publications

Friend or Foe: S100 Proteins in Cancer

Friend or Foe: S100 Proteins in Cancer

Upregulation of S100A10 in metastasized breast cancer stem cells

S100A10 Accelerates Aerobic Glycolysis and Malignant Growth by Activating mTOR-Signaling Pathway in Gastric Cancer

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