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aberrant S100A16 expression might be modulated by its DNA hypomethylation and serves as an independent prognostic indicator of unfavorable overall survival and recurrence-free survival in non-small cell lung adenocarcinoma
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High expression of S100A6 in ICC defines a special group of patients with worse clinical characteristics and outcomes. Besides, S100A6 may promote ICC proliferation via activating p38/MAPK pathway.
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The results suggest that binding of S100A6 to integrin beta1 affects cell adhesion/proliferation due to activation of ILK and FAK signaling pathways.
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Authors demonstrated that the expression of S100A6 was significantly associated with patient age and tumor differentiation.
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Data show that S100 calcium binding protein A6 (S100A6) is required for the Ca2+-dependent nuclear translocation of calcyclin binding protein (CacyBP/SIP) in colon cancer SW480 cells.
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Isothermal titration calorimetry measured the binding of peptides with diverse sequence and biochemistry to human S100A5 and S110A6. These proteins bound distinct, but overlapping, sets of peptide targets. The specificity of S100 peptide interfaces is likely important for the biology of these proteins.
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S100A6 is a potential risk marker for screening of cholangiocarcinoma.
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The S100A6 interacts with FOR20 and related centrosomal proteins through a conserved N-terminal domain, suggesting a novel Ca(2+)-dependent regulation of centrosomal function.
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REVIEW: summary of novel discoveries concerning S100A6 targets, its involvement in cellular signaling pathways, and presence in stem/progenitor cells, extracellular matrix and body fluids of diseased patients
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Results showed that S100A6 was markedly up-regulated in nasopharyngeal carcinoma (NPC) tissues and cell lines and, may promote NPC development via the activation of p38/MAPK signaling pathways.
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As an intracellular protein, S100A6 has been implicated in the regulation of several cellular functions, such as proliferation, apoptosis, the cytoskeleton dynamics, and the cellular response to different stress factors. S100A6 can be secreted/released by certain cell types which points to extracellular effects of the protein. [review]
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suppression of S100A6 expression with RNAi significantly decreased the expression levels of beta-catenin, inhibited the growth and migration of eutopic endometrial stromal cells, and promoted their apoptosis.
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Study reports the crystallographic structure of an S100-bound full-length RAGE ectodomain. The structure reveals a unique dimeric conformation of RAGE, which appears suited for signal transduction, and shows that the S100A6 protein adopts a non-canonical homodimeric arrangement.
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STAT1 suppression by S100A6 may represent a promising therapeutic target to facilitate reendothelialization in damaged vessels.
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Our results indicate that serum levels of S100A2 and S100A6 are significantly elevated in early stage non-small cell lung cancer
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findings strongly suggest that S100A6 may promote OS cell proliferation and OS tumor growth at least in part by facilitating cell cycle progression, preventing apoptosis, and inhibiting osteogenic differentiation
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S100A6 induces EMT and promotes cell migration and invasion in a beta-catenin-dependent manner.
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Weak or absent S100A6 staining supports a diagnosis of pilar leiomyoma, whereas strong positive staining supports a diagnosis of cutaneous leiomyosarcoma.
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Elevated S100A6 enhances tumorigenesis and suppresses CXCL14-induced apoptosis in clear cell renal cell carcinoma.
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Applying this serum marker to clinical practice would require less-invasive examinations of patients and would help to detect life-threatening cancerous lesions earlier than current modalities.
