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S100 calcium-binding protein A10 contributes to malignant traits in osteosarcoma cells by regulating glycolytic metabolism via the AKT/mTOR pathway.

ABSTRACT: As an aggressive musculoskeletal malignancy, osteosarcoma (OSa) is popular among young adults and teenagers worldwide. S100 calcium-binding protein A10 (S100A10) functioned as a novel tumor-promoting protein in several human cancers. However, its role in OSa remains obscure. In this study, gene and protein levels were respectively determined by RT-qPCR or Western blotting. OSa cell proliferation, apoptosis, and metastasis were evaluated via CCK-8, colony formation, flow cytometry, and Transwell assays. To assess the glycolysis level, glucose consumption and lactate production were detected. It was found S100A10 was highly expressed in OSa tissues and cell lines. Besides, S100A10 facilitated proliferation and metastasis, and inhibited apoptosis in OSa cells. In addition, S100A10 regulated OSa cell proliferation, metastasis and apoptosis via mediating the glycolysis process. Furthermore, S100A10-mediated AKT/mTOR signaling accelerated glycolysis, thereby promoting malignant behaviors in OSa cells. Taken together, our findings indicated that S100A10 might promote malignant phenotypes of OSa cells by accelerating glycolysis and activating the AKT/mTOR signaling, providing a promising target for OSa treatment.

SUBMITTER: Ling F

PROVIDER: S-EPMC9276053 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

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S100 calcium-binding protein A10 contributes to malignant traits in osteosarcoma cells by regulating glycolytic metabolism via the AKT/mTOR pathway.

Ling Feng F Lu Qifeng Q

Bioengineered 20220501 5

As an aggressive musculoskeletal malignancy, osteosarcoma (OSa) is popular among young adults and teenagers worldwide. S100 calcium-binding protein A10 (S100A10) functioned as a novel tumor-promoting protein in several human cancers. However, its role in OSa remains obscure. In this study, gene and protein levels were respectively determined by RT-qPCR or Western blotting. OSa cell proliferation, apoptosis, and metastasis were evaluated via CCK-8, colony formation, flow cytometry, and Transwell ...[more]

PMID: 35579448

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Project description:PURPOSE: Pterygium is an ocular surface disease of unknown etiology associated with epithelial and fibrovascular outgrowth from the conjunctiva onto the cornea. S100 proteins are calcium-activated signaling proteins that interact with other proteins to modulate biological functions such as cell migration, proliferation, and differentiation. The aim of this study was to investigate the presence of various S100 proteins in pterygium compared to normal conjunctiva. METHODS: Immunofluorescent staining using antibodies against S100A4, S100A6, S100A8, S100A9, and S100A11 were conducted to investigate the expression and tissue distribution. S100 protein secretions and expressions were confirmed using western blot and quantitative real-time polymerase chain reaction (RT-PCR), respectively. RESULTS: Immunofluorescent staining demonstrated the presence of S100A4, S100A6, S100A8, S100A8, S100A9, and S100A11 in both conjunctival and pterygial epithelium. No significant difference was found in the localization and expression of S100A4. In both conjunctiva and pterygium, S100A4-positive cells were found in superficial and suprabasal layers. S100A6 expression was strong in the superficial layer of pterygium epithelium but relatively weaker in the suprabasal and superficial cells of normal conjunctiva epithelium. S100A8 and S100A9 were localized in the superficial layer of both pterygium and normal conjunctiva epithelium, with higher levels in pterygium than uninvolved conjunctiva. S100A11 was expressed in the basal cells of conjunctival epithelium but in the suprabasal layers of pterygium epithelium. Western blot and RT-PCR confirmed the presence of S100A4, S100A6, S100A8, S100A9, and S100A11 in pterygium and conjunctiva tissue. CONCLUSIONS: Higher levels of S100A6, S100A8, and S100A9 expressions were detected in the pterygium tissue relative to normal conjunctiva. In addition, a distinct alteration of localization of S100A11 expression was observed in pterygium epithelium compared to the conjunctiva. Therefore, these S100 proteins may be associated with the formation of pterygium.

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S100 calcium-binding protein A10 contributes to malignant traits in osteosarcoma cells by regulating glycolytic metabolism via the AKT/mTOR pathway.

Publications

S100 calcium-binding protein A10 contributes to malignant traits in osteosarcoma cells by regulating glycolytic metabolism via the AKT/mTOR pathway.

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