The First School of Clinical Medicine of Lanzhou University, Lanzhou, 730013, Gansu Province, China.
Department of Gynecology, the Second Hospital of Lanzhou University, Lanzhou, 730013, Gansu Province, China.
BMC Cancer. 2023 Nov 17;23(1):1124. doi: 10.1186/s12885-023-11574-y.
S100A16 protein belongs to the S100 family of calcium-binding proteins, which is widely distributed in human tissues and highly conserved. S100 calcium-binding proteins possess broad biological functions, such as cancer cell proliferation, apoptosis, tumor metastasis, and inflammation (Nat Rev Cancer 15:96-109, 2015). The S100A16 protein was initially isolated from a cell line derived from astrocytoma. The S100A16 protein, consisting of 103 amino acids, is a small acidic protein with a molecular weight of 11,801.4 Da and an isoelectric point (pI) of 6.28 (Biochem Biophys Res Commun 313:237-244, 2004). This protein exhibits high conservation among mammals and is widely expressed in various human tissues (Biochem Biophys Res Commun 322:1111-1122, 2004). Like other S100 proteins, S100A16 contains two EF-hand motifs that form a helix-loop-helix structural domain. The N-terminal domain and the C-terminal domain of S100A16 are connected by a "hinge" linker.S100A16 protein exhibits distinct characteristics that distinguish it from other S100 proteins. A notable feature is the presence of a single functional Ca2 + binding site located in the C-terminal EF-hand, consisting of 12 amino acids per protein monomer (J Biol Chem 281:38905-38917, 2006). In contrast, the N-terminal EF-hand of S100A16 comprises 15 amino acids instead of the typical 14, and it lacks the conserved glutamate residue at the final position. This unique attribute may contribute to the impaired Ca2 + binding capability in the N-terminal region (J Biol Chem 281:38905-38917, 2006). Studies have shown an integral role of S100 calcium-binding proteins in the diagnosis, treatment, and prognosis of certain diseases (Cancers 12:2037, 2020). Abnormal expression of S100A16 protein is implicated in the progression of breast and prostate cancer, but an inhibitor of oral cancer and acute lymphoblastic leukemia tumor cell proliferation (BMC Cancer 15:53, 2015; BMC Cancer 15:631, 2015). Tu et al. (Front Cell Dev Biol 9:645641, 2021) indicate that the overexpression of S100A16 mRNA in cervical cancer(CC) such as cervical squamous cell carcinoma and endocervical adenocarcinoma as compared to the control specimens. Tomiyama N. and co-workers (Oncol Lett 15:9929-9933, 2018) (Tomiyama, N) investigated the role of S100A16 in cancer stem cells using Yumoto cells (a CC cell line),The authors found upregulation of S100A16 in Yumoto cells following sphere formation as compared to monolayer culture.Despite a certain degree of understanding, the exact biological function of S100A16 in CC is still unclear. This article explores the role of S100A16 in CC through a bioinformatics analysis. Referencing the mRNA expression and SNP data of cervical cancer available through The Cancer Genome Atlas (TCGA) database, we analyzed S100A16 and its associated regulatory gene expression network in cervical cancer. We further screened genes co-expressed with S100A16 to hypothesize their function and relationship to the S100A16 cervical cancer phenotype.Our results showed that data mining can effectively elucidate the expression and gene regulatory network of S100A16 in cervical cancer, laying the foundation for further investigations into S100A16 cervical tumorigenesis.
S100A16 蛋白属于 S100 家族的钙结合蛋白,广泛分布于人体组织中,高度保守。S100 钙结合蛋白具有广泛的生物学功能,如促进癌细胞增殖、凋亡、肿瘤转移和炎症(Nat Rev Cancer 15:96-109, 2015)。S100A16 蛋白最初从星形细胞瘤衍生的细胞系中分离出来。S100A16 蛋白由 103 个氨基酸组成,是一种分子量为 11801.4 Da、等电点(pI)为 6.28 的小酸性蛋白(Biochem Biophys Res Commun 313:237-244, 2004)。这种蛋白质在哺乳动物中高度保守,广泛存在于各种人体组织中(Biochem Biophys Res Commun 322:1111-1122, 2004)。与其他 S100 蛋白一样,S100A16 含有两个 EF 手模体,形成一个螺旋-环-螺旋结构域。S100A16 的 N 端结构域和 C 端结构域由一个“铰链”连接。S100A16 蛋白具有独特的特征,使其与其他 S100 蛋白区分开来。一个显著的特征是存在一个单一的功能 Ca2+结合位点,位于 C 端 EF 手模体中,每个蛋白单体由 12 个氨基酸组成(J Biol Chem 281:38905-38917, 2006)。相比之下,S100A16 的 N 端 EF 手模体由 15 个氨基酸组成,而不是典型的 14 个,并且最后一个位置没有保守的谷氨酸残基。这种独特的属性可能导致 N 端区域 Ca2+结合能力受损(J Biol Chem 281:38905-38917, 2006)。研究表明,S100 钙结合蛋白在某些疾病的诊断、治疗和预后中具有重要作用(Cancers 12:2037, 2020)。S100A16 蛋白的异常表达与乳腺癌和前列腺癌的进展有关,但对口腔癌和急性淋巴细胞白血病肿瘤细胞增殖有抑制作用(BMC Cancer 15:53, 2015; BMC Cancer 15:631, 2015)。Tu 等人(Front Cell Dev Biol 9:645641, 2021)指出,与对照标本相比,宫颈癌(如宫颈鳞状细胞癌和宫颈内膜腺癌)中 S100A16 mRNA 的过度表达。Tomiyama N. 和他的同事(Oncol Lett 15:9929-9933, 2018)(Tomiyama, N)使用 Yumoto 细胞(一种宫颈癌细胞系)研究了 S100A16 在癌症干细胞中的作用,作者发现与单层培养相比,S100A16 在 Yumoto 细胞形成球体后上调。尽管对其有一定程度的了解,但 S100A16 在宫颈癌中的确切生物学功能仍不清楚。本文通过生物信息学分析探讨了 S100A16 在宫颈癌中的作用。参考癌症基因组图谱(TCGA)数据库中宫颈癌的 mRNA 表达和 SNP 数据,我们分析了宫颈癌中 S100A16 及其相关调节基因表达网络。我们进一步筛选与 S100A16 共表达的基因,假设它们的功能与 S100A16 宫颈癌表型的关系。我们的结果表明,数据挖掘可以有效地阐明 S100A16 在宫颈癌中的表达和基因调控网络,为进一步研究 S100A16 宫颈癌发生机制奠定了基础。