RESUMEN
Using in situ formed metal complexes of [Fe(bipy)3]2+ or [Ni(bipy)3]2+ (bipy = 2,2'-bipyridine) as templates, four new Ag-Bi-X (X = I and Br) compounds are first isolated in the metal-complex-decorated heterometallic halobismuthate family, namely [M(bipy)3]AgBiI6 (M = Fe (1), Ni (2)), [Fe(bipy)3]AgBiBr6 (3), and [Ni(bipy)3]AgBiBr6 (4). Compounds 1-4 feature discrete [AgBiX6]n2n- anions, exhibiting three polymorphisms that may be ascribed to the different stackings and the flexible condensations of [BiX6] octahedrons and [AgX4] tetrahedra/[AgX3] triangles. UV-vis diffuse reflectance analyses reveal that they are narrow band gap semiconductor materials (ca. 1.82-2.13 eV). Intriguingly, the title compounds display excellent photoelectrical switching properties, with photocurrent density following the order 3 > 4 > 2 > 1. In addition, the comparative studies of intermolecular interactions, theoretical band structures, density of states, and effective masses of three polymorphisms have also been investigated.
RESUMEN
BACKGROUND: Long noncoding RNAs (lncRNAs) are essential modulators of cancers initiation and progression via regulating gene expression and biological behaviors. LncRNA SAMD12-AS1 has been validated to promote the progression of several cancers, while its role in gastric cancer (GC) remains unclear. This study aims to explore the role of LncRNA SAMD12-AS1 in GC. METHODS: qRT-PCR was performed to analyze the expression of lncRNA SAMD12-AS1 in GC tissues and cell lines, with Kaplan-Meier curve analyzing the correlation between LncRNA SAMD12-AS1 and prognosis. CCK-8 assay, and flow cytometry were applied to detect GC cells proliferation, cell cycle. Binding of RNA and proteins were detected via RNA binding protein immunoprecipitation (RIP) assay. Protein levels of oncogenesis-related genes were determined via western blotting. RESULTS: SAMD12-AS1 was highly up-regulated in human gastric cancer tissues and cell lines compared to their normal counterparts. High SAMD12-AS1 expression was closely related to TNM stage, and shorter survival span of patients with GC. Moreover, SAMD12-AS1 was also found to promote the oncogenic role of GC cells via inhibiting the P53 signaling pathway. Mechanistically, SAMD12-AS1 might performed its biological roles in GC via directly interacting with DNMT1 and facilitating DNMT1 repress the P53 signaling pathway. CONCLUSION: Our study demonstrated that SAMD12-AS1 promoted GC progression via DNMT1/P53 axis, indicating SAMD12-AS1 may be envisioned as a novel biomarker of, and therapeutic target for GC.