Background: N6-methyladenosine (m6A) is found in almost all nuclear RNAs of eukaryotes, playing an important and diverse role in many biological processes. Nonetheless, the roles of m6A regulators in abdominal aortic aneurysm (AAA) unknown. Therefore, there is a pressing need to identify m6A RNA methylation regulators in the diagnosis of AAA, determination of individualized risk, discovery of therapeutic targets, and improve understanding of pathogenesis.Methods: The GSE98278 dataset were obtained from the Gene Expression Omnibus (GEO) database to perform differential analysis of m6A-related regulators between elective stable abdominal aortic aneurysms (eAAA) and abdominal aortic aneurysm ruptured (rAAA). The random forest model was used to screen candidate m6A regulators to predict the risk of rAAA. The single sample gene set enrichment analysis (ssGSEA) method was then used to evaluate the abundance of 23 immune cells in AAA. The m6A RNA Methylation Quantification Kit was used to measure the total m6A levels of AAA and normal abdominal aorta. The terminal deoxynucleotidyl transferase mediated dUTP Nick-End Labeling (TUNEL) apoptosis assay kit was used to detect the human aortic smooth muscle cells (HASMCs) apoptotic after RBM15 knockdown. Mechanically, RBM15 knockdown was found to reduce the expression of CASP3 in an m6A-dependent manner by Western blotting, RNA immunoprecipitation (RIP), and methylated RNA immunoprecipitation-quantitative polymerase chain reaction (MeRIP-RT-PCR).Results: RBM15, WTAP, ALKBH5, and IGFBP3 were highly expressed in rAAA. In contrast, RBM15B showed opposite results (P<0.05). The high m6A level in the rAAA compared with eAAA and normal abdominal aorta (P<0.05). The random forest model was used to screen 5 candidate m6A regulators to predict the risk of rAAA. Expression of the 5 m6A methylation regulators was validated in AAA samples (P<0.05). RBM15 knockdown inhibited the apoptosis of HASMCs. RBM15 knockdown reduced the expression of CASP3 in an m6A-dependent manner. A strong correlation between the five m6A methylation regulators and immune cell infiltration was identified.Conclusions: In summary, m6A regulators play nonnegligible roles in the occurrence of rAAA. Our investigation of m6A patterns may be able to guide future immunotherapy strategies for AAA.

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In the title salt, [Zn(C6H15NO3)2](C8H4O4), the ZnII cation, located on a centre of inversion, is coordinated by four O atoms and two N atoms from two tridentate 2-[bis­(2-hy­droxy­eth­yl)amino]­ethanol (BHEA) ligands, giving rise to a slightly distorted octa­hedral geometry. The terephthalate dianion, located about a centre of inversion, is not coordinated to ZnII but is connected through O—H⋯O contacts with [Zn(BHEA)2]2+ cations, leading to a three-dimensional crystal structure.

In the title compound, {[Zn(C12H8O4)(C12H8N2)(H2O)]·0.5H2O}n, each ZnII atom is six-coordinated by two N atoms from one 1,10-phenanthroline (phen), three carboxyl­ate O atoms from two different L ligands [H2 L = 3,3′-(p-phenyl­ene)diacrylic acid] and one water mol­ecule in a distorted octa­hedral environment. The two L dianions are situated across inversion centres and bridge neighbouring ZnII centres, yielding a chain propagating parallel to [100]. O—H⋯O hydrogen bonds between the coordinated water molecule, the solvent water molecule (half-occupied) and the carboxylate O atoms further stabilize the structure.