A Heterogeneous Graph to Abstract Syntax Tree Framework for Text-to-SQL.

Text-to-SQL is the task of converting a natural language utterance plus the corresponding database schema into a SQL program. The inputs naturally form a heterogeneous graph while the output SQL can be transduced into an abstract syntax tree (AST). Traditional encoder-decoder models ignore higher-order semantics in heterogeneous graph encoding and introduce permutation biases during AST construction, thus incapable of exploiting the refined structure knowledge precisely. In this work, we propose a generic heterogeneous graph to abstract syntax tree (HG2AST) framework to integrate dedicated structure knowledge into statistics-based models. On the encoder side, we leverage a line graph enhanced encoder (LGESQL) to iteratively update both node and edge features through dual graph message passing and aggregation. On the decoder side, a grammar-based decoder first constructs the equivalent SQL AST and then transforms it into the desired SQL via post-processing. To avoid over-fitting permutation biases, we propose a golden tree-oriented learning (GTL) algorithm to adaptively control the expanding order of AST nodes. The graph encoder and tree decoder are combined into a unified framework through two auxiliary modules. Extensive experiments on various text-to-SQL datasets, including single/multi-table, single/cross-domain, and multilingual settings, demonstrate the superiority and broad applicability.

Overexpression of miR-146a promotes cell proliferation and migration in a model of diabetic foot ulcers by regulating the AKAP12 axis.

In the current study, we aimed to study the effect of miR-146a on proliferation and migration in an in vitro diabetic foot ulcer (DFU) model by targeting A-kinase-anchoring protein 12 (AKAP12). An in vitro DFU model was initially established using HaCaT cells derived from human keratinocytes and induced by advanced glycation end products (AGEs). The effects of overexpression of miR-146a on proliferation and migration ability were analysed. The expression levels of miR-146a and AKAP12 were measured by quantitative real-time polymerase chain reaction (qRT-PCR), and AKAP12, hypoxia-inducible factor-1α (HIF-1α), Wnt3a and ß-catenin protein levels were measured by western blotting. The cell proliferation ability was measured by MTT, and the migration ability was analysed by a cell scratch assay. The binding between miR-146a and AKAP12 was identified using a luciferase reporter assay. The results demonstrated that AGEs significantly suppressed cell proliferation and migration, while the expression of miR-146a decreased and the expression of AKAP12 increased. A luciferase reporter assay revealed that miR-146a could directly target AKAP12. Overexpression of miR-146a promoted cell proliferation and migration in an in vitro DFU model and also promoted the expression of HIF-1α, Wnt3a and ß-catenin but suppressed the expression of AKAP12. Co-overexpression of miR-146a and AKAP12 reversed the effect of miR-146a on cell proliferation and migration. Our findings revealed that miR-146a directly targeted AKAP12 and promoted cell proliferation and migration in an in vitro DFU model. This study provides a new perspective for the study of miR-146a in the treatment of DFU.

WTS-1/LATS regulates endocytic recycling by restraining F-actin assembly in a synergistic manner.

The disruption of endosomal actin architecture negatively affects endocytic recycling. However, the underlying homeostatic mechanisms that regulate actin organization during recycling remain unclear. In this study, we identified a synergistic endosomal actin assembly restricting mechanism in C. elegans involving WTS-1, the homolog of LATS kinases, which is a core component of the Hippo pathway. WTS-1 resides on the sorting endosomes and colocalizes with the actin polymerization regulator PTRN-1 [the homolog of the calmodulin-regulated spectrin-associated proteins (CAMSAPs)]. We observed an increase in PTRN-1-labeled structures in WTS-1-deficient cells, indicating that WTS-1 can limit the endosomal localization of PTRN-1. Accordingly, the actin overaccumulation phenotype in WTS-1-depleted cells was mitigated by the associated PTRN-1 loss. We further demonstrated that recycling defects and actin overaccumulation in WTS-1-deficient cells were reduced by the overexpression of constitutively active UNC-60A(S3A) (a cofilin protein homolog), which aligns with the role of LATS as a positive regulator of cofilin activity. Altogether, our data confirmed previous findings, and we propose an additional model, that WTS-1 acts alongside the UNC-60A-mediated actin disassembly to restrict the assembly of endosomal F-actin by curbing PTRN-1 dwelling on endosomes, preserving recycling transport.

MicroRNA screening identifies circulating microRNAs as potential biomarkers for osteosarcoma.

MicroRNAs (miRNAs) are a family of small non-protein coding RNAs, which regulate the expression of a wide variety of genes at the post-transcriptional level to control numerous biological and pathological processes. Various circulating miRNAs have been identified as potential diagnostic and prognostic biomarkers in multiple types of cancer and disease. The aim of the present study was to identify potential miRNA biomarkers for the early diagnosis and relapse prediction of osteosarcoma (OS). miRNA profiling was performed on serum from patients with osteosarcoma and healthy controls. All putative miRNAs were verified by reverse transcription-quantitative polymerase chain reaction analysis of 20 pre-therapeutic OS patients and 20 healthy individuals. The expression of miR-106a-5p, miR16-5p, miR-20a-5p, miR-425-5p, miR451a, miR-25-3p and miR139-5p was demonstrated to be downregulated in the serum of OS patients when compared with that of the healthy controls. Receiver-operating characteristic curve analyses indicated that these 7 miRNAs may be used as diagnostic biomarkers with the ability to discriminate between the healthy cohort and patients with OS. These results provide novel insights into the use of miRNAs in early blood screening for OS.