Identification of the STY13 gene family across the entire genome and an analysis of the essential function of GhSTY13-12 in cotton’s response to abiotic stress

Article

Author: Lu, Quanwei ; Wan, Sumei ; Zhang, Shaoliang ; Liu, Zili ; Liu, Yuling ; Wei, Yangyang ; Shan, Huiyun ; Peng, Renhai ; Hu, Shoulin ; Yang, Xiaojie ; Bo, Xiaopei ; Li, Pengtao ; Li, Jiahui

Cotton is an important cash crop, and its yield and quality were affected by abiotic stresses. The serine/threonine protein kinase STY13 gene, belonging to the protein kinase family, is one of the largest and most functionally diverse gene families, which is a critical regulatory molecule for cell function. In this study, we systematically identified and analyzed the STY13 gene family in two major cultivated cotton species (Gossypium hirsutum and Gossypium barbadense) and their two ancestors (Gossypium arboretum and Gossypium raimondii). A total of 46, 50, 26 and 24 STY13 genes were identified from these four species, respectively. Phylogeny analysis showed that cotton STY13 genes (cotton STY protein kinase genes) could be classified into five groups. This gene family was evenly distributed on each chromosome in cotton. STY13 genes contain light-responsive elements, stress-responsive elements, growth and developmental elements, and multiple gene and protein binding sites. Most motifs in the STY13 proteins were conserved and had similar distribution patterns. However, there were some differences in specific motifs in different subfamilies. Gene expression analysis based on RNA-seq and qRT-PCR showed that STY13 genes were responsive to abiotic stress. GhSTY13-12 gene was located in cytoplasm. Silencing of the GhSTY13-12 gene resulted in reduced leaf chlorosis, increased total antioxidant capacity, decreased malondialdehyde content, and enhanced drought and salt tolerance. These results provide a scientific basis for further research on the function of STY13 in cotton and its application on cotton trait improvement.

01 Aug 2025·Food Chemistry

Metabolomics unravels the formation pathway of advanced glycation end products in preserved egg yolk mediated by OH− during pickling

Article

Author: Yu, Zhuosi ; Li, Shugang ; Huang, Yiqun ; Dong, Shiqin ; Chen, Le ; Xiang, Xiaole ; Ye, Lin ; He, Yu

Metabolomics was first applied to explore the formation pathway and regulatory factors for advanced glycation end products (AGEs) in preserved egg yolk (PEY) during pickling. Most reactions that contributed to formation of AGEs, including oxidation and/or degradation of matrix/precursors and Maillard reaction, occurred primarily in PEY in early stage, and lipid oxidation occurred prior to protein oxidation. Additionally, the formation of N^ε-carboxymethyl-lysine (CML) in PEY was mainly attributed to glyoxal derived from D-glucuronic acid in early stage based on the correlation between metabolites and AGEs. Reactive oxygen radicals from oxidized lipids also promoted the enrichment of CML and N^ε-carboxymethyl-lysine (CEL). Moreover, during later stage, the accumulation of CEL was enhanced through methylglyoxal from Schiff bases, and acidic compounds could inhibit AGEs via hindering Maillard reaction. This manuscript pioneered the application of metabolomics to reveal the formation pathway of AGEs, and will provide new perspective on AGEs formation in foods.

01 Jun 2025·Surgery

Beta-catenin/sirtuin 1/farnesoid X receptor pathway promotion of portal vein ligation and parenchymal transection-induced rapid liver regeneration

Article

Author: Li, Zheyong ; Shen, Bo ; Tong, Yifan ; Cai, Xiujun ; Gu, Qiuxia ; Feng, Lifeng ; Ji, Tong ; Dong, Bingzhi ; Shen, Xiaoyun ; Yu, Hong ; Ying, Hanning

BACKGROUNDBy accelerating the regeneration of the future liver remnant, portal vein ligation and parenchymal transection allows for more extensive hepatectomy. Given that the mechanism remains poorly understood, the aim of this study was to investigate the mechanism of portal vein ligation and parenchymal transection-induced liver regeneration.METHODSA portal vein ligation and parenchymal transection-induced liver regeneration mouse model was established, followed by RNA microarray analysis to identify candidate molecules. Genomic deletion and chemical manipulation of target molecules were used to explore their functions in portal vein ligation and parenchymal transection-induced liver regeneration. Validation was conducted using a diseased liver model and human samples.RESULTSPortal vein ligation and parenchymal transection-induced liver regeneration was significantly accelerated compared with that in sham-operated mice (P < .05). An RNA microarray revealed that Sirtuin 1 is a crucial molecule in the proliferation of the future liver remnant. Regardless of whether Sirtuin 1 is inhibited chemically or through genetic deletion, portal vein ligation and parenchymal transection-induced liver regeneration is distinctly attenuated. Further investigation revealed that Sirtuin 1 promoted portal vein ligation and parenchymal transection-induced liver regeneration via the farnesoid X receptor. In addition, beta-catenin also was found to participate in the process of future liver remnant proliferation. Chemical inhibition of beta-catenin markedly impaired but activation of WNT/beta-catenin mildly enhanced portal vein ligation and parenchymal transection-induced liver regeneration (P < .05). Deletion of Sirtuin 1 blocked the facilitating effect of beta-catenin on portal vein ligation and parenchymal transection-induced liver regeneration. These findings were validated in diseased liver models and patient samples, confirming the correlation between the beta-catenin/Sirtuin 1/farnesoid X receptor pathway and portal vein ligation and parenchymal transection-induced liver regeneration.CONCLUSIONActivation of the beta-catenin/Sirtuin 1/farnesoid X receptor pathway offers critical mechanistic insights into accelerating portal vein ligation and parenchymal transection-induced liver regeneration. Modulation of beta-catenin/Sirtuin 1/farnesoid X receptor may therefore improve clinical outcomes in patients receiving staged hepatectomy.

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