14 results on '"Baihui Sun"'
Search Results
2. Analysis of scene-guided camera assistance in transaxillary gasless endoscopic thyroidectomy: a minor improvement in operative technique
- Author
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Baihui Sun, Shitong Yu, Junna Ge, Zhicheng Zhang, Weisheng Chen, Zhigang Wei, Tingting Li, and Shangtong Lei
- Subjects
transaxillary gasless endoscopic thyroidectomy ,scene-guided camera assistance ,camera holders ,thyroid carcinoma ,operative technique ,Diseases of the endocrine glands. Clinical endocrinology ,RC648-665 - Abstract
BackgroundTransaxillary gasless endoscopic thyroidectomy (TGET) is a widely performed operation, but its side view angle and instrument interference have caused concerns for most surgical groups. The aim of this study was to introduce scene-guided camera assistance (SGA) and analyze its role in facilitating TGET.MethodsWe put forward key points for camera holders, including one pivot, two positions, and three planes, and separated TGET operations into five parts. We also established the view angle for each part of the operation for the camera holder to follow. Then, we reviewed 416 patients who underwent TGET with or without SGA and analyzed their demographic characteristics, operative outcomes, pathologic outcomes, and early complications.ResultsThe TGET and TGET-SGA groups were similar in terms of age, sex ratio, height, weight, tumor size, Hashimoto’s thyroiditis ratio, and cN1 ratio. The operation time and postoperative hospital stay were significantly longer in the TGET group than in the TGET-SGA group (114.43 ± 17.20 minutes vs. 101.82 ± 19.39 minutes and 3.16 ± 0.77 days vs. 2.16 ± 0.55 days, respectively, P < 0.001). The account of retrieved lymph nodes was less in the TGET group than in the TGET-SGA group (5.61 ± 4.27 vs. 6.57 ± 4.96, P = 0.038).ConclusionSGA provided guidance for camera holders, and the data showed that it was an improvement for TGET operations.
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- 2023
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3. Advanced oxidation protein products sensitized the transient receptor potential vanilloid 1 via NADPH oxidase 1 and 4 to cause mechanical hyperalgesia
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Ruoting Ding, Hui Jiang, Baihui Sun, Xiaoliang Wu, Wei Li, Siyuan Zhu, Congrui Liao, Zhaoming Zhong, and Jianting Chen
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Advanced oxidation protein products ,Hyperalgesia ,Dorsal root ganglion ,NADPH oxidase ,TRPV1 ,Medicine (General) ,R5-920 ,Biology (General) ,QH301-705.5 - Abstract
Oxidative stress is a possible pathogenesis of hyperalgesia. Advanced oxidation protein products (AOPPs), a new family of oxidized protein compounds, have been considered as a novel marker of oxidative stress. However, the role of AOPPs in the mechanism of hyperalgesia remains unknown. Our study aims to investigate whether AOPPs have an effect on hyperalgesia and the possible underlying mechanisms. To identify the AOPPs involved, we induced hyperalgesia in rats by injecting complete Freund’s adjuvant (CFA) in hindpaw. The level of plasma AOPPs in CFA-induced rats was 1.6-fold in comparison with what in normal rats (P
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- 2016
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4. Advanced Oxidative Protein Products Cause Pain Hypersensitivity in Rats by Inducing Dorsal Root Ganglion Neurons Apoptosis via NADPH Oxidase 4/c-Jun N-terminal Kinase Pathways
- Author
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Ruoting Ding, Baihui Sun, Zhongyuan Liu, Xinqiang Yao, Haiming Wang, Xing Shen, Hui Jiang, and Jianting Chen
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advanced oxidative protein products ,hypersensitivity ,apoptosis ,oxidative stress ,dorsal root ganglion ,Neurosciences. Biological psychiatry. Neuropsychiatry ,RC321-571 - Abstract
Pain hypersensitivity is the most common category of chronic pain and is difficult to cure. Oxidative stress and certain cells apoptosis, such as dorsal root ganglion (DRG) neurons, play an essential role in the induction and development of pain hypersensitivity. The focus of this study is at a more specific molecular level. We investigated the role of advanced oxidative protein products (AOPPs) in inducing hypersensitivity and the cellular mechanism underlying the proapoptotic effect of AOPPs. Normal rats were injected by AOPPs-Rat serum albumin (AOPPs–RSA) to cause pain hypersensitivity. Primary cultured DRG neurons were treated with increasing concentrations of AOPPs–RSA or for increasing time durations. The MTT, flow cytometry and western blot analyses were performed in the DRG neurons. A loss of mitochondrial membrane potential (MMP) and an increase in intracellular reactive oxygen species (ROS) were observed. We found that AOPPs triggered DRG neurons apoptosis and MMP loss. After AOPPs treatment, intracellular ROS generation increased in a time- and dose-dependent manner, whereas, N-acetyl-L-cysteine (NAC), a specific ROS scavenger could inhibit the ROS generation. Proapoptotic proteins, such as Bax, caspase 9/caspase 3, and PARP-1 were activated, whereas anti-apoptotic Bcl-2 protein was down-regulated. AOPPs also increased Nox4 and JNK expression. Taken together, these findings suggest that AOPPs cause pain hypersensitivity in rats, and extracellular AOPPs accumulation triggered Nox4-dependent ROS production, which activated JNK, and induced DRG neurons apoptosis by activating caspase 3 and PARP-1.
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- 2017
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5. The lymph node yield in the initial lateral neck dissection predicts recurrence in the lateral neck of papillary thyroid carcinoma: a revision surgery cohort study
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Shi-Tong Yu, Junna Ge, Zhigang Wei, Baihui Sun, Zizheng Xiao, Tingting Li, Zhicheng Zhang, Weisheng Chen, and Shang-Tong Lei
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Surgery ,General Medicine - Published
- 2023
6. Fusion of acoustic and deep features for pig cough sound recognition.
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Weizheng Shen, Nan Ji, Yanling Yin, Baisheng Dai, Ding Tu, Baihui Sun, Handan Hou, Shengli Kou, and Yize Zhao
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- 2022
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7. Advanced oxidation protein products mediate human keratinocytes apoptosis by inducing cell autophagy through the mTOR–Beclin‐1 pathway
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Ruoting Ding, Zhongyuan Liu, Jie Tan, and Baihui Sun
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Clinical Biochemistry ,Cell Biology ,General Medicine ,Biochemistry - Abstract
Excessive keratinocyte apoptosis leads to impaired wound healing. Recently, advanced oxidation protein products (AOPP) have been recognized as a marker of oxidative stress and a potent inducer of apoptosis. Previously, we have demonstrated that extracellular AOPP accumulation induced keratinocyte apoptosis, and we discovered that autophagy was involved. To further elucidate the role and mechanism of autophagy in AOPP-induced-apoptosis of keratinocytes, we treated HaCaT cells with increasing concentrations of AOPP-human serum albumin or with AOPP-human serum albumin for increasing durations. Cyto-ID solution staining was used to assess cell autophagy using confocal laser scanning microscopy. Autophagy-related protein interactions were investigated using western blot analysis. Exposure of HaCaT cells to AOPP decreased the expression of mammalian target of rapamycin (mTOR) and increased the expression of autophagy-related proteins Beclin-l and LC3, and eventually led to autophagy. Furthermore, an autophagy agonist significantly decreased the expression of apoptosis-related proteins. Taken together, we showed that accumulation of extracellular AOPP induced autophagy in HaCaT cells via a reactive oxygen species-dependent, mTOR-Beclin-1-mediated pathway, and that excessive autophagy-mediated apoptosis, which resulted in delayed wound healing.
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- 2022
8. The learning curve for gasless transaxillary posterior endoscopic thyroidectomy for thyroid cancer: a cumulative sum analysis
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Weisheng Chen, Shitong Yu, Baihui Sun, Cangui Wu, Tingting Li, Shumin Dong, Junna Ge, and Shangtong Lei
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Surgery - Published
- 2023
9. Discovery and optimization of 4-anilinoquinazoline derivatives spanning ATP binding site and allosteric site as effective EGFR-C797S inhibitors
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Dou Dou, Jie Wang, Yunjin Qiao, Gulinuer Wumaier, Wenjie Sha, Wenjie Li, Wenyi Mei, Tingyuan Yang, Chen Zhang, Huan He, Caolin Wang, Linna Chu, Baihui Sun, Rongrong Su, Xiangyu Ma, Mengdie Gong, Lijuan Xie, Wenzhe Jiang, Yanyan Diao, Lili Zhu, Zhenjiang Zhao, Zhuo Chen, Yufang Xu, Shengqing Li, and Honglin Li
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Pharmacology ,Binding Sites ,Lung Neoplasms ,Aniline Compounds ,Organic Chemistry ,General Medicine ,ErbB Receptors ,Adenosine Triphosphate ,Drug Resistance, Neoplasm ,Carcinoma, Non-Small-Cell Lung ,Cell Line, Tumor ,Mutation ,Drug Discovery ,Quinazolines ,Humans ,Protein Kinase Inhibitors ,Allosteric Site - Abstract
Epidermal growth factor receptor (EGFR) is an effective drug target for the treatment of non-small cell lung cancer (NSCLC). However, a tertiary point mutation (C797S) at the ATP binding pocket of the EGFR induces resistance to the third-generation EGFR inhibitors, due to the loss of covalent interaction with Cys797. Here, we designed a series of 4-anilinoquinazoline derivatives that simultaneously occupied the ATP binding pocket and the allosteric site. The newly-synthesized compounds displayed high potency against EGFR-C797S resistance mutation. Among them, compound 14d presented high anti-proliferative effect against BaF3-EGFR
- Published
- 2022
10. Proteomics and bioinformatics reveal insights into neuroinflammation in the acute to subacute phases in rat models of spinal cord contusion injury
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Xinqiang Yao, Junhao Liu, Zucheng Huang, Ruoting Ding, Jia-Ying Chen, Jian-Ting Chen, Baihui Sun, Zhongyuan Liu, and Qingan Zhu
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Male ,Proteomics ,0301 basic medicine ,Contusions ,Biology ,Biochemistry ,Neuroprotection ,Rats, Sprague-Dawley ,03 medical and health sciences ,0302 clinical medicine ,Western blot ,Lysosome ,Genetics ,medicine ,Animals ,Myeloid Cells ,Molecular Biology ,Spinal Cord Injuries ,Neuroinflammation ,Inflammation ,Neurons ,GPNMB ,medicine.diagnostic_test ,Microglia ,Macrophages ,Immunity ,Computational Biology ,PYCARD ,Rats ,Up-Regulation ,Cell biology ,Disease Models, Animal ,030104 developmental biology ,medicine.anatomical_structure ,Spinal Cord ,030217 neurology & neurosurgery ,Signal Transduction ,Biotechnology - Abstract
Neuroinflammation is recognized as a hallmark of spinal cord injury (SCI). Although neuroinflammation is an important pathogenic factor that leads to secondary injuries after SCI, neuroprotective anti-inflammatory treatments remain ineffective in the management of SCI. Moreover, the molecular signatures involved in the pathophysiological changes that occur during the course of SCI remain ambiguous. The current study investigated the proteins and pathways involved in C5 spinal cord hemi-contusion injury using a rat model by means of 4-D label-free proteomic analysis. Furthermore, two Gene Expression Omnibus (GEO) transcriptomic datasets, Western blot assays, and immunofluorescent staining were used to validate the expression levels and localization of dysregulated proteins. The present study observed that the rat models of SCI were associated with the enrichment of proteins related to the complement and coagulation cascades, cholesterol metabolism, and lysosome pathway throughout the acute and subacute phases of injury. Intriguingly, the current study also observed that 75 genes were significantly altered in both the GEO datasets, including ANXA1, C1QC, CTSZ, GM2A, GPNMB, and PYCARD. Further temporal clustering analysis revealed that the continuously upregulated protein cluster was associated with immune response, lipid regulation, lysosome pathway, and myeloid cells. Additionally, five proteins were further validated by means of Western blot assays and the immunofluorescent staining showed that these proteins coexisted with the F4/80+ reactive microglia and infiltrating macrophages. In conclusion, the proteomic data pertaining to the current study indicate the notable proteins and pathways that may be novel therapeutic targets for the treatment of SCI.
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- 2021
11. Residue mutations of xylanase in Aspergillus kawachii alter its optimum pH
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Baihui Sun, Rihe Peng, Lei Chen, Quanhong Yao, Jin Qiu, Chengye Yu, and Han Hongjuan
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Models, Molecular ,0301 basic medicine ,Mutant ,Protein Engineering ,Microbiology ,Pichia ,Pichia pastoris ,Fungal Proteins ,03 medical and health sciences ,Enzyme Stability ,Fungal protein ,Binding Sites ,Endo-1,4-beta Xylanases ,biology ,Aspergillus niger ,Hydrogen-Ion Concentration ,biology.organism_classification ,Yeast ,Kinetics ,030104 developmental biology ,Biochemistry ,Mutation ,Mutagenesis, Site-Directed ,Xylanase ,Fermentation - Abstract
Aspergillus kawachii and Aspergillus niger have been traditionally used as molds for commercial microbial fermentation because of their capability to grow in extremely acidic environments and produce acid-stable enzymes. Endo-1,4-β-xylanase cleaves the glycosidic bonds in the xylan backbone, consequently reducing the degree of polymerization of the substrate. The amino acid sequences of xylanases from A. kawachii and A. niger only differ in one amino acid residue. However, the xylanases from A. kawachii and A. niger show different optimum pH values of 2.0 and 3.0, respectively. In this study, we synthesized the A. kawachii xylanase gene (XynC) on the basis of the bias codon of yeast and mutated the gene in the dominating region related to optimum pH shifting during gene synthesis. After the overexpression of this gene in Pichia pastoris G115, the mutant (Thr64Ser) enzyme (XynC-C) showed an optimum pH of 3.8, which indicated partial alkalinity compared with the original xylanase from A. kawachii. Similar to that of the enzyme with one residue mutation (Asp48Asn), the optimum pH of the enzyme with two residue mutations (Thr64Ser and Asp48Asn) shifted to 5.0. The result indicated that mutation Asp48 was more important than mutation Thr64 in optimum pH shifting. We proposed a model that explains the lower optimum pH of XynC-C than other members of the xylanase family G. XynC-C showed similar proteolytic resistance and Km and Vmax values for beechwood xylan to other xylanases.
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- 2016
- Full Text
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12. Advanced Oxidative Protein Products Cause Pain Hypersensitivity in Rats by Inducing Dorsal Root Ganglion Neurons Apoptosis via NADPH Oxidase 4/c-Jun N-terminal Kinase Pathways
- Author
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Xing Shen, Baihui Sun, Xinqiang Yao, Hui Jiang, Ruoting Ding, Jianting Chen, Zhongyuan Liu, and Haiming Wang
- Subjects
0301 basic medicine ,dorsal root ganglion ,Caspase 3 ,medicine.disease_cause ,lcsh:RC321-571 ,03 medical and health sciences ,Cellular and Molecular Neuroscience ,0302 clinical medicine ,Dorsal root ganglion ,advanced oxidative protein products ,medicine ,oxidative stress ,Molecular Biology ,lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry ,Original Research ,Caspase-9 ,NADPH oxidase ,biology ,c-jun ,apoptosis ,NOX4 ,Cell biology ,030104 developmental biology ,medicine.anatomical_structure ,Apoptosis ,Immunology ,biology.protein ,hypersensitivity ,030217 neurology & neurosurgery ,Oxidative stress ,Neuroscience - Abstract
Pain hypersensitivity is the most common category of chronic pain and is difficult to cure. Oxidative stress and certain cells apoptosis, such as dorsal root ganglion (DRG) neurons, play an essential role in the induction and development of pain hypersensitivity. The focus of this study is at a more specific molecular level. We investigated the role of advanced oxidative protein products (AOPPs) in inducing hypersensitivity and the cellular mechanism underlying the proapoptotic effect of AOPPs. Normal rats were injected by AOPPs-Rat serum albumin (AOPPs–RSA) to cause pain hypersensitivity. Primary cultured DRG neurons were treated with increasing concentrations of AOPPs–RSA or for increasing time durations. The MTT, flow cytometry and western blot analyses were performed in the DRG neurons. A loss of mitochondrial membrane potential (MMP) and an increase in intracellular reactive oxygen species (ROS) were observed. We found that AOPPs triggered DRG neurons apoptosis and MMP loss. After AOPPs treatment, intracellular ROS generation increased in a time- and dose-dependent manner, whereas, N-acetyl-L-cysteine (NAC), a specific ROS scavenger could inhibit the ROS generation. Proapoptotic proteins, such as Bax, caspase 9/caspase 3, and PARP-1 were activated, whereas anti-apoptotic Bcl-2 protein was down-regulated. AOPPs also increased Nox4 and JNK expression. Taken together, these findings suggest that AOPPs cause pain hypersensitivity in rats, and extracellular AOPPs accumulation triggered Nox4-dependent ROS production, which activated JNK, and induced DRG neurons apoptosis by activating caspase 3 and PARP-1.
- Published
- 2017
13. Advanced oxidative protein products induced human keratinocyte apoptosis through the NOX-MAPK pathway
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Ruoting Ding, Wenlin Yu, Yanhong Wu, Baihui Sun, Qin Li, and Bulin Wang
- Subjects
0301 basic medicine ,MAPK/ERK pathway ,Keratinocytes ,Cancer Research ,Poly ADP ribose polymerase ,p38 mitogen-activated protein kinases ,Clinical Biochemistry ,Pharmaceutical Science ,Caspase 3 ,Apoptosis ,Biology ,p38 Mitogen-Activated Protein Kinases ,Cell Line ,03 medical and health sciences ,0302 clinical medicine ,Humans ,Protein kinase A ,Extracellular Signal-Regulated MAP Kinases ,Pharmacology ,Kinase ,Biochemistry (medical) ,Cell Biology ,Molecular biology ,Cell biology ,Mitochondria ,HaCaT ,030104 developmental biology ,Advanced Oxidation Protein Products ,NADPH Oxidase 4 ,030220 oncology & carcinogenesis ,Poly(ADP-ribose) Polymerases ,Reactive Oxygen Species ,Intracellular ,Signal Transduction - Abstract
Impaired wound healing is a major diabetes-related complication. Keratinocytes play an important role in wound healing. Multiple factors have been proposed that can induce dysfunction in keratinocytes. The focus of present research is at a more specific molecular level. We investigated the role of advanced oxidative protein products (AOPPs) in inducing human immortalized keratinocyte (HaCaT) cell apoptosis and the cellular mechanism underlying the proapoptotic effect of AOPPs. HaCaT cells were treated with increasing concentrations of AOPP-human serum albumin or for increasing time durations. The cell viability was measured using the thiazolyl blue tetrazolium bromide method, and flow cytometry was used to assess the rate of cell apoptosis. A loss of mitochondrial membrane potential (MMP) and an increase in intracellular reactive oxygen species (ROS) were observed through a confocal laser scanning microscope system, and the level of ROS generation was determined using a microplate reader. Nicotinamide adenine dinucleotide phosphate oxidase (NOX)4, extracellular signal-regulated kinase (ERK)1/2, p38 mitogen-activated protein kinase (MAPK), and apoptosis-related downstream protein interactions were investigated using the Western blot analysis. We found that AOPPs triggered HaCaT cell apoptosis and MMP loss. After AOPP treatment, intracellular ROS generation increased in a time- and dose-dependent manner. Proapoptotic proteins, such as Bax, caspase 9/caspase 3, and poly(ADP-ribose) polymerase (PARP)-1 were activated, whereas anti-apoptotic Bcl-2 protein was downregulated. AOPPs also increased NOX4, ERK1/2, and p38 MAPK expression. Taken together, these findings suggest that extracellular AOPP accumulation triggered NOX-dependent ROS production, which activated ERK1/2 and p38 MAPK, and induced HaCaT cell apoptosis by activating caspase 3 and PARP-1.
- Published
- 2016
14. Characterization and high expression of recombinant Ustilago maydis xylanase in Pichia pastoris
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Bo Zhu, Ri-He Peng, Baihui Sun, Xiaoyan Fu, Shuang You, Lei Chen, Jin Qiu, Quan-Hong Yao, Han Hongjuan, and Chengye Yu
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Ustilago ,Cations, Divalent ,Iron ,Molecular Sequence Data ,Enzyme Activators ,Gene Expression ,Bioengineering ,Applied Microbiology and Biotechnology ,Pichia ,law.invention ,Pichia pastoris ,chemistry.chemical_compound ,law ,Catalytic Domain ,Hydrolase ,Enzyme Stability ,Glycosyl ,Amino Acid Sequence ,Phylogeny ,Manganese ,biology ,Molecular mass ,Sequence Homology, Amino Acid ,business.industry ,Chemistry ,Temperature ,Active site ,General Medicine ,Hydrogen-Ion Concentration ,biology.organism_classification ,Recombinant Proteins ,Biotechnology ,Molecular Weight ,Xylosidases ,Biochemistry ,biology.protein ,Xylanase ,Recombinant DNA ,business - Abstract
A recombinant xylanase gene (rxynUMB) from Ustilago maydis 521 was expressed in Pichia pastoris, and the enzyme was purified and characterized. Phylogenetic analysis demonstrated that rxynUMB belongs to glycosyl hydrolase family 11. The Trp84, Trp95, Glu93, and Glu189 residues are proposed to be present at the active site. The apparent molecular mass of the recombinant xylananse was approximately 24 kDa, and the optimum pH and temperature were 4.3 and 50 °C, respectively. Xylanase activity was enhanced by 166 and 115 % with Fe2+ and Mn2+, respectively. The biochemical properties of this recombinant xylanase suggest that it may be a useful candidate for a variety of commercial applications.
- Published
- 2014
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