We are analyzing https://link.springer.com/article/10.1186/s13046-021-01977-9.

Title:
A novel lncRNA ARST represses glioma progression by inhibiting ALDOA-mediated actin cytoskeleton integrity | Journal of Experimental & Clinical Cancer Research
Description:
Background Glioma is one of the most aggressive malignant brain tumors that is characterized with inevitably infiltrative growth and poor prognosis. ARST is a novel lncRNA whose expression level is significantly decreased in the patients with glioblastoma multiforme. However, the exact mechanisms of ARST in gliomagenesis are largely unknown. Methods The expressions of ARST in the glioma samples and cell lines were analyzed by qRT-PCR. FISH was utilized to detect the distribution of ARST in the glioma cells. CCK-8, EdU and flow cytometry were used to examine cellular viability, proliferation and apoptosis. Transwell and wound-healing assays were performed to determine the migratory and invasive abilities of the cells. Intracranial tumorigenesis models were established to explore the roles of ARST in vivo. RNA pulldown assay was used to examine proteins that bound to ARST. The activities of key enzymes in the glycolysis and production of lactate acid were measured by colorimetry. In addition, RIP, Co-IP, western blot and immunofluorescence were used to investigate the interaction and regulation between ARST, F-actin, ALDOA and cofilin. Results In this study, we reported that ARST was downregulated in the gliomas. Overexpression of ARST in the glioma cells significantly suppressed various cellular vital abilities such as cell growth, proliferation, migration and invasion. The tumorigenic capacity of these cells in vivo was reduced as well. We further demonstrated that the tumor suppressive effects of ARST could be mediated by a direct binding to a glycolytic enzyme aldolase A (ALDOA), which together with cofilin, keeping the polymerization and depolymerization of actin filaments in an orderly dynamic equilibrium. Upregulation of ARST interrupted the interaction between ALDOA and actin cytoskeleton, which led to a rapid cofilin-dependent loss of F-actin stress fibers. Conclusions Taken together, it is concluded that ARST performs its function via a non-metabolic pathway associated with ALDOA, which otherwise modifies the morphology and invasive properties of the glioma cells. This has added new perspective to its role in tumorigenesis, thus providing potential target for glioma diagnosis, therapy, and prognosis.
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Keywords {🔍}

arst, aldoa, cells, fig, glioma, actin, cofilin, factin, assay, cell, article, performed, rna, binding, tissues, gliomas, china, database, results, pubmed, proteins, umg, google, scholar, expression, interaction, control, cytoskeleton, wang, significantly, shandong, usa, cas, data, lncrna, human, supplementary, cancer, detect, migration, protein, transfected, analysis, normal, pulldown, scale, experiments, bar, proliferation, depolymerization,

Topics {✒️}

ddx3/yy1/mmp1/pi3k-akt axis targeting mir-8855p-cdk2 pathway wnt/β-catenin signaling pathway suffix e-signal represented uniprotkb/swiss-prot human database suffix t-signal represented wnt/beta-catenin signalling biotin-labeled rna pulldown central nervous system 6-diami-dino-2-phenylindole bca annexin v-fitc article download pdf frequent t-cell targets rhoa/rock1/limk/cofilin pathway large-scale microarray profiling quantitative real-time pcr related subjects human idh-mutant glioma nano-lc-ms/ms extended cap-gly domains cofilin-related cytoskeleton dynamics releasing g-actin monomers 100 μl serum-free medium rapid cofilin-dependent loss f-actin-aldolase rafts anti-igm magnetic beads cell counting kit-8 rhoa/rock1/limk/cofilin natural science foundation f-actin stress fibers full access experimental cell lines rna-binding protein hnrnpk mass spectrometry-based assay privacy choices/manage cookies full size image flow cytometry assay 5 μg ip-grade antibodies inhibiting cell proliferation adjacent brain tissue actin fiber integrity cell motil cytoskeleton wound-healing assay showed clin cancer res tumor suppressor protein-coding genes omega bio-tek human glioblastoma multiforme marie france carlier solid orthotopic transplantation

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         headline:A novel lncRNA ARST represses glioma progression by inhibiting ALDOA-mediated actin cytoskeleton integrity
         description:Glioma is one of the most aggressive malignant brain tumors that is characterized with inevitably infiltrative growth and poor prognosis. ARST is a novel lncRNA whose expression level is significantly decreased in the patients with glioblastoma multiforme. However, the exact mechanisms of ARST in gliomagenesis are largely unknown. The expressions of ARST in the glioma samples and cell lines were analyzed by qRT-PCR. FISH was utilized to detect the distribution of ARST in the glioma cells. CCK-8, EdU and flow cytometry were used to examine cellular viability, proliferation and apoptosis. Transwell and wound-healing assays were performed to determine the migratory and invasive abilities of the cells. Intracranial tumorigenesis models were established to explore the roles of ARST in vivo. RNA pulldown assay was used to examine proteins that bound to ARST. The activities of key enzymes in the glycolysis and production of lactate acid were measured by colorimetry. In addition, RIP, Co-IP, western blot and immunofluorescence were used to investigate the interaction and regulation between ARST, F-actin, ALDOA and cofilin. In this study, we reported that ARST was downregulated in the gliomas. Overexpression of ARST in the glioma cells significantly suppressed various cellular vital abilities such as cell growth, proliferation, migration and invasion. The tumorigenic capacity of these cells in vivo was reduced as well. We further demonstrated that the tumor suppressive effects of ARST could be mediated by a direct binding to a glycolytic enzyme aldolase A (ALDOA), which together with cofilin, keeping the polymerization and depolymerization of actin filaments in an orderly dynamic equilibrium. Upregulation of ARST interrupted the interaction between ALDOA and actin cytoskeleton, which led to a rapid cofilin-dependent loss of F-actin stress fibers. Taken together, it is concluded that ARST performs its function via a non-metabolic pathway associated with ALDOA, which otherwise modifies the morphology and invasive properties of the glioma cells. This has added new perspective to its role in tumorigenesis, thus providing potential target for glioma diagnosis, therapy, and prognosis.
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      headline:A novel lncRNA ARST represses glioma progression by inhibiting ALDOA-mediated actin cytoskeleton integrity
      description:Glioma is one of the most aggressive malignant brain tumors that is characterized with inevitably infiltrative growth and poor prognosis. ARST is a novel lncRNA whose expression level is significantly decreased in the patients with glioblastoma multiforme. However, the exact mechanisms of ARST in gliomagenesis are largely unknown. The expressions of ARST in the glioma samples and cell lines were analyzed by qRT-PCR. FISH was utilized to detect the distribution of ARST in the glioma cells. CCK-8, EdU and flow cytometry were used to examine cellular viability, proliferation and apoptosis. Transwell and wound-healing assays were performed to determine the migratory and invasive abilities of the cells. Intracranial tumorigenesis models were established to explore the roles of ARST in vivo. RNA pulldown assay was used to examine proteins that bound to ARST. The activities of key enzymes in the glycolysis and production of lactate acid were measured by colorimetry. In addition, RIP, Co-IP, western blot and immunofluorescence were used to investigate the interaction and regulation between ARST, F-actin, ALDOA and cofilin. In this study, we reported that ARST was downregulated in the gliomas. Overexpression of ARST in the glioma cells significantly suppressed various cellular vital abilities such as cell growth, proliferation, migration and invasion. The tumorigenic capacity of these cells in vivo was reduced as well. We further demonstrated that the tumor suppressive effects of ARST could be mediated by a direct binding to a glycolytic enzyme aldolase A (ALDOA), which together with cofilin, keeping the polymerization and depolymerization of actin filaments in an orderly dynamic equilibrium. Upregulation of ARST interrupted the interaction between ALDOA and actin cytoskeleton, which led to a rapid cofilin-dependent loss of F-actin stress fibers. Taken together, it is concluded that ARST performs its function via a non-metabolic pathway associated with ALDOA, which otherwise modifies the morphology and invasive properties of the glioma cells. This has added new perspective to its role in tumorigenesis, thus providing potential target for glioma diagnosis, therapy, and prognosis.
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         Glioma
         ARST
         ALDOA
         Actin
         Cytoskeleton
         Cancer Research
         Immunology
         Apoptosis
         Oncology
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            name:Shandong University
            address:
               name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
               type:PostalAddress
            type:Organization
      name:Yanbang Wei
      affiliation:
            name:Shandong University
            address:
               name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
               type:PostalAddress
            type:Organization
      name:Yuji Guo
      affiliation:
            name:Shandong University
            address:
               name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
               type:PostalAddress
            type:Organization
      name:Qi Pang
      affiliation:
            name:Shandong University
            address:
               name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Qian Liu
      affiliation:
            name:Shandong University
            address:
               name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Obstetrics and Gynecology, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Physiology, Shandong Medical College, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Pathology, Tai-an Municipal Hospital, Jinan, People’s Republic of China
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Neurosurgery, Shandong Provincial Hospital, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China
      name:Department of Histology and Embryology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, People’s Republic of China

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