3 results on '"Hureshitanmu Kuerban"'
Search Results
2. VDAC1 Mediated Anticancer Activity of Gallic Acid in Human Lung Adenocarcinoma A549 Cells
- Author
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Aikebaier Maimaiti, Hureshitanmu Kuerban, Amier Aili, and Xuejun Li
- Subjects
0301 basic medicine ,Cancer Research ,Lung Neoplasms ,Cell Survival ,Cell ,Adenocarcinoma of Lung ,Antineoplastic Agents ,Structure-Activity Relationship ,03 medical and health sciences ,Western blot ,Gallic Acid ,Tumor Cells, Cultured ,medicine ,Humans ,Viability assay ,Protein kinase B ,Cell Proliferation ,Pharmacology ,A549 cell ,Dose-Response Relationship, Drug ,Molecular Structure ,medicine.diagnostic_test ,Chemistry ,Voltage-Dependent Anion Channel 1 ,Transfection ,Molecular biology ,030104 developmental biology ,medicine.anatomical_structure ,A549 Cells ,Apoptosis ,Molecular Medicine ,Drug Screening Assays, Antitumor ,VDAC1 - Abstract
Aims: Gallic acid (GA) is generally distributed in a variety of plants and foods, and possesses cell growth-inhibiting activities in cancer cell lines. In the present study, the impact of GA on cell viability, apoptosis induction and possible molecular mechanisms in cultured A549 lung carcinoma cells was investigated. Methods: In vitro experiments showed that treating A549 cells with various concentrations of GA inhibited cell viability and induced apoptosis in a dose-dependent manner. In order to understand the mechanism by which GA inhibits cell viability, comparative proteomic analysis was applied. The changed proteins were identified by Western blot and siRNA methods. Results: Two-dimensional electrophoresis revealed changes that occurred to the cells when treated with or without GA. Four up-regulated protein spots were clearly identified as malate dehydrogenase (MDH), voltagedependent, anion-selective channel protein 1(VDAC1), calreticulin (CRT) and brain acid soluble protein 1(BASP1). VDAC1 in A549 cells was reconfirmed by western blot. Transfection with VDAC1 siRNA significantly increased cell viability after the treatment of GA. Further investigation showed that GA down regulated PI3K/Akt signaling pathways. These data strongly suggest that up-regulation of VDAC1 by GA may play an important role in GA-induced, inhibitory effects on A549 cell viability.
- Published
- 2018
3. New Insights into the Coupling between Microtubule Depolymerization and ATP Hydrolysis by Kinesin-13 Protein Kif2C
- Author
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Benoît Gigant, Fuming Zhang, Marcel Knossow, Ting Shen, Yuncong Lv, Chunguang Wang, Hureshitanmu Kuerban, Raphael Guerois, Weiyi Wang, Biochimie Structurale des Microtubules, des Kinésines et de leurs Cargos ( MIKICA ), Département Biochimie, Biophysique et Biologie Structurale ( B3S ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Institute of Protein Research, Tong Ji University, Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Assemblage moléculaire et intégrité du génome ( AMIG ), Biochimie Structurale des Microtubules, des Kinésines et de leurs Cargos (MIKICA), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Assemblage moléculaire et intégrité du génome (AMIG)
- Subjects
Conformational change ,Protein Conformation ,[SDV]Life Sciences [q-bio] ,Kinesin 13 ,Kinesins ,macromolecular substances ,Biology ,Crystallography, X-Ray ,Microtubules ,Biochemistry ,kinesin ,Tubulin binding ,Structure-Activity Relationship ,Adenosine Triphosphate ,Protein structure ,conformational change ,Tubulin ,ATP hydrolysis ,Microtubule ,Serine ,Humans ,ATPase ,Molecular Biology ,Adenosine Triphosphatases ,Binding Sites ,[ SDV ] Life Sciences [q-bio] ,Hydrolysis ,Valine ,Cell Biology ,Protein Structure, Tertiary ,molecular motor ,Amino Acid Substitution ,Enzymology ,biology.protein ,Biophysics ,Kinesin ,Protein Binding ,microtubule - Abstract
International audience; Kinesin-13 proteins depolymerize microtubules in an ATP hydrolysis-dependent manner. The coupling between these two activities remains unclear. Here, we first studied the role of the kinesin-13 subfamily-specific loop 2 and of the KVD motif at the tip of this loop. Shortening the loop, the lysine/glutamate interchange and the additional Val to Ser substitution all led to Kif2C mutants with decreased microtubule-stimulated ATPase and impaired depolymerization capability. We rationalized these results based on a structural model of the Kif2C-ATP-tubulin complex derived from the recently determined structures of kinesin-1 bound to tubulin. In this model, upon microtubule binding Kif2C undergoes a conformational change governed in part by the interaction of the KVD motif with the tubulin interdimer interface. Second, we mutated to an alanine the conserved glutamate residue of the switch 2 nucleotide binding motif. This mutation blocks motile kinesins in a post-conformational change state and inhibits ATP hydrolysis. This Kif2C mutant still depolymerized microtubules and yielded complexes of one Kif2C with two tubulin heterodimers. These results demonstrate that the structural change of Kif2C-ATP upon binding to microtubule ends is sufficient for tubulin release, whereas ATP hydrolysis is not required. Overall, our data suggest that the conformation reached by kinesin-13s upon tubulin binding is similar to that of tubulin-bound, ATP-bound, motile kinesins but that this conformation is adapted to microtubule depolymerization.
- Published
- 2015
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