المؤلفون: Zilong Ren, Lin Ma, Min Zhang, Xiafan Xu, Chunlan Du

المصدر: ACS Omega
ACS Omega, Vol 6, Iss 16, Pp 10859-10865 (2021)

مصطلحات موضوعية: chemistry.chemical_classification, Conformational change, Circular dichroism, biology, Chemistry, General Chemical Engineering, technology, industry, and agriculture, Substrate (chemistry), General Chemistry, macromolecular substances, Cofactor, Article, Hydrophobic effect, chemistry.chemical_compound, Enzyme, Sodium pyruvate, Lactate dehydrogenase, biology.protein, Biophysics, QD1-999

الوصف: For a better understanding on the interaction between polyethyleneimine (PEI) and proteins, spectroscopic studies including UV-vis absorption, resonance Rayleigh scattering, fluorescence, and circular dichroism were conducted to reveal the conformational change of rabbit muscle lactate dehydrogenase (rmLDH) and related to the bioactivity of the enzyme. Regardless of the electrostatic repulsion, PEI could bind on the surface of rmLDH, a basic protein, via hydrogen binding of the dense amine groups and hydrophobic interaction of methyl groups. The competitive binding by PEI led to a reduction of the binding efficiency of rmLDH toward β-nicotinamide adenine dinucleotide, the coenzyme, and sodium pyruvate, the substrate. However, the complex formation with PEI induced a less ordered conformation and an enhanced surface hydrophobicity of rmLDH, facilitating the turnover of the enzyme and generally resulting in an increased activity. PEI of higher molecular weight was more efficient to induce alteration in the conformation and catalytic activity of the enzyme.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce97445409c87cbd05630bb1c6db950bTest
http://europepmc.org/articles/PMC8153759Test

المؤلفون: Patrick Kestemont, Martine Raes, Jennifer Dorts, Marc Dieu, Frédéric Silvestre

المصدر: Journal of Proteome Research. 10(2):470-478

مصطلحات موضوعية: Gill, Fish Proteins, Gills, Male, Proteomics, Proteome, Biochemistry, chemistry.chemical_compound, Tandem Mass Spectrometry, Lactate dehydrogenase, Cytochrome c oxidase, Citrate synthase, Animals, Gobio, Electrophoresis, Gel, Two-Dimensional, chemistry.chemical_classification, biology, Dose-Response Relationship, Drug, Fishes, General Chemistry, Environmental exposure, Environmental Exposure, biology.organism_classification, Molecular biology, Enzyme, chemistry, Liver, Toxicity, biology.protein, Female, Sentinel Surveillance, Metabolic Networks and Pathways, Cadmium, Chromatography, Liquid

الوصف: The present study aimed at evaluating the toxicity of short-term cadmium (Cd) exposure in the European bullhead Cottus gobio, a candidate sentinel species. Several enzymatic activity assays (citrate synthase, cytochrome c oxidase, and lactate dehydrogenase) were carried out in liver and gills of fish exposed to 0.01, 0.05, 0.25, and 1 mg Cd/L for 4 days. Exposure to high Cd concentrations significantly altered the activity of these enzymes either in liver and/or in gills. Second, 2D-DIGE technique was used to identify proteins differentially expressed in tissues of fish exposed to either 0.01 or 1 mg Cd/L. Fifty-four hepatic protein spots and 37 branchial protein spots displayed significant changes in abundance in response to Cd exposure. A total of 26 and 12 different proteins were identified using nano LC-MS/MS in liver and gills, respectively. The identified differentially expressed proteins can be categorized into diverse functional classes, related to metabolic process, general stress response, protein fate, and cell structure for instance. This work provides new insights into the biochemical and molecular events in Cd-induced toxicity in fish and suggests that further studies on the identified proteins could provide crucial information to better understand the mechanisms of Cd toxicity in fish.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1061818ad3a1fe146665fee2bb3ca0f1Test
https://researchportal.unamur.be/en/publications/69837c68-297d-4c70-bfe8-c4feac2ca2e2Test

المؤلفون: Khuloud T. Al-Jamal, Alberto Bianco, Sophie Lanone, Maurizio Prato, Cyrill Bussy, Jorge Boczkowski, Kostas Kostarelos

المساهمون: Immunopathologie et chimie thérapeutique (ICT), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Bussy, Cyrill, Al Jamal, Khuloud T., Boczkowski, Jorge, Lanone, Sophie, Prato, Maurizio, Bianco, Alberto, Kostarelos, Kostas

المصدر: ACS Nano
ACS Nano, American Chemical Society, 2015, 9 (8), pp.7815-7830. ⟨10.1021/acsnano.5b02358⟩

مصطلحات موضوعية: implant, Cell, General Physics and Astronomy, Gene Expression, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, Engineering (all), Drug Delivery Systems, Cytotoxic T cell, General Materials Science, Cytotoxicity, nanomaterials, CD11b Antigen, Microglia, biology, General Engineering, brain, carbon nanotubes, nanotoxicology, Materials Science (all), Physics and Astronomy (all), chemistry, toxicity, Cell biology, Frontal Lobe, secretion, medicine.anatomical_structure, Integrin alpha M, Organ Specificity, nanomaterial, Intracellular, Chimie/Chimie thérapeutique, drug effects, metabolism, Materials science, Cell Survival, Central nervous system, Primary Cell Culture, Nanotechnology, Nitric Oxide, cytology, Fetus, Glial Fibrillary Acidic Protein, medicine, Animals, carbon nanotube, Brain Chemistry, L-Lactate Dehydrogenase, Nanotubes, Carbon, genetics, Coculture Techniques, Corpus Striatum, CD11c Antigen, Rats, nervous system, Nanotoxicology, Astrocytes, Culture Media, Conditioned, biology.protein, pharmacology, Biomarkers

الوصف: Surface tunability and their ability to translocate plasma membranes make chemically functionalized carbon nanotubes (f-CNTs) promising intracellular delivery systems for therapeutic or diagnostic purposes in the central nervous system (CNS). The present study aimed to determine the biological impact of different types of multiwalled CNTs (MWNTs) on primary neuronal and glial cell populations isolated from fetal rat frontal cortex (FCO) and striatum (ST). Neurons from both brain regions were generally not affected by exposure to MWNTs as determined by a modified LDH assay. In contrast, the viability of mixed glia was reduced in ST-derived mixed glial cultures, but not in FCO-derived ones. Cytotoxicity was independent of MWNT type or dose, suggesting an inherent sensitivity to CNTs. Characterization of the cell populations in mixed glial cultures prior to nanotube exposure showed higher number of CD11b/c positive cells in the ST-derived mixed glial cultures. After exposure to MWNTs, CNT were uptaken more effectively by CD11b/c positive cells (microglia), compared to GFAP positive cells (astrocytes). When exposed to conditioned media from microglia enriched cultures exposed to MWNTs, ST-derived glial cultures secreted more NO than FCO-derived cells. These results suggested that the more significant cytotoxic response obtained from ST-derived mixed glia cultures was related to the higher number of microglial cells in this brain region. Our findings emphasize the role that resident macrophages of the CNS play in response to nanomaterials and the need to thoroughly investigate the brain region-specific effects toward designing implantable devices or delivery systems to the CNS. journal article research support, non-u.s. gov't 2015 Aug 25 2015 06 26 imported

وصف الملف: STAMPA

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1761bb582a10a756e89028f4adad6d91Test

المؤلفون: M. Isabel Escribano, Oscar Goñi, Irene Romero, Carmen Merodio, Carlos Fernandez-Caballero, M. Teresa Sanchez-Ballesta

المصدر: Digital.CSIC. Repositorio Institucional del CSIC
instname

مصطلحات موضوعية: Antifungal, medicine.drug_class, Molecular Sequence Data, Class I chitinase, Gene Expression, Berry, Biology, Cryoprotective Agents, Freezing, Gene expression, Botany, Escherichia coli, medicine, Vitis, Amino Acid Sequence, Vitis vinifera, Plant Proteins, L-Lactate Dehydrogenase, Chitinases, Table grape, General Chemistry, Recombinant Proteins, Fungicides, Industrial, Fruit, Chitinase, biology.protein, sense organs, General Agricultural and Biological Sciences, Sequence Alignment

الوصف: Gene expression of a class I chitinase (Vcchit1b) in the skin of table grapes was analyzed as a molecular marker for changes induced at low temperature and also to study the effect of high CO2 levels modulating transcript levels at 0 °C. An active recombinant VcCHIT1b was overexpressed in Escherichia coli, and as the protein was produced as insoluble inclusion bodies, it was solubilized and refolded. The purified recombinant chitinase showed an optimum pH of 6.0 and a temperature of 50 °C, retaining activity at 0 and -10 °C. Purified chitinase exerted in vitro antifungal activity against Botrytis cinerea. Furthermore, recombinant chitinase was able to cryoprotect lactate dehydrogenase against freeze/thaw inactivation. However, the recombinant VcCHIT1b did not show any antifreeze activity when the thermal hysteresis activity was measured using differential scanning calorimetry. © 2009 American Chemical Society.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::463463300d239747c50b8be011456292Test
http://hdl.handle.net/10261/77736Test