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5. An environmentally benign and selective electrochemical oxidation of sulfides and thiols in a continuous-flow microreactor

Author

Laudadio, G., Straathof, N.J.W., Lanting, M.D., Knoops, B., Hessel, V., Noël, T., Laudadio, G., Straathof, N.J.W., Lanting, M.D., Knoops, B., Hessel, V., and Noël, T.

Abstract

A practical and environmentally benign electrochemical oxidation of thioethers and thiols in a commercially-available continuous-flow microreactor is presented. Water is used as the source of oxygen to enable the oxidation process. The oxidation reaction utilizes the same reagents in all scenarios and the selectivity is solely governed by the applied potential. The procedure exhibits a broad scope and good functional group compatibility providing access to various sulfoxides (15 examples), sulfones (15 examples) and disulfides (6 examples). The use of continuous flow allows the optimal reaction parameters (e.g. residence time, applied voltage) to be rapidly assessed, to avoid mass- and heat-transfer limitations and to scale the electrochemistry.

Published
2017

7. The crystal structure of the C45S mutant of annelid Arenicola marina peroxiredoxin 6 supports its assignment to the mechanistically typical 2-Cys subfamily without any formation of toroid-shaped decamers

Author

Smeets, A., Loumaye, E., Clippe, A., Rees, J.-F., Knoops, B., and Declercq, J.-P.

Subjects
Arenicola marina [Lugworm]
Abstract

The peroxiredoxins (PRDXs) define a superfamily of thiol-dependent peroxidases able to reduce hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. Besides their cytoprotective antioxidant function, PRDXs have been implicated in redox signaling and chaperone activity, the latter depending on the formation of decameric high-molecular-weight structures. PRDXs have been mechanistically divided into three major subfamilies, namely typical 2-Cys, atypical 2-Cys, and 1-Cys PRDXs, based on the number and position of cysteines involved in the catalysis. We report the structure of the C45S mutant of annelid worm Arenicola marina PRDX6 in three different crystal forms determined at 1.6, 2.0, and 2.4 Å resolution. Although A. marina PRDX6 was cloned during the search of annelid homologs of mammalian 1-Cys PRDX6s, the crystal structures support its assignment to the mechanistically typical 2-Cys PRDX subfamily. The protein is composed of two distinct domains: a C-terminal domain and an N-terminal domain exhibiting a thioredoxin fold. The subunits are associated in dimers compatible with the formation of intersubunit disulfide bonds between the peroxidatic and the resolving cysteine residues in the wild-type enzyme. The packing of two crystal forms is very similar, with pairs of dimers associated as tetramers. The toroid-shaped decamers formed by dimer association and observed in most typical 2-Cys PRDXs is not present. Thus, A. marina PRDX6 presents structural features of typical 2-Cys PRDXs without any formation of toroid-shaped decamers, suggesting that it should function more like a cytoprotective antioxidant enzyme or a modulator of peroxide-dependent cell signaling rather than a molecular chaperone.

Published
2008

8. Etudes du dysfonctionnement mitochondrial dans le maintien de la biogenèse mitochondriale et de la réponse à l'apoptose induite

Author

FUNDP - 2754 - Unité de Recherche en Biologie Cellulaire, Knoops, B., Wiesner, RJ., De Bolle, Xavier, Renard, Patricia, Jadot, Michel, Arnould, Thierry, MERCY, Ludovic, FUNDP - 2754 - Unité de Recherche en Biologie Cellulaire, Knoops, B., Wiesner, RJ., De Bolle, Xavier, Renard, Patricia, Jadot, Michel, Arnould, Thierry, and MERCY, Ludovic

Abstract

La mitochondrie est un organite dont les fonctions dépassent largement le rôle bioénergétique. De ce fait, il apparaît de plus en plus clairement qu'un grand nombre de pathologies sont liées à un dysfonctionnement mitochondrial. Au cours de ces dernières années l'existence d'une communication moléculaire rétrograde entre la mitochondrie non fonctionnelle et le noyau a été mise en évidence dans les cellules eucaryotes de mammifères. Les voies de signalisation moléculaire menant à l'expression différentielle de gènes nucléaires en réponse à un dysfonctionnement mitochondrial sont néanmoins encore peu connues. Dans ce domaine, l'utilisation de lignées cellulaire totalement (r0) ou partiellement (r-) déplétées en ADN mitochondrial (ADNmt) s'est révélée essentielle dans l'étude de la réponse cellulaire induite par un dysfonctionnement mitochondrial. L'objectif de ce travail était de mieux comprendre les mécanismes moléculaires impliqués dans la réponse cellulaire à un dysfonctionnement mitochondrial 1) en recherchant comment les cellules déplétées en ADNmt maintiennent un potentiel de membrane mitochondrial en étudiant les mécanismes impliqués dans le maintien de la biogenèse mitochondriale et 3) en caractérisant la sensibilité des cellules déplétées en ADNmt à l'apoptose. Au cours de la première partie de ce travail, nous avons mis en évidence le rôle de la protéine mtCLIC dans le maintien du Dym des cellules déplétées en ADNmt. Nous avons ainsi démontré que le gène codant cette protéine est surexprimé dans les cellules présentant un dysfonctionnement mitochondrial, et que l'activité de canal à chlore pouvait rendre compte du maintien du Dym dans ces cellules. Dans la deuxième partie de ce travail, nous avons caractérisé et comparé les populations mitochondriales des cellules parentales et déplétées en ADNmt (143B r0, ostéosarcome humain). L'activité de certains facteurs de transcription décrits pour jouer un rôle dans le processus de biogenèse mitochondriale a été rech, Mitochondria are involved in numerous cell processes, such as ATP production, calcium homeostasis, fatty acid metabolism, heme synthesis, urea cycle, redox cell status, autophagy and apoptosis. Impairment of its bioenergetic activity is thus obviously associated with numerous pathologies. However, while various origins and symptoms have been described for mitochondrial diseases over the past 10 years, only very few retrograde signalling pathways (that could be defined as communication between impaired mitochondria and nucleus) have been identified. In addition, little is still known about the molecular mechanisms leading to differential gene expression in response to chronic or acute mitochondrial dysfunction. In that research field, the generation of cells totally (r0) or partially (r-) depleted in mtDNA has been very useful to study the response of cells to a chronic energetic stress. The major aim of this work was to get a better understanding of the molecular mechanisms involved in the retrograde communication between impaired mitochondria and the nucleus that participate to the maintenance of 1) the mitochondrial membrane potential (Dym), 2) the mitochondrial biogenesis and 3) the apoptotic response to staurosporine, an alkaloïd that inhibits numerous kinases. In the first part of this work, we highlighted the role of the protein mtCLIC/CLIC4 in the maintenance of the Dym in mtDNA-depleted cells. Using a "mRNA RT-PCR differential display" approach, we first identified that the gene was over-expressed in mtDNA-depleted cells. We also show that modifications of its abundance (over expresion and silencing by siRNA) were able to modify the Dym. Finally, we evidenced that mtCLIC allows the importation of chlorine into mitochondria of r-L929 (murine fibrosarcoma cells). In the second part of this work, we characterized and compared mitochondrial populations between 143B (osteosarcoma cell line) and 143B r0 cells. We monitored the activity status of several key transc, (DOCSC03)--FUNDP, 2008

Published
2008

19. Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family.

Author

Knoops, B, Clippe, A, Bogard, C, Arsalane, K, Wattiez, R, Hermans, C, Duconseille, E, Falmagne, P, and Bernard, A

Abstract

Using two-dimensional electrophoresis, we have recently identified in human bronchoalveolar lavage fluid a novel protein, termed B166, with a molecular mass of 17 kDa. Here, we report the cloning of human and rat cDNAs encoding B166, which has been renamed AOEB166 for antioxidant enzyme B166. Indeed, the deduced amino acid sequence reveals that AOEB166 represents a new mammalian subfamily of AhpC/TSA peroxiredoxin antioxidant enzymes. Human AOEB166 shares 63% similarity with Escherichia coli AhpC22 alkyl hydroperoxide reductase and 66% similarity with a recently identified Saccharomyces cerevisiae alkyl hydroperoxide reductase/thioredoxin peroxidase. Moreover, recombinant AOEB166 expressed in E. coli exhibits a peroxidase activity, and an antioxidant activity comparable with that of catalase was demonstrated with the glutamine synthetase protection assay against dithiothreitol/Fe3+/O(2) oxidation. The analysis of AOEB166 mRNA distribution in 30 different human tissues and in 10 cell lines shows that the gene is widely expressed in the body. Of interest, the analysis of N- and C-terminal domains of both human and rat AOEB166 reveals amino acid sequences presenting features of mitochondrial and peroxisomal targeting sequences. Furthermore, human AOEB166 expressed as a fusion protein with GFP in HepG2 cell line is sorted to these organelles. Finally, acute inflammation induced in rat lung by lipopolysaccharide is associated with an increase of AOEB166 mRNA levels in lung, suggesting a protective role for AOEB166 in oxidative and inflammatory processes.

Published
1999

28. Differential toxicity of ganciclovir for rat neurons and astrocytes in primary culture following adenovirus-mediated transfer of the HSVtk gene

Author

Maron, A., Havaux, N., Leroux, A., Knoops, B., Perricaudet, M., and Octave, J.N.

Subjects
Ganciclovir -- Health aspects -- Research, Gene therapy -- Research -- Health aspects, Brain tumors -- Care and treatment -- Research, Health, Care and treatment, Research, Health aspects
Abstract

Maron, A.; Havaux, N.; Leroux, A.; Knoops, B.; Perricaudet, M.; Octave, J.N. 'Differential Toxicity of Ganciclovir for Rat Neurons and Astrocytes in Primary Culture Following Adenovirus-Mediated Transfer of the HSVtk [...]

Published
1997

29. Insights into metazoan evolution from alvinella pompejana cDNAs

Author

Thierry Jean-Claude, Tanguy Arnaud, Shillito Bruce, Segurens Béatrice, Rees Jean-François, Perrodou Emmanuel, Moras Dino, Mary Jean, Leize-Wagner Emmanuelle, Lallier François, Hourdez Stéphane, Knoops Bernard, Gaill Françoise, Higuet Dominique, Da Silva Corinne, Busso Didier, Brélivet Yann, Jollivet Didier, Boutet Isabelle, Gagnière Nicolas, Weissenbach Jean, Wincker Patrick, Zal Franck, Poch Olivier, and Lecompte Odile

Subjects
Biotechnology, TP248.13-248.65, Genetics, QH426-470
Abstract

Abstract Background Alvinella pompejana is a representative of Annelids, a key phylum for evo-devo studies that is still poorly studied at the sequence level. A. pompejana inhabits deep-sea hydrothermal vents and is currently known as one of the most thermotolerant Eukaryotes in marine environments, withstanding the largest known chemical and thermal ranges (from 5 to 105°C). This tube-dwelling worm forms dense colonies on the surface of hydrothermal chimneys and can withstand long periods of hypo/anoxia and long phases of exposure to hydrogen sulphides. A. pompejana specifically inhabits chimney walls of hydrothermal vents on the East Pacific Rise. To survive, Alvinella has developed numerous adaptations at the physiological and molecular levels, such as an increase in the thermostability of proteins and protein complexes. It represents an outstanding model organism for studying adaptation to harsh physicochemical conditions and for isolating stable macromolecules resistant to high temperatures. Results We have constructed four full length enriched cDNA libraries to investigate the biology and evolution of this intriguing animal. Analysis of more than 75,000 high quality reads led to the identification of 15,858 transcripts and 9,221 putative protein sequences. Our annotation reveals a good coverage of most animal pathways and networks with a prevalence of transcripts involved in oxidative stress resistance, detoxification, anti-bacterial defence, and heat shock protection. Alvinella proteins seem to show a slow evolutionary rate and a higher similarity with proteins from Vertebrates compared to proteins from Arthropods or Nematodes. Their composition shows enrichment in positively charged amino acids that might contribute to their thermostability. The gene content of Alvinella reveals that an important pool of genes previously considered to be specific to Deuterostomes were in fact already present in the last common ancestor of the Bilaterian animals, but have been secondarily lost in model invertebrates. This pool is enriched in glycoproteins that play a key role in intercellular communication, hormonal regulation and immunity. Conclusions Our study starts to unravel the gene content and sequence evolution of a deep-sea annelid, revealing key features in eukaryote adaptation to extreme environmental conditions and highlighting the proximity of Annelids and Vertebrates.

Published
2010
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31. Evidence for the spin-0 nature of the Higgs boson using ATLAS data

Author

G. Aad, E. Abat, B. Abbott, J. Abdallah, A. A. Abdelalim, A. Abdesselam, O. Abdinov, B. Abi, M. Abolins, H. Abramowicz, H. Abreu, E. Acerbi, B. S. Acharya, M. Ackers, D. L. Adams, T. N. Addy, J. Adelman, M. Aderholz, C. Adorisio, P. Adragna, T. Adye, S. Aefsky, J. A. Aguilar Saavedra, M. Aharrouche, S. P. Ahlen, F. Ahles, A. Ahmad, H. Ahmed, M. Ahsan, G. Aielli, T. Akdogan, P. F. Akesson, T. P. A. Akesson, G. Akimoto, A. V. Akimov, A. Aktas, M. S. Alam, M. A. Alam, J. Albert, S. Albrand, M. Aleksa, I. N. Aleksandrov, M. Aleppo, F. Alessandria, C. Alexa, G. Alexander, G. Alexandre, T. Alexopoulos, M. Alhroob, M. Aliev, G. Alimonti, J. Alison, M. Aliyev, P. P. Allport, S. E. Allwood Spiers, J. Almond, A. Aloisio, R. Alon, A. Alonso, J. Alonso, M. G. Alviggi, K. Amako, P. Amaral, G. Ambrosini, G. Ambrosio, C. Amelung, V. V. Ammosov, A. Amorim, G. Amoros, N. Amram, C. Anastopoulos, T. Andeen, C. F. Anders, K. J. Anderson, A. Andreazza, V. Andrei, M. L. Andrieux, X. S. Anduaga, A. Angerami, F. Anghinolfi, N. Anjos, A. Annovi, A. Antonaki, M. Antonelli, S. Antonelli, J. Antos, B. Antunovic, F. Anulli, S. Aoun, G. Arabidze, I. Aracena, Y. Arai, A. T. H. Arce, J. P. Archambault, S. Arfaoui, J. F. Arguin, T. Argyropoulos, E. Arik, M. Arik, A. J. Armbruster, K. E. Arms, S. R. Armstrong, O. Arnaez, C. Arnault, A. Artamonov, D. Arutinov, M. Asai, S. Asai, R. Asfandiyarov, S. Ask, B. Asman, D. Asner, L. Asquith, K. Assamagan, A. Astbury, A. Astvatsatourov, B. Athar, G. Atoian, B. Aubert, B. Auerbach, E. Auge, K. Augsten, M. Aurousseau, N. Austin, G. Avolio, R. Avramidou, D. Axen, C. Ay, G. Azuelos, Y. Azuma, M. A. Baak, G. Baccaglioni, C. Bacci, A. M. Bach, H. Bachacou, K. Bachas, G. Bachy, M. Backes, E. Badescu, P. Bagnaia, Y. Bai, D. C. Bailey, T. Bain, J. T. Baines, O. K. Baker, M. D. Baker, S. Baker, F. Baltasar Dos Santos Pedrosa, E. Banas, P. Banerjee, S. Banerjee, D. Banfi, A. Bangert, V. Bansal, S. P. Baranov, S. Baranov, A. Barashkou, T. Barber, E. L. Barberio, D. Barberis, M. Barbero, D. Y. Bardin, T. Barillari, M. Barisonzi, T. Barklow, N. Barlow, B. M. Barnett, R. M. Barnett, A. Baroncelli, M. Barone, A. J. Barr, F. Barreiro, J. Barreiro Guimaraes da Costa, P. Barrillon, V. Bartheld, H. Bartko, R. Bartoldus, D. Bartsch, R. L. Bates, S. Bathe, L. Batkova, J. R. Batley, A. Battaglia, M. Battistin, G. Battistoni, F. Bauer, H. S. Bawa, M. Bazalova, B. Beare, T. Beau, P. H. Beauchemin, R. Beccherle, N. Becerici, P. Bechtle, G. A. Beck, H. P. Beck, M. Beckingham, K. H. Becks, A. J. Beddall, A. Beddall, V. A. Bednyakov, C. Bee, M. Begel, S. Behar Harpaz, P. K. Behera, M. Beimforde, G. A. N. Belanger, C. Belanger Champagne, B. Belhorma, P. J. Bell, W. H. Bell, G. Bella, F. Bellina, G. Bellomo, M. Bellomo, A. Belloni, K. Belotskiy, O. Beltramello, A. Belymam, S. Ben Ami, O. Benary, D. Benchekroun, C. Benchouk, M. Bendel, B. H. Benedict, N. Benekos, Y. Benhammou, G. P. Benincasa, D. P. Benjamin, M. Benoit, J. R. Bensinger, K. Benslama, S. Bentvelsen, M. Beretta, D. Berge, E. Bergeaas Kuutmann, N. Berger, F. Berghaus, E. Berglund, J. Beringer, K. Bernardet, P. Bernat, R. Bernhard, C. Bernius, T. Berry, F. Bertinelli, S. Bertolucci, M. I. Besana, N. Besson, S. Bethke, R. M. Bianchi, M. Bianco, O. Biebel, M. Bieri, J. Biesiada, M. Biglietti, H. Bilokon, M. Binder, M. Bindi, S. Binet, A. Bingul, C. Bini, C. Biscarat, R. Bischof, U. Bitenc, K. M. Black, R. E. Blair, O. Blanch, J. B. Blanchard, G. Blanchot, C. Blocker, J. Blocki, A. Blondel, W. Blum, U. Blumenschein, C. Boaretto, G. J. Bobbink, A. Bocci, D. Bocian, R. Bock, M. Boehler, M. Boehm, J. Boek, N. Boelaert, S. Boser, J. A. Bogaerts, A. Bogouch, C. Bohm, J. Bohm, V. Boisvert, T. Bold, V. Boldea, A. Boldyrev, V. G. Bondarenko, M. Bondioli, R. Bonino, M. Boonekamp, G. Boorman, M. Boosten, C. N. Booth, P. S. L. Booth, P. Booth, J. R. A. Booth, S. Bordoni, C. Borer, K. Borer, A. Borisov, G. Borissov, I. Borjanovic, S. Borroni, K. Bos, M. Bosman, H. Boterenbrood, D. Botterill, J. Bouchami, J. Boudreau, E. V. Bouhova Thacker, C. Boulahouache, C. Bourdarios, A. Boveia, J. Boyd, B. H. Boyer, I. R. Boyko, N. I. Bozhko, I. Bozovic Jelisavcic, S. Braccini, J. Bracinik, A. Braem, E. Brambilla, P. Branchini, G. W. Brandenburg, A. Brandt, G. Brandt, O. Brandt, U. Bratzler, B. Brau, J. E. Brau, H. M. Braun, S. Bravo, B. Brelier, J. Bremer, R. Brenner, S. Bressler, D. Breton, N. D. Brett, P. G. Bright Thomas, D. Britton, F. M. Brochu, I. Brock, R. Brock, T. J. Brodbeck, E. Brodet, F. Broggi, C. Bromberg, G. Brooijmans, W. K. Brooks, G. Brown, E. Brubaker, P. A. Bruckman de Renstrom, D. Bruncko, R. Bruneliere, S. Brunet, M. Bruschi, T. Buanes, F. Bucci, J. Buchanan, N. J. Buchanan, P. Buchholz, A. G. Buckley, I. A. Budagov, B. Budick, V. Buscher, L. Bugge, D. Buira Clark, E. J. Buis, F. Bujor, O. Bulekov, M. Bunse, T. Buran, H. Burckhart, S. Burdin, T. Burgess, S. Burke, E. Busato, P. Bussey, C. P. Buszello, F. Butin, B. Butler, J. M. Butler, C. M. Buttar, J. M. Butterworth, T. Byatt, J. Caballero, S. Cabrera Urban, M. Caccia, O. Cakir, P. Calafiura, G. Calderini, P. Calfayan, R. Calkins, L. P. Caloba, R. Caloi, D. Calvet, A. Camard, P. Camarri, M. Cambiaghi, D. Cameron, J. Cammin, S. Campana, M. Campanelli, V. Canale, F. Canelli, A. Canepa, J. Cantero, L. Capasso, M. D. M. Capeans Garrido, I. Caprini, M. Caprini, M. Caprio, M. Capua, R. Caputo, C. Caramarcu, R. Cardarelli, L. Cardiel Sas, T. Carli, G. Carlino, L. Carminati, B. Caron, S. Caron, C. Carpentieri, G. D. Carrillo Montoya, S. Carron Montero, A. A. Carter, J. R. Carter, J. Carvalho, D. Casadei, M. P. Casado, M. Cascella, C. Caso, A. M. Castaneda Hernadez, E. Castaneda Miranda, V. Castillo Gimenez, N. F. Castro, F. Castrovillari, G. Cataldi, F. Cataneo, A. Catinaccio, J. R. Catmore, A. Cattai, G. Cattani, S. Caughron, D. Cauz, A. Cavallari, P. Cavalleri, D. Cavalli, M. Cavalli Sforza, V. Cavasinni, A. Cazzato, F. Ceradini, C. Cerna, A. S. Cerqueira, A. Cerri, L. Cerrito, F. Cerutti, M. Cervetto, S. A. Cetin, F. Cevenini, A. Chafaq, D. Chakraborty, K. Chan, J. D. Chapman, J. W. Chapman, E. Chareyre, D. G. Charlton, S. Charron, S. Chatterjii, V. Chavda, S. Cheatham, S. Chekanov, S. V. Chekulaev, G. A. Chelkov, H. Chen, L. Chen, S. Chen, T. Chen, X. Chen, S. Cheng, A. Cheplakov, V. F. Chepurnov, R. Cherkaoui El Moursli, V. Tcherniatine, D. Chesneanu, E. Cheu, S. L. Cheung, L. Chevalier, F. Chevallier, V. Chiarella, G. Chiefari, L. Chikovani, J. T. Childers, A. Chilingarov, G. Chiodini, V. Chizhov, G. Choudalakis, S. Chouridou, T. Christiansen, I. A. Christidi, A. Christov, D. Chromek Burckhart, M. L. Chu, J. Chudoba, G. Ciapetti, E. Cicalini, A. K. Ciftci, R. Ciftci, D. Cinca, V. Cindro, M. D. Ciobotaru, C. Ciocca, A. Ciocio, M. Cirilli, M. Citterio, A. Clark, P. J. Clark, W. Cleland, J. C. Clemens, B. Clement, C. Clement, D. Clements, R. W. Clifft, Y. Coadou, M. Cobal, A. Coccaro, J. Cochran, R. Coco, P. Coe, S. Coelli, J. Coggeshall, E. Cogneras, C. D. Cojocaru, J. Colas, B. Cole, A. P. Colijn, C. Collard, N. J. Collins, C. Collins Tooth, J. Collot, G. Colon, R. Coluccia, G. Comune, P. Conde Muino, E. Coniavitis, M. Consonni, S. Constantinescu, C. Conta, F. Conventi, J. Cook, M. Cooke, B. D. Cooper, A. M. Cooper Sarkar, N. J. Cooper Smith, K. Copic, T. Cornelissen, M. Corradi, S. Correard, F. Corriveau, A. Corso Radu, A. Cortes Gonzalez, G. Cortiana, G. Costa, M. J. Costa, D. Costanzo, T. Costin, D. Cote, R. Coura Torres, L. Courneyea, C. Couyoumtzelis, G. Cowan, C. Cowden, B. E. Cox, K. Cranmer, J. Cranshaw, M. Cristinziani, G. Crosetti, R. Crupi, S. Crepe Renaudin, C. Cuenca Almenar, T. Cuhadar Donszelmann, S. Cuneo, A. Cunha, M. Curatolo, C. J. Curtis, P. Cwetanski, Z. Czyczula, S. D'Auria, M. D'Onofrio, A. D'Orazio, A. Da Rocha Gesualdi Mello, P. V. M. Da Silva, C. Da Via, W. Dabrowski, A. Dahlhoff, T. Dai, C. Dallapiccola, S. J. Dallison, J. Dalmau, C. H. Daly, M. Dam, M. Dameri, H. O. Danielsson, R. Dankers, D. Dannheim, V. Dao, G. Darbo, G. L. Darlea, C. Daum, J. P. Dauvergne, W. Davey, T. Davidek, D. W. Davidson, N. Davidson, R. Davidson, M. Davies, A. R. Davison, I. Dawson, J. W. Dawson, R. K. Daya, K. De, R. de Asmundis, P. E. De Castro Faria Salgado, S. De Cecco, J. de Graat, N. De Groot, P. de Jong, E. De La Cruz Burelo, C. De La Taille, B. De Lotto, L. De Mora, M. De Oliveira Branco, D. De Pedis, P. de Saintignon, A. De Salvo, U. De Sanctis, A. De Santo, J. B. De Vivie De Regie, G. De Zorzi, S. Dean, H. Deberg, G. Dedes, D. V. Dedovich, P. O. Defay, J. Degenhardt, M. Dehchar, M. Deile, C. Del Papa, J. Del Peso, T. Del Prete, A. Dell'Acqua, L. Dell'Asta, M. Della Pietra, D. della Volpe, M. Delmastro, P. Delpierre, N. Delruelle, P. A. Delsart, C. Deluca, S. Demers, M. Demichev, B. Demirkoz, J. Deng, W. Deng, S. P. Denisov, C. Dennis, J. E. Derkaoui, F. Derue, P. Dervan, K. Desch, P. O. Deviveiros, A. Dewhurst, B. DeWilde, S. Dhaliwal, R. Dhullipudi, A. Di Ciaccio, L. Di Ciaccio, A. Di Domenico, A. Di Girolamo, B. Di Girolamo, S. Di Luise, A. Di Mattia, R. Di Nardo, A. Di Simone, M. A. Diaz, M. M. Diaz Gomez, F. Diblen, E. B. Diehl, H. Dietl, J. Dietrich, T. A. Dietzsch, S. Diglio, K. Dindar Yagci, D. J. Dingfelder, C. Dionisi, R. Dipanjan, P. Dita, S. Dita, F. Dittus, F. Djama, R. Djilkibaev, T. Djobava, M. A. B. do Vale, A. Do Valle Wemans, T. K. O. Doan, M. Dobbs, R. Dobinson, D. Dobos, E. Dobson, M. Dobson, J. Dodd, O. B. Dogan, C. Doglioni, T. Doherty, Y. Doi, J. Dolejsi, I. Dolenc, Z. Dolezal, B. A. Dolgoshein, T. Dohmae, E. Domingo, M. Donega, J. Donini, J. Dopke, A. Doria, A. Dos Anjos, M. Dosil, A. Dotti, M. T. Dova, J. D. Dowell, A. Doxiadis, A. T. Doyle, J. Dragic, D. Drakoulakos, Z. Drasal, J. Drees, N. Dressnandt, H. Drevermann, C. Driouichi, M. Dris, J. G. Drohan, J. Dubbert, T. Dubbs, E. Duchovni, G. Duckeck, A. Dudarev, F. Dudziak, M. Duhrssen, H. Dur, I. P. Duerdoth, L. Duflot, M. A. Dufour, M. Dunford, H. Duran Yildiz, A. Dushkin, R. 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Wildauer, M. A. Wildt, I. Wilhelm, H. G. Wilkens, E. Williams, H. H. Williams, W. Willis, S. Willocq, J. A. Wilson, M. G. Wilson, A. Wilson, I. Wingerter Seez, F. Winklmeier, M. Wittgen, E. Woehrling, M. W. Wolter, H. Wolters, B. K. Wosiek, J. Wotschack, M. J. Woudstra, K. Wraight, C. Wright, D. Wright, B. Wrona, S. L. Wu, X. Wu, J. Wuestenfeld, E. Wulf, R. Wunstorf, B. M. Wynne, L. Xaplanteris, S. Xella, S. Xie, Y. Xie, D. Xu, G. Xu, N. Xu, M. Yamada, A. Yamamoto, K. Yamamoto, S. Yamamoto, T. Yamamura, J. Yamaoka, T. Yamazaki, Y. Yamazaki, Z. Yan, H. Yang, S. Yang, U. K. Yang, Y. Yang, Z. Yang, W. M. Yao, Y. Yao, K. Yarradoddi, Y. Yasu, J. Ye, S. Ye, M. Yilmaz, R. Yoosoofmiya, K. Yorita, H. Yoshida, R. Yoshida, C. Young, S. P. Youssef, D. Yu, J. Yu, J. Yuan, L. Yuan, A. Yurkewicz, V. G. Zaets, R. Zaidan, A. M. Zaitsev, Z. Zajacova, Y.o. K. Zalite, V. Zambrano, L. Zanello, P. Zarzhitsky, A. Zaytsev, M. Zdrazil, C. Zeitnitz, M. Zeller, P. F. Zema, A. Zemla, C. Zendler, A. V. Zenin, O. Zenin, T. Zenis, Z. Zenonos, S. Zenz, D. Zerwas, G. Zevi della Porta, Z. Zhan, H. Zhang, J. Zhang, Q. Zhang, X. Zhang, L. Zhao, T. Zhao, Z. Zhao, A. Zhemchugov, S. Zheng, J. Zhong, B. Zhou, N. Zhou, Y. Zhou, C. G. Zhu, H. Zhu, Y. Zhu, X. Zhuang, V. Zhuravlov, B. Zilka, R. Zimmermann, S. Zimmermann, M. Ziolkowski, R. Zitoun, L. Zivkovic, V. V. Zmouchko, G. Zobernig, Y. Zolnierowski, A. Zsenei, M. zur Nedden, V. Zutshi, BELLAGAMBA, LORENZO, BERTIN, ANTONIO, BOSCHERINI, DAVIDE, BRUNI, ALESSIA, BRUNI, GRAZIANO, CAFORIO, DAVIDE, DE CASTRO, STEFANO, DI SIPIO, RICCARDO, FABBRI, LAURA, FRANCHINI, MATTEO, GABRIELLI, ALESSANDRO, GIACOBBE, BENEDETTO, MASSA, IGNAZIO GIACOMO, MENGARELLI, ALBERTO, MONZANI, SIMONE, PICCININI, MAURIZIO, RINALDI, LORENZO, ROMANO, MARINO, SBARRA, CARLA, SBRIZZI, ANTONIO, SEMPRINI CESARI, NICOLA, SPIGHI, ROBERTO, VALENTINETTI, SARA, VILLA, MAURO, ZOCCOLI, ANTONIO, Doğuş Üniversitesi, Fen Edebiyat Fakültesi, Fizik Bölümü, TR3959, Çetin, Serkant Ali, UAM. Departamento de Física Teórica, Aad, G., Aloisio, Alberto, Alviggi, Mariagrazia, Canale, Vincenzo, Cevenini, Francesco, Chiefari, Giovanni, DELLA VOLPE, Domenico, Merola, Leonardo, Patricelli, Sergio, Conventi, Francesco, DELLA PIETRA, Massimo, Giordano, Raffaele, Musto, Elisa, Rossi, Elvira, SANCHEZ PINEDA, ARTURO RODOLFO, Carlino, Gianpaolo, de Asmundis, Riccardo, Di Donato, Camilla, Doria, Alessandra, Iengo, Paolo, Izzo, Vincenzo, Sekhniaidze, Givi, Zurzolo, Giovanni, Al, e. t. ., Laboratoire de Physique Subatomique et de Cosmologie (LPSC), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Centre de Calcul de l'IN2P3 (CC-IN2P3), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique Corpusculaire - Clermont-Ferrand (LPC), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Centre de Physique des Particules de Marseille (CPPM), Aix Marseille Université (AMU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Purple Mountain Observatory, Laboratoire d'Annecy de Physique des Particules (LAPP), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Laboratoire de l'Accélérateur Linéaire (LAL), Centre National de la Recherche Scientifique (CNRS)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Sud - Paris 11 (UP11), ATLAS, Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Institut Polytechnique de Grenoble - Grenoble Institute of Technology-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Universidade do Minho, Współautorami artykułu są członkowie ATLAS Collaboration w liczbie 2922, G., Aad, Bianco, Michele, G., Chiodini, Gorini, Edoardo, Primavera, Margherita, Spagnolo, Stefania Antonia, Ventura, Andrea, ATLAS Collaboration (ukupan broj autora: 2923), Alexandre, Gauthier, Barone, Gaetano, Bell, Paul, Bell, William, Benhar Noccioli, Eleonora, Bilbao De Mendizabal, Javier, Bucci, Francesca, Camacho Toro, Reina, Clark, Allan Geoffrey, Doglioni, Caterina, Ferrere, Didier, Gadomski, Szymon, Gonzalez Sevilla, Sergio, Goulette, Marc, Guescini, Francesco, Iacobucci, Giuseppe, Katre, Akshay, La Rosa, Alessandro, Martin Dit Latour, Bertrand, Mermod, Philippe, Mora Herrera, Maria Clemencia Rosario, Muenstermann, Daniel, Nektarijevic, Snezana, Nikolics, Katalin, Pasztor, Arpad, Picazio, Attilio, Pohl, Martin, Rosbach, Kilian, Vallecorsa, Sofia, Wu, Xin, G. Aad, E. Abat, B. Abbott, J. Abdallah, A.A. Abdelalim, A. Abdesselam, O. Abdinov, B. Abi, M. Abolin, H. Abramowicz, H. Abreu, E. Acerbi, B.S. Acharya, M. Acker, D.L. Adam, T.N. Addy, J. Adelman, M. Aderholz, C. Adorisio, P. Adragna, T. Adye, S. Aefsky, J.A. Aguilar-Saavedra, M. Aharrouche, S.P. Ahlen, F. Ahle, A. Ahmad, H. Ahmed, M. Ahsan, G. Aielli, T. Akdogan, P.F. Akesson, T.P.A. Akesson, G. Akimoto, A.V. Akimov, A. Akta, M.S. Alam, M.A. Alam, J. Albert, S. Albrand, M. Aleksa, I.N. Aleksandrov, M. Aleppo, F. Alessandria, C. Alexa, G. Alexander, G. Alexandre, T. Alexopoulo, M. Alhroob, M. Aliev, G. Alimonti, J. Alison, M. Aliyev, P.P. Allport, S.E. Allwood-Spier, J. Almond, A. Aloisio, R. Alon, A. Alonso, J. Alonso, M.G. Alviggi, K. Amako, P. Amaral, G. Ambrosini, G. Ambrosio, C. Amelung, V.V. Ammosov, A. Amorim, G. Amoro, N. Amram, C. Anastopoulo, T. Andeen, C.F. Ander, K.J. Anderson, A. Andreazza, V. Andrei, M.-L. Andrieux, X.S. Anduaga, A. Angerami, F. Anghinolfi, N. Anjo, A. Annovi, A. Antonaki, M. Antonelli, S. Antonelli, J. Anto, B. Antunovic, F. Anulli, S. Aoun, G. Arabidze, I. Aracena, Y. Arai, A.T.H. Arce, J.P. Archambault, S. Arfaoui, J.-F. Arguin, T. Argyropoulo, E. Arik, M. Arik, A.J. Armbruster, K.E. Arm, S.R. Armstrong, O. Arnaez, C. Arnault, A. Artamonov, D. Arutinov, M. Asai, S. Asai, R. Asfandiyarov, S. Ask, B. Asman, D. Asner, L. Asquith, K. Assamagan, A. Astbury, A. Astvatsatourov, B. Athar, G. Atoian, B. Aubert, B. Auerbach, E. Auge, K. Augsten, M. Aurousseau, N. Austin, G. Avolio, R. Avramidou, D. Axen, C. Ay, G. Azuelo, Y. Azuma, M.A. Baak, G. Baccaglioni, C. Bacci, A.M. Bach, H. Bachacou, K. Bacha, G. Bachy, M. Backe, E. Badescu, P. Bagnaia, Y. Bai, D.C. Bailey, T. Bain, J.T. Baine, O.K. Baker, M.D. Baker, S. Baker, F. Baltasar Dos Santos Pedrosa, E. Bana, P. Banerjee, S. Banerjee, D. Banfi, A. Bangert, V. Bansal, S.P. Baranov, S. Baranov, A. Barashkou, T. Barber, E.L. Barberio, D. Barberi, M. Barbero, D.Y. Bardin, T. Barillari, M. Barisonzi, T. Barklow, N. Barlow, B.M. Barnett, R.M. Barnett, A. Baroncelli, M. Barone, A.J. Barr, F. Barreiro, J. Barreiro Guimaraes da Costa, P. Barrillon, V. Bartheld, H. Bartko, R. Bartoldu, D. Bartsch, R.L. Bate, S. Bathe, L. Batkova, J.R. Batley, A. Battaglia, M. Battistin, G. Battistoni, F. Bauer, H.S. Bawa, M. Bazalova, B. Beare, T. Beau, P.H. Beauchemin, R. Beccherle, N. Becerici, P. Bechtle, G.A. Beck, H.P. Beck, M. Beckingham, K.H. Beck, A.J. Beddall, A. Beddall, V.A. Bednyakov, C. Bee, M. Begel, S. Behar Harpaz, P.K. Behera, M. Beimforde, G.A.N. Belanger, C. Belanger-Champagne, B. Belhorma, P.J. Bell, W.H. Bell, G. Bella, L. Bellagamba, F. Bellina, G. Bellomo, M. Bellomo, A. Belloni, K. Belotskiy, O. Beltramello, A. Belymam, S. Ben Ami, O. Benary, D. Benchekroun, C. Benchouk, M. Bendel, B.H. Benedict, N. Beneko, Y. Benhammou, G.P. Benincasa, D.P. Benjamin, M. Benoit, J.R. Bensinger, K. Benslama, S. Bentvelsen, M. Beretta, D. Berge, E. Bergeaas Kuutmann, N. Berger, F. Berghau, E. Berglund, J. Beringer, K. Bernardet, P. Bernat, R. Bernhard, C. Berniu, T. Berry, A. Bertin, F. Bertinelli, S. Bertolucci, M.I. Besana, N. Besson, S. Bethke, R.M. Bianchi, M. Bianco, O. Biebel, M. Bieri, J. Biesiada, M. Biglietti, H. Bilokon, M. Binder, M. Bindi, S. Binet, A. Bingul, C. Bini, C. Biscarat, R. Bischof, U. Bitenc, K.M. Black, R.E. Blair, O. Blanch, J.-B. Blanchard, G. Blanchot, C. Blocker, J. Blocki, A. Blondel, W. Blum, U. Blumenschein, C. Boaretto, G.J. Bobbink, A. Bocci, D. Bocian, R. Bock, M. Boehler, M. Boehm, J. Boek, N. Boelaert, S. Boser, J.A. Bogaert, A. Bogouch, C. Bohm, J. Bohm, V. Boisvert, T. Bold, V. Boldea, A. Boldyrev, V.G. Bondarenko, M. Bondioli, R. Bonino, M. Boonekamp, G. Boorman, M. Boosten, C.N. Booth, P.S.L. Booth, P. Booth, J.R.A. Booth, S. Bordoni, C. Borer, K. Borer, A. Borisov, G. Borissov, I. Borjanovic, S. Borroni, K. Bo, D. Boscherini, M. Bosman, H. Boterenbrood, D. Botterill, J. Bouchami, J. Boudreau, E.V. Bouhova-Thacker, C. Boulahouache, C. Bourdario, A. Boveia, J. Boyd, B.H. Boyer, I.R. Boyko, N.I. Bozhko, I. Bozovic-Jelisavcic, S. Braccini, J. Bracinik, A. Braem, E. Brambilla, P. Branchini, G.W. Brandenburg, A. Brandt, G. Brandt, O. Brandt, U. Bratzler, B. Brau, J.E. Brau, H.M. Braun, S. Bravo, B. Brelier, J. Bremer, R. Brenner, S. Bressler, D. Breton, N.D. Brett, P.G. Bright-Thoma, D. Britton, F.M. Brochu, I. Brock, R. Brock, T.J. Brodbeck, E. Brodet, F. Broggi, C. Bromberg, G. Brooijman, W.K. Brook, G. Brown, E. Brubaker, P.A. Bruckman de Renstrom, D. Bruncko, R. Bruneliere, S. Brunet, A. Bruni, G. Bruni, M. Bruschi, T. Buane, F. Bucci, J. Buchanan, N.J. Buchanan, P. Buchholz, A.G. Buckley, I.A. Budagov, B. Budick, V. Buscher, L. Bugge, D. Buira-Clark, E.J. Bui, F. Bujor, O. Bulekov, M. Bunse, T. Buran, H. Burckhart, S. Burdin, T. Burge, S. Burke, E. Busato, P. Bussey, C.P. Buszello, F. Butin, B. Butler, J.M. Butler, C.M. Buttar, J.M. Butterworth, T. Byatt, J. Caballero, S. Cabrera Urban, M. Caccia, D. Caforio, O. Cakir, P. Calafiura, G. Calderini, P. Calfayan, R. Calkin, L.P. Caloba, R. Caloi, D. Calvet, A. Camard, P. Camarri, M. Cambiaghi, D. Cameron, J. Cammin, S. Campana, M. Campanelli, V. Canale, F. Canelli, A. Canepa, J. Cantero, L. Capasso, M.D.M. Capeans Garrido, I. Caprini, M. Caprini, M. Caprio, M. Capua, R. Caputo, C. Caramarcu, R. Cardarelli, L. Cardiel Sa, T. Carli, G. Carlino, L. Carminati, B. Caron, S. Caron, C. Carpentieri, G.D. Carrillo Montoya, S. Carron Montero, A.A. Carter, J.R. Carter, J. Carvalho, D. Casadei, M.P. Casado, M. Cascella, C. Caso, A.M. Castaneda Hernadez, E. Castaneda-Miranda, V. Castillo Gimenez, N.F. Castro, F. Castrovillari, G. Cataldi, F. Cataneo, A. Catinaccio, J.R. Catmore, A. Cattai, G. Cattani, S. Caughron, D. Cauz, A. Cavallari, P. Cavalleri, D. Cavalli, M. Cavalli-Sforza, V. Cavasinni, A. Cazzato, F. Ceradini, C. Cerna, A.S. Cerqueira, A. Cerri, L. Cerrito, F. Cerutti, M. Cervetto, S.A. Cetin, F. Cevenini, A. Chafaq, D. Chakraborty, K. Chan, J.D. Chapman, J.W. Chapman, E. Chareyre, D.G. Charlton, S. Charron, S. Chatterjii, V. Chavda, S. Cheatham, S. Chekanov, S.V. Chekulaev, G.A. Chelkov, H. Chen, L. Chen, S. Chen, T. Chen, X. Chen, S. Cheng, A. Cheplakov, V.F. Chepurnov, R. Cherkaoui El Moursli, V. Tcherniatine, D. Chesneanu, E. Cheu, S.L. Cheung, L. Chevalier, F. Chevallier, V. Chiarella, G. Chiefari, L. Chikovani, J.T. Childer, A. Chilingarov, G. Chiodini, V. Chizhov, G. Choudalaki, S. Chouridou, T. Christiansen, I.A. Christidi, A. Christov, D. Chromek-Burckhart, M.L. Chu, J. Chudoba, G. Ciapetti, E. Cicalini, A.K. Ciftci, R. Ciftci, D. Cinca, V. Cindro, M.D. Ciobotaru, C. Ciocca, A. Ciocio, M. Cirilli, M. Citterio, A. Clark, P.J. Clark, W. Cleland, J.C. Clemen, B. Clement, C. Clement, D. Clement, R.W. Clifft, Y. Coadou, M. Cobal, A. Coccaro, J. Cochran, R. Coco, P. Coe, S. Coelli, J. Coggeshall, E. Cognera, C.D. Cojocaru, J. Cola, B. Cole, A.P. Colijn, C. Collard, N.J. Collin, C. Collins-Tooth, J. Collot, G. Colon, R. Coluccia, G. Comune, P. Conde Muino, E. Coniaviti, M. Consonni, S. Constantinescu, C. Conta, F. Conventi, J. Cook, M. Cooke, B.D. Cooper, A.M. Cooper-Sarkar, N.J. Cooper-Smith, K. Copic, T. Cornelissen, M. Corradi, S. Correard, F. Corriveau, A. Corso-Radu, A. Cortes-Gonzalez, G. Cortiana, G. Costa, M.J. Costa, D. Costanzo, T. Costin, D. Cote, R. Coura Torre, L. Courneyea, C. Couyoumtzeli, G. Cowan, C. Cowden, B.E. Cox, K. Cranmer, J. Cranshaw, M. Cristinziani, G. Crosetti, R. Crupi, S. Crepe-Renaudin, C. Cuenca Almenar, T. Cuhadar Donszelmann, S. Cuneo, A. Cunha, M. Curatolo, C.J. Curti, P. Cwetanski, Z. Czyczula, S. D'Auria, M. D'Onofrio, A. D'Orazio, A. Da Rocha Gesualdi Mello, P.V.M. Da Silva, C. Da Via, W. Dabrowski, A. Dahlhoff, T. Dai, C. Dallapiccola, S.J. Dallison, J. Dalmau, C.H. Daly, M. Dam, M. Dameri, H.O. Danielsson, R. Danker, D. Dannheim, V. Dao, G. Darbo, G.L. Darlea, C. Daum, J.P. Dauvergne, W. Davey, T. Davidek, D.W. 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Subjects
Physics::Instrumentation and Detectors, Ciencias Físicas, Higgs boson, Parity, Spin, spin, 01 natural sciences, 7. Clean energy, High Energy Physics - Experiment, purl.org/becyt/ford/1 [https], High Energy Physics - Experiment (hep-ex), Naturvetenskap, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], QC, Physics, Large Hadron Collider, Atlas (topology), 4. Education, ATLAS experiment, Settore FIS/01 - Fisica Sperimentale, ATLAS, Quantum number, parity, ComputingMethodologies_DOCUMENTANDTEXTPROCESSING, Condensed Matter::Strongly Correlated Electrons, Física nuclear, LHC, Natural Sciences, Particle Physics - Experiment, CIENCIAS NATURALES Y EXACTAS, Particle physics, Nuclear and High Energy Physics, Ciências Naturais::Ciências Físicas, 530 Physics, Ciências Físicas [Ciências Naturais], FOS: Physical sciences, ddc:500.2, Nuclear physics, 0103 physical sciences, ddc:530, Higgsboson, High Energy Physics, 010306 general physics, Ciencias Exactas, Coupling constant, higgs boson, spin-0 nature, Science & Technology, 010308 nuclear & particles physics, High Energy Physics::Phenomenology, Física, Parity (physics), purl.org/becyt/ford/1.3 [https], ATLAS data, Astronomía, HADRON-HADRON COLLISIONS, Experimental High Energy Physics, High Energy Physics::Experiment, Lepton
Abstract

We acknowledge the support of ANPCyT, Argentina; YerPhl, Armenia; ARC, Australia; BMWF and FWF, Austria; ANAS, Azerbaijan; SSTC, Belarus; CNPq and FAPESP, Brazil; NSERC, NRC and CFI, Canada; CERN; CONICYT, Chile; CAS, MOST and NSFC, China; COLCIENCIAS, Colombia; MSMT CR, MPO CR and VSC CR, Czech Republic; DNRF, DNSRC and Lundbeck Foundation, Denmark; EPLANET, ERC and NSRF, European Union; IN2P3-CNRS, CEA-DSM/IRFU, France; GNSF, Georgia; BMBF, DFG, HGF, MPG and AvH Foundation, Germany; GSRT and NSRF, Greece; ISF, MINERVA, GIF, DIP and Benoziyo Center, Israel; INFN, Italy; MEXT and JSPS, Japan; CNRST, Morocco; FOM and NWO, Netherlands; BRF and RCN, Norway; MNiSW, Poland; GRICES and FCT, Portugal; MERYS (MECTS), Romania; MES of Russia and ROSATOM, Russian Federation; JINR; MSTD, Serbia; MSSR, Slovakia; ARRS and MIZS, Slovenia; DST/NRF, South Africa; MICINN, Spain; SRC and Wallenberg Foundation, Sweden; SER, SNSF and Cantons of Bern and Geneva, Switzerland; NSC, Taiwan; TAEK, Turkey; STFC, the Royal Society and Leverhulme Trust, United Kingdom; DOE and NSF, United States of America., Studies of the spin and parity quantum numbers of the Higgs boson are presented, based on proton-proton collision data collected by the ATLAS experiment at the LHC. The Standard Model spin-parity JP=0+ hypothesis is compared with alternative hypotheses using the Higgs boson decays H→γγ, H→ZZ*→4ℓ and H→WW*→ℓνℓν, as well as the combination of these channels. The analysed dataset corresponds to an integrated luminosity of 20.7 fb-1 collected at a centre-of-mass energy of s=8TeV. For the H→ZZ*→4ℓ decay mode the dataset corresponding to an integrated luminosity of 4.6 fb-1 collected at s=7TeV is included. The data are compatible with the Standard Model JP=0+ quantum numbers for the Higgs boson, whereas all alternative hypotheses studied in this Letter, namely some specific JP=0-, 1+, 1-, 2+ models, are excluded at confidence levels above 97.8%. This exclusion holds independently of the assumptions on the coupling strengths to the Standard Model particles and in the case of the JP=2+ model, of the relative fractions of gluon-fusion and quark-antiquark production of the spin-2 particle. The data thus provide evidence for the spin-0 nature of the Higgs boson, with positive parity being strongly preferred., ANPCyT, YerPhl, Armenia, Australian Research Council, BMWF, Austrian Science Fund (FWF), Azerbaijan National Academy of Sciences (ANAS), SSTC, Belarus, National Council for Scientific and Technological Development (CNPq), Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP), Natural Sciences and Engineering Research Council of Canada, National Research Centre (NRC), Canada Foundation for Innovation, CERN, Comision Nacional de Investigacion Cientifica y Tecnologica (CONICYT), Chinese Academy of Sciences, MOST, National Natural Science Foundation of China, Departamento Administrativo de Ciencia, Tecnologia e Innovacion Colciencias, Ministry of Education, Youth & Sports - Czech Republic, MPO CR, Czech Republic Government, DNRF, Danish Natural Science Research Council, Lundbeckfonden, EPLANET, European Research Council (ERC), NSRF, European Union (EU), Centre National de la Recherche Scientifique (CNRS), CEA-DSM/IRFU, France, GNSF, Georgia, Federal Ministry of Education & Research (BMBF), German Research Foundation (DFG), HGF, Max Planck Society, Alexander von Humboldt Foundation, Greek Ministry of Development-GSRT, NSRF, Greece, Israel Science Foundation, MINERVA, German-Israeli Foundation for Scientific Research and Development, DIP, Benoziyo Center, Israel, Istituto Nazionale di Fisica Nucleare (INFN), Ministry of Education, Culture, Sports, Science and Technology, Japan (MEXT) Japan Society for the Promotion of Science, CNRST, Morocco, FOM (The Netherlands), Netherlands Organization for Scientific Research (NWO) Netherlands Government, BRF, RCN, Norway, Ministry of Science and Higher Education, Poland, GRICES, Portuguese Foundation for Science and Technology, MERYS (MECTS), Romania, MES of Russia, Russian Federation, JINR, MSTD, Serbia, MSSR, Slovakia, Slovenian Research Agency - Slovenia, MIZS, Slovenia, DST/NRF, South Africa, Spanish Government, SRC, Wallenberg Foundation, Sweden, SER, Swiss National Science Foundation (SNSF), Cantons of Bern and Geneva, Switzerland, National Science Council of Taiwan, Ministry of Energy & Natural Resources - Turkey, Royal Society of London, Leverhulme Trust, United States Department of Energy (DOE), National Science Foundation (NSF), ICREA, Science & Technology Facilities Council (STFC) ST/M001474/1 ST/K003496/1 ST/J005460/1 ST/K003496/1 GRIDPP PP/E003699/2 ST/F007337/1 ST/H00095X/1 ST/J005568/1 ST/K001361/1 LHCb Upgrades ST/K001361/1 MINOS/MINOS+ ST/K003437/1 GRIDPP PP/E002757/1 ST/I005803/1 GRIDPP ST/K00073X/1 ST/L00335X/1 ST/K000659/1 ST/J005576/1 ST/K003658/1 ST/K501840/1 GRIDPP ST/L001004/1 ST/K00140X/1 ATLAS ST/J004928/1 ST/I005803/1 ST/J500641/1 ST/F00754X/1 ST/J004944/1 PP/E000347/1 ST/F007418/1 ST/I005811/1 ST/J004928/1 ATLAS Upgrade ST/J004936/1 ST/K001361/1 ST/M000664/1 ST/K001329/1 ATLAS ST/J005541/1 ST/L00352X/1 ST/L001209/1 ATLAS Upgrades ST/I000186/1 ST/K50208X/1 ST/L001144/1 ST/J501074/1 ST/L003325/1 ST/K001361/1 LHCb ST/K001361/1 ATLAS ST/K001337/1 ST/K001264/1 ATLAS PP/E003699/1 ST/K00140X/1 ST/M001431/1 ST/K00137X/1 ST/J004804/1 ST/K001248/1 PP/E003087/1 ST/M000761/1 ST/H001042/1 ST/H00095X/2 ATLAS ST/H001042/2 PP/E000487/1 ST/H001069/2 ST/K003658/1 GRIDPP ST/K003437/1 ST/I006080/1 ST/I003142/1 ST/K501840/1 ST/K001388/1 ST/I505756/1 ST/H001093/1 ST/I003517/1 ST/K001337/1 ATLAS ST/K000713/1 GRIDPP ST/H001093/2 ST/J002798/1 ST/L000970/1 ST/G502320/1 ST/K000195/1 ST/L000970/1 ATLAS Upgrade ST/K001361/1 ATLAS Upgrades

Published
2013
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32. Incretin-induced changes in the transcriptome of skeletal muscles of fa/fa Zucker rat (ZFR) with obesity, without diabetes.

Author

Colin IM, Knoops B, and Gérard AC

Subjects
AMP-Activated Protein Kinases metabolism, Animals, Exenatide pharmacology, Insulin metabolism, Muscle, Skeletal metabolism, Obesity metabolism, Rats, Rats, Zucker, Transcriptome genetics, Diabetes Mellitus, Type 2 metabolism, Incretins metabolism, Incretins pharmacology
Abstract

Introduction: Glucagon-like peptide-1 receptor agonists (GLP-1ra) are increasingly used in treating type 2 diabetes and obesity. Exendin-4 (Ex-4), a long acting GLP-1ra, was previously reported to decrease oxidative stress in hepatocytes, adipocytes and skeletal muscle cells in obese nondiabetic fa/fa Zucker rats (ZFR), thereby improving insulin resistance., Aim: We aimed first to identify Ex-4-induced changes in the transcriptome of skeletal muscle cells in ZFR., Results: Ontology analysis of differentially expressed genes (DEGs) in ZFR versus lean animals (LR) showed that the extracellular matrix (ECM) is the first most affected cellular compartment, followed by myofibrils and endoplasmic reticulum (ER). Interestingly, among 15 genes regulated in ZFR versus LR, 14 of them were inversely regulated by Ex-4, as further confirmed by RT-qPCR. Picro-Sirius red histological staining showed that decreased ECM fiber area in ZFR is partially restored by Ex-4. Ontology analysis of the myofibril compartment revealed that decreased muscle contractile function in ZFR is partially restored by Ex-4, as confirmed by Phalloidin histological staining that showed a partial restoration by Ex-4 of altered contractile apparatus in ZFR. Ontology analysis of ER DEGs in ZFR versus LR showed that some of them are related to the AMP-activated protein kinase (AMPK) signaling pathway. Phosphorylated AMPK levels were strongly increased in Ex-4-treated ZFR., Conclusion: Altogether, our results suggest that GLP-1ra strongly restructure ECM and reinforce contractile capabilities in ZFR, while optimizing the cellular metabolism through AMPK., (© 2022. The Author(s), under exclusive licence to Springer Nature Limited.)

Published
2022
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33. Peroxisome-Derived Hydrogen Peroxide Modulates the Sulfenylation Profiles of Key Redox Signaling Proteins in Flp-In T-REx 293 Cells.

Author

Lismont C, Revenco I, Li H, Costa CF, Lenaerts L, Hussein MAF, De Bie J, Knoops B, Van Veldhoven PP, Derua R, and Fransen M

Abstract

The involvement of peroxisomes in cellular hydrogen peroxide (H 2 O 2 ) metabolism has been a central theme since their first biochemical characterization by Christian de Duve in 1965. While the role of H 2 O 2 substantially changed from an exclusively toxic molecule to a signaling messenger, the regulatory role of peroxisomes in these signaling events is still largely underappreciated. This is mainly because the number of known protein targets of peroxisome-derived H 2 O 2 is rather limited and testing of specific targets is predominantly based on knowledge previously gathered in related fields of research. To gain a broader and more systematic insight into the role of peroxisomes in redox signaling, new approaches are urgently needed. In this study, we have combined a previously developed Flp-In T-REx 293 cell system in which peroxisomal H 2 O 2 production can be modulated with a yeast AP-1-like-based sulfenome mining strategy to inventory protein thiol targets of peroxisome-derived H 2 O 2 in different subcellular compartments. By using this approach, we identified more than 400 targets of peroxisome-derived H 2 O 2 in peroxisomes, the cytosol, and mitochondria. We also observed that the sulfenylation kinetics profiles of key targets belonging to different protein families (e.g., peroxiredoxins, annexins, and tubulins) can vary considerably. In addition, we obtained compelling but indirect evidence that peroxisome-derived H 2 O 2 may oxidize at least some of its targets (e.g., transcription factors) through a redox relay mechanism. In conclusion, given that sulfenic acids function as key intermediates in H 2 O 2 signaling, the findings presented in this study provide valuable insight into how peroxisomes may be integrated into the cellular H 2 O 2 signaling network., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2022 Lismont, Revenco, Li, Costa, Lenaerts, Hussein, De Bie, Knoops, Van Veldhoven, Derua and Fransen.)

Published
2022
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34. Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function.

Author

Poncin MA, Van Meerbeeck P, Simpson JD, Clippe A, Tyckaert F, Bouillenne F, Degand H, Matagne A, Morsomme P, Knoops B, and Alsteens D

Abstract

Human peroxiredoxin-5 (PRDX5) is a unique redox-sensitive protein that plays a dual role in brain ischemia-reperfusion injury. While intracellular PRDX5 has been reported to act as a neuroprotective antioxidative enzyme by scavenging peroxides, once released extracellularly from necrotic brain cells, the protein aggravates neural cell death by inducing expression of proinflammatory cytokines in macrophages through activation of Toll-like receptor (TLR) 2 (TLR2) and 4 (TLR4). Although recent evidence showed that PRDX5 was able to interact directly with TLR4, little is known regarding the role of the cysteine redox state of PRDX5 on its DAMP function. To gain insights into the role of PRDX5 redox-active cysteine residues in the TLR4-dependent proinflammatory activity of the protein, we used a recombinant human PRDX5 in the disulfide (oxidized) form and a mutant version lacking the peroxidatic cysteine, as well as chemically reduced and hyperoxidized PRDX5 proteins. We first analyzed the oxidation state and oligomerization profile by Western blot, mass spectrometry, and SEC-MALS. Using ELISA, we demonstrate that the disulfide bridge between the enzymatic cysteines is required to allow improved TLR4-dependent IL-8 secretion. Moreover, single-molecule force spectroscopy experiments revealed that TLR4 alone is not sufficient to discriminate the different PRDX5 redox forms. Finally, flow cytometry binding assays show that disulfide PRDX5 has a higher propensity to bind to the surface of living TLR4-expressing cells than the mutant protein. Taken together, these results demonstrate the importance of the redox state of PRDX5 cysteine residues on TLR4-induced inflammation.

Published
2021
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35. Punicic Acid Triggers Ferroptotic Cell Death in Carcinoma Cells.

Author

Vermonden P, Vancoppenolle M, Dierge E, Mignolet E, Cuvelier G, Knoops B, Page M, Debier C, Feron O, and Larondelle Y

Subjects
Carcinoma metabolism, Cell Line, Tumor, Colorectal Neoplasms drug therapy, Colorectal Neoplasms metabolism, Docosahexaenoic Acids metabolism, HCT116 Cells, Humans, Hypopharyngeal Neoplasms drug therapy, Hypopharyngeal Neoplasms metabolism, Lipid Peroxidation drug effects, Antineoplastic Agents pharmacology, Carcinoma drug therapy, Ferroptosis drug effects, Linolenic Acids pharmacology
Abstract

Plant-derived conjugated linolenic acids (CLnA) have been widely studied for their preventive and therapeutic properties against diverse diseases such as cancer. In particular, punicic acid (PunA), a conjugated linolenic acid isomer (C18:3 c9t11c13) present at up to 83% in pomegranate seed oil, has been shown to exert anti-cancer effects, although the mechanism behind its cytotoxicity remains unclear. Ferroptosis, a cell death triggered by an overwhelming accumulation of lipid peroxides, has recently arisen as a potential mechanism underlying CLnA cytotoxicity. In the present study, we show that PunA is highly cytotoxic to HCT-116 colorectal and FaDu hypopharyngeal carcinoma cells grown either in monolayers or as three-dimensional spheroids. Moreover, our data indicate that PunA triggers ferroptosis in carcinoma cells. It induces significant lipid peroxidation and its effects are prevented by the addition of ferroptosis inhibitors. A combination with docosahexaenoic acid (DHA), a known polyunsaturated fatty acid with anticancer properties, synergistically increases PunA cytotoxicity. Our findings highlight the potential of using PunA as a ferroptosis-sensitizing phytochemical for the prevention and treatment of cancer.

Published
2021
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36. Peroxisomes as Modulators of Cellular Protein Thiol Oxidation: A New Model System.

Author

Lismont C, Nordgren M, Brees C, Knoops B, Van Veldhoven PP, and Fransen M

Subjects
Cells, Cultured, Forkhead Box Protein O3 metabolism, HEK293 Cells, Humans, Hydrogen Peroxide metabolism, NF-kappa B p50 Subunit metabolism, Oxidation-Reduction, Peroxiredoxins metabolism, Peroxisome-Targeting Signal 1 Receptor metabolism, Proto-Oncogene Mas, Transcription Factor RelA metabolism, Models, Biological, Peroxisomes metabolism, Sulfhydryl Compounds metabolism
Abstract

Aims: Peroxisomes are ubiquitous, single-membrane-bounded organelles that contain considerable amounts of enzymes involved in the production or breakdown of hydrogen peroxide (H 2 O 2 ), a key signaling molecule in multiple biological processes and disease states. Despite this, the role of this organelle in cross-compartmental H 2 O 2 signaling remains largely unclear, mainly because of the difficulty to modulate peroxisomal H 2 O 2 production in a selective manner. This study aimed at establishing and validating a cellular model suitable to decipher the complex signaling processes associated with peroxisomal H 2 O 2 release., Results: Here, we report the development of a human cell line that can be used to selectively generate H 2 O 2 inside peroxisomes in a time- and dose-controlled manner. In addition, we provide evidence that peroxisome-derived H 2 O 2 can oxidize redox-sensitive cysteine residues in multiple proteins within (e.g., peroxiredoxin-5 [PRDX5]) and outside (e.g., nuclear factor kappa B subunit 1 [NFKB1] and subunit RELA proto-oncogene [RELA], phosphatase and tensin homolog [PTEN], forkhead box O3 [FOXO3], and peroxin 5 [PEX5]) the peroxisomal compartment. Furthermore, we show that the extent of protein oxidation depends on the subcellular location of the target protein and is inversely correlated to catalase activity and cellular glutathione content. Finally, we demonstrate that excessive H 2 O 2 production inside peroxisomes does not induce their selective degradation, at least not under the conditions examined., Innovation: This study describes for the first time a powerful model system that can be used to examine the role of peroxisome-derived H 2 O 2 in redox-regulated (patho)physiological processes, a research area in need of further investigation and innovative approaches., Conclusion: Our results provide unambiguous evidence that peroxisomes can serve as regulatory hubs in thiol-based signaling networks.

Published
2019
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37. Specific Interactions Measured by AFM on Living Cells between Peroxiredoxin-5 and TLR4: Relevance for Mechanisms of Innate Immunity.

Author

Knoops B, Becker S, Poncin MA, Glibert J, Derclaye S, Clippe A, and Alsteens D

Subjects
Animals, CHO Cells, Cell Line, Cricetulus, Immunity, Innate, Inflammation immunology, Inflammation metabolism, Mechanotransduction, Cellular, Molecular Docking Simulation, Peroxiredoxins immunology, Protein Binding, Toll-Like Receptor 4 immunology, Microscopy, Atomic Force methods, Peroxiredoxins metabolism, Toll-Like Receptor 4 metabolism
Abstract

Inflammation is a pathophysiological response of innate immunity to infection or tissue damage. This response is among others triggered by factors released by damaged or dying cells, termed damage-associated molecular pattern (DAMP) molecules that act as danger signals. DAMPs interact with pattern recognition receptors (PRRs) to contribute to the induction of inflammation. However, how released peroxiredoxins (PRDXs) are able to activate PRRs, such as Toll-like receptors (TLRs), remains elusive. Here, we used force-distance curve-based atomic force microscopy to investigate the molecular mechanisms by which extracellular human PRDX5 can activate a proinflammatory response. Single-molecule experiments demonstrated that PRDX5 binds to purified TLR4 receptors, on macrophage-differentiated THP-1 cells, and on human TLR4-transfected CHO cells. These findings suggest that extracellular PRDX5 can specifically trigger a proinflammatory response. Moreover, our work also revealed that PRDX5 binding induces a cellular mechanoresponse. Collectively, this study provides insights into the role of extracellular PRDX5 in innate immunity., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Published
2018
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38. The curious case of peroxiredoxin-5: what its absence in aves can tell us and how it can be used.

Author

Pirson M, Clippe A, and Knoops B

Subjects
Amino Acid Sequence, Animals, Blotting, Western, Cell Line, Tumor, Conserved Sequence, Cysteine metabolism, Electroporation, Humans, Peroxidases genetics, Peroxiredoxins chemistry, Sequence Homology, Amino Acid, Subcellular Fractions metabolism, Chickens metabolism, Peroxiredoxins metabolism
Abstract

Background: Peroxiredoxins are ubiquitous thiol-dependent peroxidases that represent a major antioxidant defense in both prokaryotic cells and eukaryotic organisms. Among the six vertebrate peroxiredoxin isoforms, peroxiredoxin-5 (PRDX5) appears to be a particular peroxiredoxin, displaying a different catalytic mechanism, as well as a wider substrate specificity and subcellular distribution. In addition, several evolutionary peculiarities, such as loss of subcellular targeting in certain species, have been reported for this enzyme., Results: Western blotting analyses of 2-cys PRDXs (PRDX1-5) failed to identify the PRDX5 isoform in chicken tissue homogenates. Thereafter, via in silico analysis of PRDX5 orthologs, we went on to show that the PRDX5 gene is conserved in all branches of the amniotes clade, with the exception of aves. Further investigation of bird genomic sequences and expressed tag sequences confirmed the disappearance of the gene, though TRMT112, a gene located closely to the 5' extremity of the PRDX5 gene, is conserved. Finally, using in ovo electroporation to overexpress the long and short forms of human PRDX5, we showed that, though the gene is lost in birds, subcellular targeting of human PRDX5 is conserved in the chick., Conclusions: Further adding to the distinctiveness of this enzyme, this study reports converging evidence supporting loss of PRDX5 in aves. In-depth analysis revealed that this absence is proper to birds as PRDX5 appears to be conserved in non-avian amniotes. Finally, taking advantage of the in ovo electroporation technique, we validate the subcellular targeting of human PRDX5 in the chick embryo and bring forward this gain-of-function model as a potent way to study PRDX5 functions in vivo.

Published
2018
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39. Expression and distribution of peroxiredoxins in the retina and optic nerve.

Author

Chidlow G, Wood JP, Knoops B, and Casson RJ

Subjects
Animals, Astrocytes metabolism, Axons metabolism, Callithrix, Ependymoglial Cells metabolism, Humans, Isoenzymes metabolism, Neurons metabolism, RNA, Messenger metabolism, Rats, Rats, Sprague-Dawley, Optic Nerve metabolism, Peroxiredoxins metabolism, Retina metabolism
Abstract

Oxidative stress is implicated in various pathological conditions of the retina and optic nerve. Peroxiredoxins (Prdxs) comprise a recently characterized family of antioxidant enzymes. To date, little information exists regarding the distribution of Prdxs in the eye. Herein, we employed a combination of qRT-PCR, immunohistochemistry and Western blotting to determine the level of expression and distribution of the six Prdx isoforms in the retina and optic nerve of the rat. In addition, we performed some parallel analyses on the common marmoset (Callithrix Jacchus). In the rat, all of the Prdx transcripts were expressed in relatively high amounts in both retina and optic nerve, with abundances ranging from approximately 3-50 % of the level of the housekeeping gene cyclophilin. With regard to protein expression, each isoform was detected in the retina and optic nerve by either Western blotting and/or immunohistochemistry. Excepting Prdx4, there was a good correspondence between the rodent and primate results. In the retina, Prdx1 and Prdx2 were principally localized to neurons in the inner nuclear layer and cone photoreceptors, Prdx3 and Prdx5 displayed characteristic mitochondrial immunolabeling, while Prdx6 was associated with astrocytes and Müller cells. In the optic nerve, Prdx1 was robustly expressed by oligodendrocytes, Prdx3 and Prdx5 were observed in axons, and Prdx6 was restricted to astrocytes. The present findings augment our understanding of the distribution and expression of the Prdxs in the retina and optic nerve of rodents and primates and lay the foundation for subsequent analysis of their involvement in relevant blinding diseases., Competing Interests: The authors declare no competing financial interests.

Published
2016
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40. Extrapancreatic effects of incretin hormones: evidence for weight-independent changes in morphological aspects and oxidative status in insulin-sensitive organs of the obese nondiabetic Zucker rat (ZFR).

Author

Colin IM, Colin H, Dufour I, Gielen CE, Many MC, Saey J, Knoops B, and Gérard AC

Subjects
Adipose Tissue drug effects, Animals, Blood Glucose drug effects, Body Weight drug effects, Exenatide, Hepatocytes cytology, Hepatocytes drug effects, Insulin metabolism, Male, Muscle, Skeletal cytology, Muscle, Skeletal drug effects, Organ Size drug effects, Organ Specificity, Rats, Rats, Zucker, Incretins administration & dosage, Insulin Resistance, Oxidative Stress drug effects, Peptides administration & dosage, Venoms administration & dosage
Abstract

Incretin-based therapies are widely used to treat type 2 diabetes. Although hypoglycemic actions of incretins are mostly due to their insulinotropic/glucagonostatic effects, they may also influence extrapancreatic metabolism. We administered exendin-4 (Ex-4), a long-acting glucagon-like peptide receptor agonist, at low dose (0.1 nmol/kg/day) for a short period (10 days), in obese nondiabetic fa/fa Zucker rats (ZFRs). Ex-4-treated ZFRs were compared to vehicle (saline)-treated ZFRs and vehicle- and Ex-4-treated lean rats (LRs). Blood glucose levels were measured at days 0, 9, and 10. Ingested food and animal weight were recorded daily. On the day of sacrifice (d10), blood was sampled along with liver, epididymal, subcutaneous, brown adipose, and skeletal muscle tissues from animals fasted for 24 h. Plasma insulin and blood glucose levels, food intake, and body and epididymal fat weight were unchanged, but gross morphological changes were observed in insulin-sensitive tissues. The average size of hepatocytes was significantly lower in Ex-4-treated ZFRs, associated with decreased number and size of lipid droplets and 4-hydroxy-2-nonenal (HNE) staining, a marker of oxidative stress (OS). Myocytes, which were smaller in ZFRs than in LRs, were significantly enlarged and depleted of lipid droplets in Ex-4-treated ZFRs. Weak HNE staining was increased by Ex-4. A similar observation was made in brown adipose tissue, whereas the elevated HNE staining observed in epididymal adipocytes of ZFRs, suggestive of strong OS, was decreased by Ex-4. These results suggest that incretins by acting on OS in insulin-sensitive tissues may contribute to weight-independent improvement in insulin sensitivity., (© 2016 The Authors. Physiological Reports published by Wiley Periodicals, Inc. on behalf of the American Physiological Society and The Physiological Society.)

Published
2016
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41. Multiple Roles of Peroxiredoxins in Inflammation.

Author

Knoops B, Argyropoulou V, Becker S, Ferté L, and Kuznetsova O

Subjects
Animals, Humans, Oxidative Stress, Peroxides metabolism, Peroxynitrous Acid metabolism, Signal Transduction, Inflammation enzymology, Peroxiredoxins metabolism
Abstract

Inflammation is a pathophysiological response to infection or tissue damage during which high levels of reactive oxygen and nitrogen species are produced by phagocytes to kill microorganisms. Reactive oxygen and nitrogen species serve also in the complex regulation of inflammatory processes. Recently, it has been proposed that peroxiredoxins may play key roles in innate immunity and inflammation. Indeed, peroxiredoxins are evolutionarily conserved peroxidases able to reduce, with high rate constants, hydrogen peroxide, alkyl hydroperoxides and peroxynitrite which are generated during inflammation. In this minireview, we point out different possible roles of peroxiredoxins during inflammatory processes such as cytoprotective enzymes against oxidative stress, modulators of redox signaling, and extracellular pathogen- or damage-associated molecular patterns. A better understanding of peroxiredoxin functions in inflammation could lead to the discovery of new therapeutic targets.

Published
2016
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42. Expression of peroxiredoxins and thioredoxins in the mouse spinal cord during embryonic development.

Author

Pirson M and Knoops B

Subjects
Age Factors, Animals, Catalase metabolism, Embryo, Mammalian, Female, Forkhead Transcription Factors metabolism, Humans, LIM-Homeodomain Proteins metabolism, Mice, Mice, Inbred C57BL, Mitochondrial Proton-Translocating ATPases metabolism, Neuroglia metabolism, Neurons metabolism, Pregnancy, Rats, Receptors, Peptide metabolism, Repressor Proteins metabolism, Spinal Cord cytology, Transcription Factors metabolism, Gene Expression Regulation, Developmental physiology, Peroxiredoxins metabolism, Spinal Cord embryology, Spinal Cord metabolism, Thioredoxins metabolism
Abstract

Reactive oxygen and nitrogen species (ROS/RNS) are natural byproducts of cellular metabolism. Although these molecules are deleterious at high concentrations, moderate levels of ROS/RNS are essential for normal cell function and take part in numerous cellular processes. The regulation of ROS/RNS is largely attended by peroxiredoxins (Prdxs) and their main reductants, thioredoxins (Trxs). Through their oxidoreductase activities, the members of the Trx/Prdx system can also affect certain cellular processes, notably many implicated in central nervous system (CNS) development. Although several studies have investigated the expression of Prdxs and Trxs in mouse, rat, and human adult CNS, few data are available concerning embryonic stages. In this work, we use immunofluorescence analyses to study the distribution of these enzymes during prenatal mouse spinal cord development. Our results highlight several patterns that contrast with available data for the adult. Indeed, Prdx1, Prdx4, and Prdx6, which are expressed in glial cells in the adult CNS, present clear neuronal localization in mouse spinal cord during embryonic development. Additionally, Prdx1, Prdx2, and to a lesser extent Prdx4, Prdx6, and Trx1 are localized mainly in the nucleus of neural cells. Finally, we identified a consistent, intense expression of all Prdxs and Trxs in groups of cells located in ventral regions of the spinal cord that express motor neuronal markers. These striking expression patterns suggest novel functions of these enzymes at these stages and offer clues to the role of the Trx/Prdx system during embryonic development of the spinal cord., (© 2015 Wiley Periodicals, Inc.)

Published
2015
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43. Thioredoxin-2 Modulates Neuronal Programmed Cell Death in the Embryonic Chick Spinal Cord in Basal and Target-Deprived Conditions.

Author

Pirson M, Debrulle S, Clippe A, Clotman F, and Knoops B

Subjects
Animals, Apoptosis physiology, Cell Differentiation physiology, Chick Embryo, Gene Expression Regulation, Developmental genetics, Cell Death physiology, Motor Neurons metabolism, Motor Neurons physiology, Spinal Cord metabolism, Spinal Cord physiology, Thioredoxins metabolism
Abstract

Thioredoxin-2 (Trx2) is a mitochondrial protein using a dithiol active site to reduce protein disulfides. In addition to the cytoprotective function of this enzyme, several studies have highlighted the implication of Trx2 in cellular signaling events. In particular, growing evidence points to such roles of redox enzymes in developmental processes taking place in the central nervous system. Here, we investigate the potential implication of Trx2 in embryonic development of chick spinal cord. To this end, we first studied the distribution of the enzyme in this tissue and report strong expression of Trx2 in chick embryo post-mitotic neurons at E4.5 and in motor neurons at E6.5. Using in ovo electroporation, we go on to highlight a cytoprotective effect of Trx2 on the programmed cell death (PCD) of neurons during spinal cord development and in a novel cultured spinal cord explant model. These findings suggest an implication of Trx2 in the modulation of developmental PCD of neurons during embryonic development of the spinal cord, possibly through redox regulation mechanisms.

Published
2015
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44. Antioxidant cytoprotection by peroxisomal peroxiredoxin-5.

Author

Walbrecq G, Wang B, Becker S, Hannotiau A, Fransen M, and Knoops B

Subjects
Animals, Antioxidants metabolism, Cytoprotection, Gene Expression, Humans, Lipid Peroxidation, Mice, Mitochondria, Oxidative Stress, Peroxisomes enzymology, Oligodendroglia physiology, Peroxiredoxins physiology
Abstract

Peroxiredoxin-5 (PRDX5) is a thioredoxin peroxidase that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. This enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus in human cells. Antioxidant cytoprotective functions have been previously documented for cytosolic, mitochondrial, and nuclear mammalian PRDX5. However, the exact function of PRDX5 in peroxisomes is still not clear. The aim of this work was to determine the function of peroxisomal PRDX5 in mammalian cells and, more specifically, in glial cells. To study the role of PRDX5 in peroxisomes, the endogenous expression of PRDX5 in murine oligodendrocyte 158N cells was silenced by RNA interference. In addition, human PRDX5 was also overexpressed in peroxisomes using a vector coding for human PRDX5, whose unconventional peroxisomal targeting sequence 1 (PTS1; SQL) was replaced by the prototypical PTS1 SKL. Stable 158N clones were obtained. The antioxidant cytoprotective function of peroxisomal PRDX5 against peroxisomal and mitochondrial KillerRed-mediated reactive oxygen species production as well as H2O2 was examined using MTT viability assays, roGFP2, and C11-BOBIPY probes. Altogether our results show that peroxisomal PRDX5 protects 158N oligodendrocytes against peroxisomal and mitochondrial KillerRed- and H2O2-induced oxidative stress., (Copyright © 2015 Elsevier Inc. All rights reserved.)

Published
2015
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45. Deconstructing the catalytic efficiency of peroxiredoxin-5 peroxidatic cysteine.

Author

Portillo-Ledesma S, Sardi F, Manta B, Tourn MV, Clippe A, Knoops B, Alvarez B, Coitiño EL, and Ferrer-Sueta G

Subjects
Catalytic Domain, Escherichia coli, Gene Expression Regulation, Models, Molecular, Peroxiredoxins chemistry, Protein Conformation, Cysteine chemistry, Peroxiredoxins metabolism
Abstract

Human peroxiredoxin-5 (PRDX5) is a thiol peroxidase that reduces H2O2 10(5) times faster than free cysteine. To assess the influence of two conserved residues on the reactivity of the critical cysteine (C47), we determined the reaction rate constants of PRDX5, wild type (WT), T44V and R127Q with one substrate electrophile (H2O2) and a nonspecific electrophile (monobromobimane). We also studied the corresponding reactions of low molecular weight (LMW) thiolates in order to construct a framework against which we could compare our proteins. To obtain a detailed analysis of the structural and energetic changes involved in the reaction between WT PRDX5 and H2O2, we performed ONIOM quantum mechanics/molecular mechanics (QM/MM) calculations with a QM region including 60 atoms of substrate and active site described by the B3LYP density functional and the 6-31+G(d,p) basis set; the rest of the protein was included in the MM region. Brønsted correlations reveal that the absence of T44 can increase the general nucleophilicity of the C47 but decreases the specific reactivity toward H2O2 by a factor of 10(3). The R127Q mutation causes C47 to behave like a LMW thiolate in the two studied reactions. QM/MM results with WT PRDX5 showed that hydrogen bonds in the active site are the cornerstone of two effects that make catalysis possible: the enhancement of thiolate nucleophilicity upon substrate ingress and the stabilization of the transition state. In both effects, T44 has a central role. These effects occur in a precise temporal sequence that ensures that the selective nucleophilicity of C47 is available only for peroxide substrates.

Published
2014
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46. Abolition of peroxiredoxin-5 mitochondrial targeting during canid evolution.

Author

Van der Eecken V, Clippe A, Dekoninck S, Goemaere J, Walbrecq G, Van Veldhoven PP, and Knoops B

Subjects
Amino Acid Sequence, Animals, Cell Line, Dogs, Humans, Molecular Sequence Data, Oxidative Stress genetics, Oxidative Stress physiology, Peroxiredoxins genetics, Peroxiredoxins chemistry, Peroxiredoxins metabolism
Abstract

In human, the subcellular targeting of peroxiredoxin-5 (PRDX5), a thioredoxin peroxidase, is dependent on the use of multiple alternative transcription start sites and two alternative in-frame translation initiation sites, which determine whether or not the region encoding a mitochondrial targeting sequence (MTS) is translated. In the present study, the abolition of PRDX5 mitochondrial targeting in dog is highlighted and the molecular mechanism underlying the loss of mitochondrial PRDX5 during evolution is examined. Here, we show that the absence of mitochondrial PRDX5 is generalized among the extant canids and that the first events leading to PRDX5 MTS abolition in canids involve a mutation in the more 5' translation initiation codon as well as the appearance of a STOP codon. Furthermore, we found that PRDX5 MTS functionality is maintained in giant panda and northern elephant seal, which are phylogenetically closely related to canids. Also, the functional consequences of the restoration of mitochondrial PRDX5 in dog Madin-Darby canine kidney (MDCK) cells were investigated. The restoration of PRDX5 mitochondrial targeting in MDCK cells, instead of protecting, provokes deleterious effects following peroxide exposure independently of its peroxidase activity, indicating that mitochondrial PRDX5 gains cytotoxic properties under acute oxidative stress in MDCK cells. Altogether our results show that, although mitochondrial PRDX5 cytoprotective function against oxidative stress has been clearly demonstrated in human and rodents, PRDX5 targeting to mitochondria has been evolutionary lost in canids. Moreover, restoration of mitochondrial PRDX5 in dog MDCK cells, instead of conferring protection against peroxide exposure, makes them more vulnerable.

Published
2013
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47. Mitochondrial peroxiredoxin-5 as potential modulator of mitochondria-ER crosstalk in MPP+-induced cell death.

Author

De Simoni S, Linard D, Hermans E, Knoops B, and Goemaere J

Subjects
Adenosine Triphosphate metabolism, Animals, Boron Compounds pharmacology, Calcium metabolism, Calpain metabolism, Caspase 3 metabolism, Caspase 9 metabolism, Cell Line, Tumor, DNA, Mitochondrial genetics, DNA, Mitochondrial metabolism, Endoplasmic Reticulum drug effects, Enzyme Inhibitors pharmacology, Gene Expression Regulation drug effects, Gene Expression Regulation genetics, Humans, Hydro-Lyases metabolism, Mice, Mitochondria drug effects, Neuroblastoma pathology, Peroxiredoxins genetics, RNA, Small Interfering genetics, RNA, Small Interfering metabolism, Reactive Oxygen Species metabolism, Subcellular Fractions drug effects, Subcellular Fractions metabolism, Transfection, Tyrosine analogs & derivatives, Tyrosine metabolism, 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine pharmacology, Apoptosis drug effects, Dopamine Agents pharmacology, Endoplasmic Reticulum metabolism, Mitochondria metabolism, Peroxiredoxins metabolism
Abstract

Peroxiredoxin-5 (PRDX5) is an antioxidant enzyme which differs from the other peroxiredoxins with regards to its enzymatic mechanism, its high affinity for organic peroxides and peroxynitrite and its wide subcellular distribution. In particular, the mitochondrial isoform of PRDX5 confers a remarkable cytoprotection toward oxidative stress to mammalian cells. Mitochondrial dysfunction and disruption of Ca²⁺ homeostasis are implicated in neurodegeneration. Growing evidence supports that endoplasmic reticulum (ER) could operate in tandem with mitochondria to regulate intracellular Ca²⁺ fluxes in neurodegenerative processes. Here, we overexpressed mitochondrial PRDX5 in SH-SY5Y cells to dissect the role of this enzyme in 1-methyl-4-phenylpyridinium (MPP)⁺-induced cell death. Our data show that mitochondria-dependent apoptosis triggered by MPP⁺, assessed by the measurement of caspase-9 activation and mitochondrial DNA damage, is prevented by mitochondrial PRDX5 overexpression. Moreover, PRDX5 overexpression blocks the increase in intracellular Ca²⁺, Ca²⁺-dependent activation of calpains and Bax cleavage. Finally, using Ca²⁺ channel inhibitors (Nimodipine, Dantrolene and 2-APB), we show that Ca²⁺ release arises essentially from ER stores through 1,4,5-inositol-trisphosphate receptors (IP3 R). Altogether, our results suggest that the MPP⁺ mitochondrial pathway of apoptosis is regulated by mitochondrial PRDX5 in a process that could involve redox modulation of Ca²⁺ transporters via a crosstalk between mitochondria and ER., (© 2012 International Society for Neurochemistry.)

Published
2013
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48. Determination of acidity and nucleophilicity in thiols by reaction with monobromobimane and fluorescence detection.

Author

Sardi F, Manta B, Portillo-Ledesma S, Knoops B, Comini MA, and Ferrer-Sueta G

Subjects
Cysteine chemistry, Fluorescence, Glutaredoxins chemistry, Humans, Hydrogen-Ion Concentration, Peroxiredoxins chemistry, Trypanosoma brucei brucei enzymology, Bridged Bicyclo Compounds chemistry, Sulfhydryl Compounds chemistry
Abstract

A method based on the differential reactivity of thiol and thiolate with monobromobimane (mBBr) has been developed to measure nucleophilicity and acidity of protein and low-molecular-weight thiols. Nucleophilicity of the thiolate is measured as the pH-independent second-order rate constant of its reaction with mBBr. The ionization constants of the thiols are obtained through the pH dependence of either second-order rate constant or initial rate of reaction. For readily available thiols, the apparent second-order rate constant is measured at different pHs and then plotted and fitted to an appropriate pH function describing the observed number of ionization equilibria. For less available thiols, such as protein thiols, the initial rate of reaction is determined in a wide range of pHs and fitted to the appropriate pH function. The method presented here shows excellent sensitivity, allowing the use of nanomolar concentrations of reagents. The method is suitable for scaling and high-throughput screening. Example determinations of nucleophilicity and pK(a) are presented for captopril and cysteine as low-molecular-weight thiols and for human peroxiredoxin 5 and Trypanosoma brucei monothiol glutaredoxin 1 as protein thiols., (Copyright © 2013 Elsevier Inc. All rights reserved.)

Published
2013
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49. Peroxiredoxin distribution in the mouse brain with emphasis on neuronal populations affected in neurodegenerative disorders.

Author

Goemaere J and Knoops B

Subjects
Animals, Female, Humans, Mice, Mice, Inbred C57BL, Neurodegenerative Diseases pathology, Neurons cytology, Oxidation-Reduction, Oxidative Stress, Peroxiredoxins genetics, Protein Isoforms genetics, Recombinant Proteins genetics, Recombinant Proteins metabolism, Brain anatomy & histology, Brain metabolism, Neurodegenerative Diseases metabolism, Neurons metabolism, Peroxiredoxins metabolism, Protein Isoforms metabolism
Abstract

Redox changes are observed in neurodegenerative diseases, ranging from increased levels of reactive oxygen/nitrogen species and disturbance of antioxidant systems, to nitro-oxidative damage. By reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides, peroxiredoxins (Prdxs) represent a major potential protective barrier against nitro-oxidative insults in the brain. While recent works have investigated the putative role of Prdxs in neurodegenerative disorders, less is known about their expression in the healthy brain. Here we used immunohistochemistry to map basal expression of Prdxs throughout C57BL/6 mouse brain. We first confirmed the neuronal localization of Prdx2-5 and the glial expression of Prdx1, Prdx4, and Prdx6. Then we performed an in-depth analysis of neuronal Prdx distribution in the brain. Our results show that Prdx2-5 are widely detected in the different neuronal populations, and especially well expressed in the olfactory bulb, in the cerebral cortex, in pons nuclei, in the red nucleus, in all cranial nerve nuclei, in the cerebellum, and in motor neurons of the spinal cord. In contrast, Prdx expression is very low in the dopaminergic neurons of substantia nigra pars compacta and in the CA1/2 pyramidal cells of hippocampus. This low basal expression may contribute to the vulnerability of these neurons to nitro-oxidative attacks occurring in Parkinson's disease and Alzheimer's disease. In addition, we found that Prdx expression levels are unevenly distributed among neurons of a determined region and that distinct regional patterns of expression are observed between isoforms, reinforcing the hypothesis of the nonredundant function of Prdxs., (Copyright © 2011 Wiley-Liss, Inc.)

Published
2012
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50. Mitochondrial targeting of peroxiredoxin 5 is preserved from annelids to mammals but is absent in pig Sus scrofa domesticus.

Author

Van der Eecken V, Clippe A, Van Veldhoven PP, and Knoops B

Subjects
Amino Acid Sequence, Animals, Humans, Mammals, Molecular Sequence Data, Polychaeta, Protein Sorting Signals, Protein Transport, Sequence Alignment, Biological Evolution, Mitochondria metabolism, Peroxiredoxins metabolism
Abstract

Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase able to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. In human, PRDX5 was reported to be localized in the cytosol, the mitochondria, the peroxisomes and the nucleus. Mitochondrial localization results from the presence of an N-terminal mitochondrial targeting sequence (MTS). Here, we examined the conservation of mitochondrial localization of PRDX5 in animal species. We found that PRDX5 MTS is present and functional in the annelid lugworm Arenicola marina. Surprisingly, although mitochondrial targeting is well conserved among animals, PRDX5 is missing in mitochondria of domestic pig. Thus, it appears that mitochondrial targeting of PRDX5 may have been lost throughout evolution in animal species, including pig, with unknown functional consequences., (Copyright © 2011 Elsevier B.V. and Mitochondria Research Society. All rights reserved. All rights reserved.)

Published
2011
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