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1دورية أكاديمية
المؤلفون: Rodríguez, Antonio C., Pérez-Mateos, Miriam, Careche, Mercedes, Sánchez Alonso, Isabel, Escribano, M. Isabel, Sanz Martínez, Pedro D., Otero, Laura
المساهمون: Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), European Commission
مصطلحات موضوعية: Anisakis, Lactate dehydrogenase, Fish muscle, Freezing kinetics
الوصف: The effects of weak oscillating magnetic fields (OMFs ≤7 mT at 50 Hz) on freezing were studied in three systems of different complexity. To do so, ferric chloride solutions, lactate dehydrogenase (LDH), and minced hake muscle experimentally infected with Anisakis L3 were frozen with and without OMF application. OMFs did not affect freezing kinetics of either ferric chloride solutions or minced hake muscle. LDH activity, Anisakis mortality, and water-holding capacity of the hake muscle after thawing were not affected by OMF either. Further studies are needed to evaluate the effectiveness of stronger OMFs in a wider frequency range. ; This work has been supported by the Spanish MINECO under the project AGL2012-39756-C02-01 and by the EuropeanUnion Seventh Framework Programme under the project EU PARASITE (GA 312068). A.C. Rodríguez has been supported by the MINECO under predoctoral grant BES-2013-065942. ; Peer reviewed
العلاقة: #PLACEHOLDER_PARENT_METADATA_VALUE#; info:eu-repo/grantAgreement/EC/FP7/312068; Publisher's version; https://doi.org/10.1515/ijfe-2019-0178Test; Sí; International Journal of Food Engineering 16(4): 20190178 (2020); http://hdl.handle.net/10261/219379Test; http://dx.doi.org/10.13039/501100004837Test; http://dx.doi.org/10.13039/501100000780Test; http://dx.doi.org/10.13039/501100003329Test
الإتاحة: https://doi.org/10.1515/ijfe-2019-0178Test
https://doi.org/10.13039/501100004837Test
https://doi.org/10.13039/501100000780Test
https://doi.org/10.13039/501100003329Test
http://hdl.handle.net/10261/219379Test -
2دورية أكاديمية
المساهمون: Fundación Ramón Areces, Fundación Banco Santander, Red de Investigación Cooperativa en Enfermedades Tropicales (España), Ministerio de Economía, Industria y Competitividad (España)
مصطلحات موضوعية: 24-Sterol methyltransferase, Miltefosine Paromomycin, D-lactate dehydrogenase, Aminotransferase of branched-chain amino acids, Leishmania donovani, Genome, Transcriptomes, Trivalent antimony, Amphotericin B
الوصف: Leishmaniasis is a serious medical issue in many countries around the World, but it remains largely neglected in terms of research investment for developing new control and treatment measures. No vaccines exist for human use, and the chemotherapeutic agents currently used are scanty. Furthermore, for some drugs, resistance and treatment failure are increasing to alarming levels. The aim of this work was to identify genomic and trancriptomic alterations associated with experimental resistance against the common drugs used against VL: trivalent antimony (Sb, S line), amphotericin B (AmB, A line), miltefosine (MIL, M line) and paromomycin (PMM, P line). A total of 1006 differentially expressed transcripts were identified in the S line, 379 in the A line, 146 in the M line, and 129 in the P line. Also, changes in ploidy of chromosomes and amplification/deletion of particular regions were observed in the resistant lines regarding the parental one. A series of genes were identified as possible drivers of the resistance phenotype and were validated in both promastigotes and amastigotes from Leishmania donovani, Leishmania infantum and Leishmania major species. Remarkably, a deletion of the gene LinJ.36.2510 (coding for 24-sterol methyltransferase, SMT) was found to be associated with AmB-resistance in the A line. In the P line, a dramatic overexpression of the transcripts LinJ.27.T1940 and LinJ.27.T1950 that results from a massive amplification of the collinear genes was suggested as one of the mechanisms of PMM resistance. This conclusion was reinforced after transfection experiments in which significant PMM-resistance was generated in WT parasites over-expressing either gene LinJ.27.1940 (coding for a D-lactate dehydrogenase-like protein, D-LDH) or gene LinJ.27.1950 (coding for an aminotransferase of branched-chain amino acids, BCAT). This work allowed to identify new drivers, like SMT, the deletion of which being associated with resistance to AmB, and the tandem D-LDH-BCAT, the amplification of which being related ...
العلاقة: Publisher's version; Sí; International Journal for Parasitology: Drugs and Drug Resistance 8: 246- 264 (2018); http://hdl.handle.net/10261/179191Test; http://dx.doi.org/10.13039/501100010198Test; http://dx.doi.org/10.13039/100008054Test; http://dx.doi.org/10.13039/100008049Test
الإتاحة: https://doi.org/10.1016/j.ijpddr.2018.04.002Test
https://doi.org/10.13039/501100010198Test
https://doi.org/10.13039/100008054Test
https://doi.org/10.13039/100008049Test
http://hdl.handle.net/10261/179191Test -
3دورية أكاديمية
المؤلفون: Azzouzi, Sawsen, Rotariua, Lucian, Benito, Ana M., Maser, Wolfgang K., Ben Alib, Mounir, Bala, Camelia
المساهمون: Ministerio de Economía y Competitividad (España), National Authority for Scientific Research (Romania), Consejo Superior de Investigaciones Científicas (España), Gobierno de Aragón
مصطلحات موضوعية: Reduced graphene oxide, Gold nanoparticles, NADH, L-lactate, Cancer biomarkers, L-lactate dehydrogenase
الوصف: In this work, a novel amperometric biosensor based on gold nanoparticles anchored on reduced graphene oxide (RGO-AuNPs) and L-lactate dehydrogenase (LDH) was developed for the sensing of Llactate. Firstly, the RGO-AuNPs modified screen printed electrodes were tested for NADH detection showing a wide dynamic range and a low detection limit. Next, the biosensor was constructed by incorporating both enzyme and RGO-AuNPs in a sol gel matrix derived from tetrametoxysilane and methyltrimetoxysilane. The enzyme loading, working pH, and coenzyme concentration were optimized. The biosensor linearly responded to L-lactate in the range of 10 μM - 5 mM and showed a good specific sensitivity of 154 μA/mM·cm2 with a detection limit of 0.13 μM. This was accompanied by good reproducibility and operational stability. Tests on artificial serum proved that L-lactate can be determined practically without interferences from commonly interfering compounds such as urate, paracetamol and L-ascorbate. Our LDH/RGO-AuNPs/SPCE based biosensor thus performs as electrochemical device for the detection of L-lactate as a viable early cancer bio-marker. ; This work was supported by Romanian National Authority for Scientific Research, grant PN-IIID-PCE-2011-3-0286 and FP7 Marie Curie PIRSES_GA_2012-318053: SMARTCANCERSENS. Ana M. Benito and Wolfgang K. Maser would like to thank the Spanish Ministry MINECO (Projects MAT2010-15026 and ENE2013-48816-C5-5-R), the Spanish National Research Council CSIC (Project 201080E124), and the regional Government of Aragon and the European Social Fund (Project DGA-ESF T66) for financial support. ; Peer reviewed
العلاقة: Postprint; http://dx.doi.org/10.1016/j.bios.2015.03.012Test; Sí; Biosensors and Bioelectronics 69: 280-286 (2015); http://hdl.handle.net/10261/123523Test; http://dx.doi.org/10.13039/501100003329Test; http://dx.doi.org/10.13039/501100003339Test; http://dx.doi.org/10.13039/501100010067Test
الإتاحة: https://doi.org/10.1016/j.bios.2015.03.012Test
https://doi.org/10.13039/501100003329Test
https://doi.org/10.13039/501100003339Test
https://doi.org/10.13039/501100010067Test
http://hdl.handle.net/10261/123523Test -
4دورية أكاديمية
المؤلفون: Cook, W.J., Senkovich, O., Hernández, Agustín, Chattopadhyay, D.
مصطلحات موضوعية: Cryptosporidium parvum, Crystal structures, Lactate dehydrogenase
الوصف: The protozoan parasite Cryptosporidium parvum causes waterborne diseases worldwide. There is no effective therapy for C. parvum infection. The parasite depends mainly on glycolysis for energy production. Lactate dehydrogenase is a major regulator of glycolysis. This paper describes the biochemical characterization of C. parvum lactate dehydrogenase and high resolution crystal structures of the apo-enzyme and four ternary complexes. The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. The results reveal distinctive features of the parasitic enzyme. For example, C. parvum lactate dehydrogenase prefers the acetylpyridine analog of NADH as a cofactor. Moreover, it is slightly less sensitive to gossypol inhibition compared with mammalian lactate dehydrogenases and not inhibited by excess pyruvate. The active site loop and the antigenic loop in C. parvum lactate dehydrogenase are considerably different from those in the human counterpart. Structural features and enzymatic properties of C. parvum lactate dehydrogenase are similar to enzymes from related parasites. Structural comparison with malate dehydrogenase supports a common ancestry for the two genes. ; Peer reviewed
العلاقة: Postprint; http://dx.doi.org/10.1016/j.ijbiomac.2014.12.019Test; Sí; International journal of Biological macromolecules, 74:608-619 (2015); http://hdl.handle.net/10261/111670Test
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5دورية أكاديمية
المؤلفون: Sánchez-Elsner, Tilman, Botella, Luisa María, Velasco, Beatriz, Langa, Carmen, Bernabéu, Carmelo
المساهمون: Ministerio de Ciencia y Tecnología (España), Comunidad de Madrid, Sanchez-Elsner, Tilman, Botella,Luisa María, Bernabéu, Carmelo
مصطلحات موضوعية: Hereditary hemorrhagic telangiectasia, Lactate-dehydrogenase-a, Vascular endothelial-cells, Binding-protein endoglin, Smooth-muscle cells, Human solid tumors, tgf-beta, Inducible factor-1, Monoclonal-antibodies, Cellular responses
الوصف: 11p.-6 fig. ; Endoglin is a transforming growth factor-beta (TGF-beta) co-receptor expressed mainly on endothelial cells and involved in cardiovascular development, angiogenesis, and vascular remodeling. This is illustrated by the fact that mutations in the endoglin gene give rise to hereditary hemorrhagic telangiectasia type 1, a dominant vascular disease with clinical manifestations that originate by a mechanism of haploinsufficiency. Thus, studies on the regulated expression of endoglin are crucial to devising therapeutic strategies for hereditary hemorrhagic telangiectasia type 1. Endoglin is highly expressed in the neovasculature associated with hypoxia such as ischemic tissues and tumors, but the molecular mechanism of this up-regulation is unknown. Here, we have investigated the possible regulation of endoglin expression by hypoxia. Surface protein, transcript, and promoter activity levels of endoglin were found to be up-regulated by hypoxia, indicating that the regulation takes place at the transcriptional level. A hypoxia-responsive element downstream of the main transcription start site of the endoglin gene was functionally characterized. Whereas hypoxia alone moderately stimulated endoglin transcription, addition of TGF-beta under bypoxic conditions resulted in transcriptional cooperation between both signaling pathways, leading to marked stimulation of endoglin expression. Because basal endoglin transcription is sustained by Sp1, and TGF-beta and hypoxia signaling pathways are mediated by Smad proteins and hypoxia-inducible factor-1 (HIF-1), respectively, the involvement of these transcription factors was analyzed. Functional and co-immunoprecipitation experiments demonstrated the existence of a multiprotein complex (Sp1.Smad3.HIF-1) on the endoglin promoter, mediating the cooperation between the hypoxia and TGF-beta pathways. Within this multiprotein complex, Smad3 appears to function not only as a coactivator factor, but also as an adaptor between HIF-1 and Sp1. We propose that basal endoglin ...
العلاقة: Publisher's version; http://dx.doi.org/10.1074/jbc.M207160200Test; Sí; Journal of Biological Chemistry 277 (46) 43799-43808 (2002); http://hdl.handle.net/10261/167755Test; http://dx.doi.org/10.13039/501100006280Test; http://dx.doi.org/10.13039/100012818Test
الإتاحة: https://doi.org/10.1074/jbc.M207160200Test
https://doi.org/10.13039/501100006280Test
https://doi.org/10.13039/100012818Test
http://hdl.handle.net/10261/167755Test -
6دورية أكاديمية
المؤلفون: Koenig, Samuel, Solé, Montserrat
مصطلحات موضوعية: Deep-sea fish, Seasonality, Lactate dehydrogenase, Submarine canyon, Acetylcholinesterase
الوصف: 8 pages, 4 figures, 1 table ; Organisms inhabiting submarine canyons can be potentially exposed to higher inputs of anthropogenic chemicals than their counterparts from the adjacent areas. To find out to what extend this observation applies to a NW Mediterranean canyon (i.e. Blanes canyon) off the Catalan coast, four deep-sea fish species were collected from inside the canyon (BC) and the adjacent open slope (OS). The selected species were: Alepocephalus rostratus, Lepidion lepidion, Coelorinchus mediterraneus and Bathypterois mediterraneus. Prior to the choice of an adequate sentinel species, the natural variation of the selected parameters (biomarkers) in relation to factors such as size, sex, sampling depth and seasonality need to be characterised. In this study, the activities of cholinesterases (ChEs) and lactate dehydrogenase (LDH) enzymes were determined in the muscle of the four deep-sea fish. Of all ChEs, acetylcholinesterase (AChE) activity was dominant and selected for further monitoring. Overall, AChE activity exhibited a significant relationship with fish size whereas LDH activity was mostly dependent on the sex and gonadal development status, although in a species-dependent manner. The seasonal variability of LDH activity was more marked than for AChE activity, and inside-outside canyon (BC-OS) differences were not consistent in all contrasted fish species, and in fact they were more dependent on biological traits. Thus, they did not suggest a differential stress condition between sites inside and outside the canyon. © 2013 Elsevier Ltd. ; The present study was funded by the Spanish Science and Technology Ministry project PROMETEO (CTM2007-66316-C02-02/MAR). Samuel Koenig holds a PhD grant (AFR 08/067) from the Fonds National de la Recherche (FNR), Luxembourg ; Peer Reviewed
العلاقة: https://doi.org/10.1016/j.marenvres.2013.11.003Test; e-issn: 1879-0291; Marine Environmental Research 94: 16-23 (2014); http://hdl.handle.net/10261/92193Test
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7دورية أكاديمية
المؤلفون: Siscar, R., Torreblanca, Amparo, Palanques, Albert, Solé, Montserrat
مصطلحات موضوعية: Lipid peroxidation, Lactate dehydrogenase, Acetylcholinesterase, Kidney, Selenium, Metallothionein
الوصف: 10 pages, 5 figures, 4 tables ; The common sole, Solea solea and the Senegalese sole, Solea senegalensis are two important commercial species that coexist in the NW Mediterranean Sea. The present field survey was designed to assess the role of kidney in metal handling and detoxification in the two sole species collected at six fishing grounds along the Catalan coast. Metallothionein (MT) and selenium (Se) were analysed in relation to toxic metal loads in kidney as potential protective mechanisms. Acetylcholinesterase (AChE) and lactate dehydrogenase (LDH) activities as well as lipid peroxidation (LP) levels were measured in several tissues as general markers of toxicity. AChE was measured in brain muscle and gills, LDH in plasma and LP in muscle and gills. The protective role of MT and Se was indicated by the positive correlations with Hg and Cd levels as well as with the high Se:Hg ratio, in a species-dependent way. Principal Component Analysis (PCA) considering all chemical and biomarker variables discriminated individuals collected at the different fishing grounds. © 2013 Elsevier Ltd. ; This work was financed by the Ministry of Science and Innovation of Spain (ref CTM2010-16611) ; Peer Reviewed
العلاقة: https://doi.org/10.1016/j.marpolbul.2013.10.026Test; e-issn: 1879-3363; Marine Pollution Bulletin 77(1-2): 90-99 (2013); http://hdl.handle.net/10261/89758Test
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8دورية أكاديمية
المؤلفون: Barata Martí, Carlos, Fabregat, M. C., Cotín, J., Huertas, David, Solé, Montserrat, Quirós, Laia, Sanpera, Carolina, Jover, Lluís, Ruiz, Xavier, Grimalt, Joan O., Piña, Benjamín
مصطلحات موضوعية: Total oxyradical scavenging capacity, Esterases, Lactate dehydrogenase oxidative stress, Organochlorine compounds, Mercury, Ardeida
الوصف: 7 pages, 2 figures, 3 tables ; Blood biomarkers and levels of major pollutants in eggs and feathers were used to determine pollution effects in nestlings of the Purple Heron Ardea purpurea and the Little Egret Egretta garzetta, sampled on three Ebro River (NE Spain) areas: a reference site, a site affected by the effluents of a chlor-alkali industry and the river Delta. The two impacted heron populations showed mutually different pollutant and response patterns, suggesting different sources of contamination. In the population nesting near the chlor-alkali plant, elevated levels of hexachlorobenzene (HCB) and polychlorobiphenyls (PCBs) in eggs, and mercury in feathers in A. purpurea chicks were related with reduced blood antioxidant defenses and increased levels of micronuclei. In Ebro Delta, high levels of plasmatic lactate dehydrogenase in A. purpurea chicks and high frequency of micronuclei in blood of both species were tentatively associated with intensive agricultural activities taking place in the area. These results provide the first evidence of a biological response in heron chicks to the release of pollutants at a chlor-alkali plant. High levels of organochlorine and mercury levels in eggs and feathers were related with altered blood biomarkers of heron nesting chicks ; This work has been supported by the Spanish Ministry for the Environment, the Catalan Water Agency (ACA) of the Generalitat de Catalunya and GRACCIE and AQUATOXIGEN (CSD2007-00067, CGL2008-01898) from the Spanish Ministry of Science ; Peer reviewed
وصف الملف: 5875 bytes; application/pdf
العلاقة: https://doi.org/10.1016/j.envpol.2009.10.018Test; Environmental Pollution 158(3): 704-710 (2010); http://hdl.handle.net/10261/20418Test
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9دورية أكاديمية
المؤلفون: López-Millán, Ana Flor, Morales Iribas, Fermín, Abadía Bayona, Anunciación, Abadía Bayona, Javier
مصطلحات موضوعية: Enzyme activity, Carbon fixation, Pyruvate decarboxylase, Plant metabolism, Plant leaf, Sugar beets, Onitate hydratase, Carboxylic acid, Enzyme assay, Genetic regulation, Glucose 6 phosphate dehydrogenase, Hydroponic culture, Iron deficiency, Isocitrate dehydrogenase, Lactate dehydrogenase, Malate dehydrogenase, Nutrient availability, Phosphoenolpyruvate carboxylase
الوصف: The effects of iron deficiency and iron resupply on the metabolism of leaf organic acids have been investigated in hydroponically grown sugar beet. Organic acid concentrations and activities in leaf extracts of severalenzymes related to organic acid metabolism were measured. Enzymes assayed included phosphoenol pyruvate carboxylase (PEP C;EC4.1.1.31), different Krebs cycle enzymes: Malate dehydrogenase (MDH; EC 1.1.1.37), aconitase (EC 4.2.1.3), fumarase (EC 4.2.1.2), citrate synthase (CS;EC4.1.3.7) and isocitrate dehydrogenase (ICDH; EC 1.1.1.42), glucose-6phosphate dehydrogenase (G6PDH; EC 1.1.1.49) and two enzymes related to anaerobic metabolism (lactate dehydrogenase |ILDH]; EC 1.1.1.27, and pyruvate decarboxylase [PDC]; EC 4.1.1.1). Iron concentration in leaves was severely decreased by iron deficiency. Iron resupply caused an increase in iron concentrations, reaching levels similar to the controls in 96 h. Iron deficiency induced a 2.3-fold (from 16 to 37 mmol m-2) increase in leaf total organic acid concentration. Organic anion concentrations were still 4-fold higher than the controls 24 h after resupply and decreased to values similar to those found in the controls after 96 h. All measured enzymes had increased activities in extracts of iron-deficient leaves when compared to the controls and generally decreased to control values 24 h after iron addition. These data provide evidence that organic acid accumulation in iron-deficient leaves is likely not due to an enhancement in leaf carbon fixation. Instead, this accumulation could be associated with organic acid export from the roots to the leaves via xylem. ; This work was supported by grants AGR97-1177 from the Comisión Interministerial de Ciencia y Tecnología to A. A., and PB97-1176 from the Dirección General de Investigación Científica y Técnica and AIR3-CT94-1973 from the Commission of European Communities to J.A., A.F.L.-M. and F.M. were supported by a predoctoral fellowship and a scientist contract from the Spanish Ministry of Science and Education. ...
العلاقة: http://dx.doi.org/10.1034/j.1399-3054.2001.1120105.xTest; Physiologia Plantarum 112 (1): 31-38 (2001); http://hdl.handle.net/10261/99933Test
الإتاحة: https://doi.org/10.1034/j.1399-3054.2001.1120105.xTest
http://hdl.handle.net/10261/99933Test -
10دورية أكاديمية
المؤلفون: Vives, M. A., Macián, M., Seguer, Joan, Infante, María Rosa, Vinardell, M. Pilar
المساهمون: Comisión Asesora de Investigación Científica y Técnica, CAICYT (España)
مصطلحات موضوعية: Anionic surfactant, Antihemolysis, Erythrocyte membrane, Hemolysis, Hypotonic hemolysis, Lactate dehydrogenase, Lysine, Rat erythrocyte
الوصف: Amphiphiles induce hemolysis at a given concentration and that would be dependent on their structure. To know this, we have synthesized anionic surfactants derived from lysine and differing in their chain length and we have studied their hemolytic action. The chain length of the surfactants affects their hemolytic behaviour. Surfactants with two chains of 7 or 9 carbons presented biphasic behaviour at a concentration below or above 50 mg/100 ml. However, only the surfactant with two chains of 7 carbons has a protective effect against hypotonic hemolysis. The maximum protection was exerted when the surfactant was added to a 150 mOsmol/L solution. The surfactant is assumed to intercalate into the membrane in an orientated fashion and prevent the hypotonic hemolysis. For this hemolytic behaviour the presence of two chains of 7 carbons seems to be necessary. ; This work has been supported by grant QFN-89/4011 from the “Programa de Quı́mica Fina.” ; Peer reviewed
العلاقة: https://doi.org/10.1016/S0742-8413Test(97)00033-9; Sí; Comparative Biochemistry and Physiology - C - Toxicology and Pharmacology 118(1): 71-74 (1997); http://hdl.handle.net/10261/332669Test; 9366037; 2-s2.0-0030800583; https://api.elsevier.com/content/abstract/scopus_id/0030800583Test
الإتاحة: https://doi.org/10.1016/s0742-8413Test(97)00033-9
https://doi.org/10.1016/S0742-8413Test(97)00033-9
http://hdl.handle.net/10261/332669Test
https://api.elsevier.com/content/abstract/scopus_id/0030800583Test