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Academic literature on the topic 'Cylindrospermopsin'

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Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Cylindrospermopsin"

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Cheng, Xiaoliang, Honglan Shi, Craig D. Adams, Terry Timmons, and Yinfa Ma. "Effects of oxidative and physical treatments on inactivation of Cylindrospermopsis raciborskii and removal of cylindrospermopsin." Water Science and Technology 60, no. 3 (July 1, 2009): 689–97. http://dx.doi.org/10.2166/wst.2009.385.

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The presence of toxic cyanobacterial blooms (or blue-green algae) in water bodies used either as drinking water or for recreational purposes may present serious health risks for the human population. In this study, the removal of the chemical toxin, cylindrospermopsin, via free chlorine, chlorine dioxide, monochloramine, permanganate, ozone, and UV irradiation was studied. Ozone and free chlorine were found to be highly effective for cylindrospermopsion removal while the other disinfectants were ineffective. Ozone and free chlorine were also determined to be highly effective for the inactivation of the cyanobacteria, Cylindrospermopsis raciborskii, at typical water treatment exposures, chlorine dioxide, monochloramine, and permanganate were only marginally effective at inactivation of Cylindrospermopsis raciborskii.
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Mazmouz, Rabia, Florence Chapuis-Hugon, St�phane Mann, Val�rie Pichon, Annick M�jean, and Olivier Ploux. "Biosynthesis of Cylindrospermopsin and 7-Epicylindrospermopsin in Oscillatoria sp. Strain PCC 6506: Identification of the cyr Gene Cluster and Toxin Analysis." Applied and Environmental Microbiology 76, no. 15 (June 4, 2010): 4943–49. http://dx.doi.org/10.1128/aem.00717-10.

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ABSTRACT Cylindrospermopsin is a cytotoxin produced by Cylindrospermopsis raciborskii and other cyanobacteria that has been implicated in human intoxications. We report here the complete sequence of the gene cluster responsible for the biosynthesis of this toxin in Oscillatoria sp. strain PCC 6506. This cluster of genes was found to be homologous with that of C. raciborskii but with a different gene organization. Using an enzyme-linked immunosorbent assay and an optimized liquid chromatography analytical method coupled to tandem mass spectrometry, we detected 7-epicylindrospermopsin, cylindrospermopsin, and 7-deoxycylindrospermopsin in the culture medium of axenic Oscillatoria PCC 6506 at the following relative concentrations: 68.6%, 30.2%, and 1.2%, respectively. We measured the intracellular and extracellular concentrations, per mg of dried cells of Oscillatoria PCC 6506, of 7-epicylindrospermopsin (0.18 μg/mg and 0.29 μg/mg, respectively) and cylindrospermopsin (0.10 μg/mg and 0.11 μg/mg, respectively). We showed that these two toxins accumulated in the culture medium of Oscillatoria PCC 6506 but that the ratio (2.5 � 0.3) was constant with 7-epicylindrospermopsin being the major metabolite. We also determined the concentrations of these toxins in culture media of other Oscillatoria strains, PCC 6407, PCC 6602, PCC 7926, and PCC 10702, and found that, except for PCC 6602, they all produced 7-epicylindrospermopsin and cylindrospermopsin, with the former being the major toxin, except for PCC 7926, which produced very little 7-epicylindrospermopsin. All the cylindrospermopsin producers studied gave a PCR product using specific primers for the amplification of the cyrJ gene from genomic DNA.
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Mihali, Troco Kaan, Ralf Kellmann, Julia Muenchhoff, Kevin D. Barrow, and Brett A. Neilan. "Characterization of the Gene Cluster Responsible for Cylindrospermopsin Biosynthesis." Applied and Environmental Microbiology 74, no. 3 (December 7, 2007): 716–22. http://dx.doi.org/10.1128/aem.01988-07.

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ABSTRACT Toxic cyanobacterial blooms cause economic losses and pose significant public health threats on a global scale. Characterization of the gene cluster for the biosynthesis of the cyanobacterial toxin cylindrospermopsin (cyr) in Cylindrospermopsis raciborskii AWT205 is described, and the complete biosynthetic pathway is proposed. The cyr gene cluster spans 43 kb and is comprised of 15 open reading frames containing genes required for the biosynthesis, regulation, and export of the toxin. Biosynthesis is initiated via an amidinotransfer onto glycine followed by five polyketide extensions and subsequent reductions, and rings are formed via Michael additions in a stepwise manner. The uracil ring is formed by a novel pyrimidine biosynthesis mechanism and tailoring reactions, including sulfation and hydroxylation that complete biosynthesis. These findings enable the design of toxic strain-specific probes and allow the future study of the regulation and biological role of cylindrospermopsin.
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González-Blanco, Carlos, Felipe Augusto Dörr, Renata Albuquerque, Janice Onuki, and Ernani Pinto. "Alternative Isolation Protocol for Desulfo and Zwitterionic Cylindrospermopsin Alkaloids and Comparison of Their Toxicity in HepG2 Cells." Molecules 25, no. 13 (July 2, 2020): 3027. http://dx.doi.org/10.3390/molecules25133027.

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The term cylindrospermopsins (CYNs) refers to a structurally related class of cyanobacterial metabolites comprised of a tricyclic guanidine group and a hydroxymethyluracil moiety. Most reports in environmental aquatic samples refer to cylindrospermopsin (CYN), and reports on other CYN alkaloids are scarce, due, in part, to a lack of versatile isolation protocols. Thus, using commercially available solid phase extraction (SPE) cartridges, we optimized an isolation protocol for the complete recovery of CYN, 7-deoxy-cylindrospermopsin (7D-CYN) and 7-deoxy-desulfo-cylindrospermopsin (7D-desulfo-CYN) from the same aliquot. The isolation protocol was adaptable depending on the nature of the sample (solid biomass, culture broth or environmental water sample) and tolerates up to 4 L of dense culture broth or 400 mg of lyophilized biomass. To quantitate the CYN alkaloids, we validated an LC-DAD-MS2 method, which takes advantage of the UV absorption of the uracil group (λ 262 nm). Using electrospray ionization (ESI) in a positive ion mode, the high-resolution MS1 data confirms the presence of the protonated alkaloids, and the MS2 fragment assignment is reported as complementary proof of the molecular structure of the CYNs. We isolated three CYN alkaloids with different water solubility using the same lyophilized sample, with a purity that ranged from 95% to 99%. The biological activity of the purified CYNs, along with a synthetic degradation product of CYN (desulfo-cylindrospermopsin), was evaluated by assessing necrosis and apoptosis in vitro using flow cytometry. CYN’s lethal potency in HepG2 cells was greater than the other analogs, due to the presence of all four functional groups: guanidine, uracil, C-7 hydroxyl and the sulfate residue.
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Yilmaz, Mete, and Edward J. Phlips. "Diversity of and Selection Acting on CylindrospermopsincyrBGene Adenylation Domain Sequences in Florida." Applied and Environmental Microbiology 77, no. 7 (February 4, 2011): 2502–7. http://dx.doi.org/10.1128/aem.02252-10.

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ABSTRACTAphanizomenon ovalisporumis the only confirmed cylindrospermopsin producer identified in the United States to date. On the other hand,Cylindrospermopsis raciborskiiis a prominent feature of many lakes in Florida and other regions of the United States. To see the variation in cylindrospermopsincyrBgene adenylation domain sequences and possibly discover new cylindrospermopsin producers, we collected water samples for a 3-year period from 17 different systems in Florida. Positive amplicons were cloned and sequenced, revealing that approximately 92% of sequences wereA. ovalisporum-like (>99% identity). Interestingly, 6% of sequences were very similar (>99% identity) tocyrBsequences ofC. raciborskiifrom Australia and ofAphanizomenonsp. from Germany. Neutrality tests suggest thatA. ovalisporum-likecyrBadenylation domain sequences are under purifying selection, with abundant low-frequency polymorphisms within the population. On the other hand, when compared between species by codon-based methods, amino acids of CyrB also seem to be under purifying selection, in accordance with the one proposed amino acid thought to be activated by the CyrB adenylation domain.
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Saker, Martin L., and Dilwyn J. Griffiths. "Occurrence of blooms of the cyanobacterium Cylindrospermopsis raciborskii (Woloszynska) Seenayya and Subba Raju in a north Queensland domestic water supply." Marine and Freshwater Research 52, no. 6 (2001): 907. http://dx.doi.org/10.1071/mf00110.

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This paper describes seasonally recurring blooms of the potentially toxic cyanobacterium Cylindrospermopsis raciborskii in relation to some limnological characteristics of Lake Julius, a large man-made water impoundment in Australia’s semi-arid tropics. These blooms have occurred each year since 1991, with subsurface concentrations of >50 000 cells mL–1. Periods of greater cyanobacterial abundance are characterized by reduced rates of vertical mixing of the water column, reduced mixed:euphotic depth ratios and high epilimnetic temperatures (>25˚C). Surface scums were not observed and, in general, this species displays a fairly uniform distribution throughout the euphotic zone and below. An isolate of C. raciborskii taken from Lake Julius during a bloom in November 1995 and grown in pure culture produced no symptoms of poisoning when tested by mouse bioassay, and absence of detectable concentrations of the hepatotoxin cylindrospermopsin was confirmed by HPLC/MS-MS. Low concentrations of cylindrospermopsin (~1–2 g L–1) were detected in the lake during blooms of C. raciborskii.
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Li, R., W. W. Carmichael, S. Brittain, G. K. Eaglesham, G. R. Shaw, A. Mahakhant, N. Noparatnaraporn, W. Yongmanitchai, K. Kaya, and M. M. Watanabe. "Isolation and identification of the cyanotoxin cylindrospermopsin and deoxy-cylindrospermopsin from a Thailand strain of Cylindrospermopsis raciborskii (Cyanobacteria)." Toxicon 39, no. 7 (July 2001): 973–80. http://dx.doi.org/10.1016/s0041-0101(00)00236-1.

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Davis, Timothy W., Philip T. Orr, Gregory L. Boyer, and Michele A. Burford. "Investigating the production and release of cylindrospermopsin and deoxy-cylindrospermopsin by Cylindrospermopsis raciborskii over a natural growth cycle." Harmful Algae 31 (January 2014): 18–25. http://dx.doi.org/10.1016/j.hal.2013.09.007.

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Ohtani, Ikuko, Richard E. Moore, and Maria T. C. Runnegar. "Cylindrospermopsin: a potent hepatotoxin from the blue-green alga Cylindrospermopsis raciborskii." Journal of the American Chemical Society 114, no. 20 (September 1992): 7941–42. http://dx.doi.org/10.1021/ja00046a067.

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Senogles, P., G. Shaw, M. Smith, R. Norris, R. Chiswell, J. Mueller, R. Sadler, and G. Eaglesham. "Degradation of the cyanobacterial toxin cylindrospermopsin, from Cylindrospermopsis raciborskii, by chlorination." Toxicon 38, no. 9 (September 2000): 1203–13. http://dx.doi.org/10.1016/s0041-0101(99)00210-x.

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Dissertations / Theses on the topic "Cylindrospermopsin"

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Smith, Maree J. "Biodegradation of the cyanotoxin cylindrospermopsin /." [St. Lucia, Qld.], 2005. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe18474.pdf.

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Bain, Peter A., and n/a. "Gene Expression Profiling of Cylindrospermopsin Toxicity." Griffith University. School of Biomolecular and Physical Sciences, 2007. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20080404.145834.

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Cylindrospermopsin (CYN) is a toxic alkaloid produced by several freshwater cyanobacterial species, the most prevalent in Australian waters being Cylindrospermopsis raciborskii. The occurrence of CYN-producing cyanobacteria in drinking water sources worldwide poses a potential human health risk, with one well-documented case of human poisoning attributed to the toxin. While extensive characterisation of CYN-induced toxicity has been conducted in rodents both in vivo and in primary cell cultures, little is known about mechanisms of toxicity in human cell types. This thesis describes studies undertaken to further define the molecular mechanisms of CYN toxicity in human cells. Concentration-response relationships were determined in various cultured human cell types using standard toxicity assays. As expected, CYN caused dose-dependent decreases in the growth of three cell lines, HepG2, Caco-2 and HeLa, and one primary cell type, human dermal fibroblasts, according to tetrazolium reduction assays. CYN treatment did not disrupt cellular membranes according to the lactate dehydrogenase release assay in HepG2 or Caco-2 cells after 24, 48 or 72 h exposure, but did cause membrane disruption in fibroblasts after 72 h exposure to relatively high concentrations of the toxin. Apoptosis occurred more readily in HeLa cells than HepG2 cells or fibroblasts, with 72 h exposure to 1 &mug/mL required before statistically significant rates of apoptosis occurred in the latter cell types. CYN did not appear to directly affect the structure of actin filaments or microtubules under the conditions used in the present study. The major portion of the work presented in this thesis comprises a large-scale interrogation of changes in gene expression induced by the toxin in cultured cells. To assess the effects of CYN on global gene expression, relative messenger RNA (mRNA) levels in human dermal fibroblasts and HepG2 cells after 6 h and 24 h exposure to 1 &mug/mL CYN were determined using oligonucleotide microarrays representing approximately 19 000 genes. Overall, the number of transcripts significantly altered in abundance was greater in fibroblasts than in HepG2 cells. In both cell types, mRNA levels for genes related to amino acid biosynthesis, carbohydrate metabolism, and protein folding and transport were reduced after CYN treatment, while transcripts representing genes for apoptosis, RNA biosynthesis and RNA processing increased in abundance. More detailed data analyses revealed the modulation of a number of stress response pathways—genes regulated by NF-&kappaB were induced, DNA damage response pathways were up-regulated, and a large number of genes involved in endoplasmic reticulum stress were strongly down-regulated. Genes for the synthesis and processing of mRNA, tRNA and rRNA were strongly up-regulated, indicating that CYN treatment may increase the turnover of all forms of cellular RNA. A small group of genes were differentially expressed in HepG2 cells and fibroblasts, revealing cell-specific responses to the toxin. Selected changes in transcript level were validated using real-time quantitative reverse transcriptase PCR (qRT-PCR). The modulation of stress response pathways by CYN, indicated by microarray analysis, was further investigated using other methods. The role of tumour suppressor protein p53 in CYN-mediated gene expression was confirmed by measuring the expression of known p53-regulated genes following CYN treatment of HepG2 cells and human dermal fibroblasts using qRT-PCR. Western blotting of protein extracts from CYNtreated cells showed that p53 protein accumulation occurred in HepG2 cells, providing additional evidence of the activation of the p53 pathway by CYN in this cell line. The immediate-early genes JUN and FOS were found to be induced by CYN in a concentration-dependent manner, and MYC was induced to a lesser extent. The mitogen-activated protein kinase c-Jun NH2-terminal kinase, implicated in the ribotoxic stress response initiated by damage to ribosomal RNA, appeared to become phosphorylated in HeLa cells after CYN exposure, suggesting that ribotoxic stress may occur in response to CYN in at least some cell types. The expression of a reporter gene under the control of a response element specific for NF-&kappaB was induced at the mRNA level but inhibited at the protein level. This shows that while transcription factors such as p53 and NF-&kappaB are apparently activated in response to the toxin, transactivation of target genes may not necessarily manifest a corresponding increase at the protein level. The current work contributes significantly to the current understanding of cylindrospermopsin toxicity in human-derived cell types, and provides further insight into putative modes of action.
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Evans, Daniel Mackenzie. "Synthetic steps towards the cylindrospermopsin alkaloids." Thesis, Bangor University, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.590643.

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Detailed herein is the tethered Biginelli condensation between irninium ion 201 and beta keto ester 206 leading to a model tricyclic ring system representative of the guanidinium core of cylindrospennopsin alkaloids. This was achieved in a biosynthetically-inspired manner in 12 steps and 8.3% overall yield from simple, commercially available 1,5-pentanediol 172. Also discussed is the adaption of this methodology to allow for the highly efficient stereoselective synthesis of all 3 of the cylindrospermopsin alkaloids and the preparation of the advanced synthetic intermediate nitro-alcohol 223.
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Bain, Peter A. "Gene Expression Profiling of Cylindrospermopsin Toxicity." Thesis, Griffith University, 2007. http://hdl.handle.net/10072/367068.

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Cylindrospermopsin (CYN) is a toxic alkaloid produced by several freshwater cyanobacterial species, the most prevalent in Australian waters being Cylindrospermopsis raciborskii. The occurrence of CYN-producing cyanobacteria in drinking water sources worldwide poses a potential human health risk, with one well-documented case of human poisoning attributed to the toxin. While extensive characterisation of CYN-induced toxicity has been conducted in rodents both in vivo and in primary cell cultures, little is known about mechanisms of toxicity in human cell types. This thesis describes studies undertaken to further define the molecular mechanisms of CYN toxicity in human cells. Concentration-response relationships were determined in various cultured human cell types using standard toxicity assays. As expected, CYN caused dose-dependent decreases in the growth of three cell lines, HepG2, Caco-2 and HeLa, and one primary cell type, human dermal fibroblasts, according to tetrazolium reduction assays. CYN treatment did not disrupt cellular membranes according to the lactate dehydrogenase release assay in HepG2 or Caco-2 cells after 24, 48 or 72 h exposure, but did cause membrane disruption in fibroblasts after 72 h exposure to relatively high concentrations of the toxin. Apoptosis occurred more readily in HeLa cells than HepG2 cells or fibroblasts, with 72 h exposure to 1 µg/mL required before statistically significant rates of apoptosis occurred in the latter cell types. CYN did not appear to directly affect the structure of actin filaments or microtubules under the conditions used in the present study. The major portion of the work presented in this thesis comprises a large-scale interrogation of changes in gene expression induced by the toxin in cultured cells. To assess the effects of CYN on global gene expression, relative messenger RNA (mRNA) levels in human dermal fibroblasts and HepG2 cells after 6 h and 24 h exposure to 1 µg/mL CYN were determined using oligonucleotide microarrays representing approximately 19 000 genes. Overall, the number of transcripts significantly altered in abundance was greater in fibroblasts than in HepG2 cells. In both cell types, mRNA levels for genes related to amino acid biosynthesis, carbohydrate metabolism, and protein folding and transport were reduced after CYN treatment, while transcripts representing genes for apoptosis, RNA biosynthesis and RNA processing increased in abundance. More detailed data analyses revealed the modulation of a number of stress response pathways—genes regulated by NF-?B were induced, DNA damage response pathways were up-regulated, and a large number of genes involved in endoplasmic reticulum stress were strongly down-regulated. Genes for the synthesis and processing of mRNA, tRNA and rRNA were strongly up-regulated, indicating that CYN treatment may increase the turnover of all forms of cellular RNA. A small group of genes were differentially expressed in HepG2 cells and fibroblasts, revealing cell-specific responses to the toxin. Selected changes in transcript level were validated using real-time quantitative reverse transcriptase PCR (qRT-PCR). The modulation of stress response pathways by CYN, indicated by microarray analysis, was further investigated using other methods. The role of tumour suppressor protein p53 in CYN-mediated gene expression was confirmed by measuring the expression of known p53-regulated genes following CYN treatment of HepG2 cells and human dermal fibroblasts using qRT-PCR. Western blotting of protein extracts from CYNtreated cells showed that p53 protein accumulation occurred in HepG2 cells, providing additional evidence of the activation of the p53 pathway by CYN in this cell line. The immediate-early genes JUN and FOS were found to be induced by CYN in a concentration-dependent manner, and MYC was induced to a lesser extent. The mitogen-activated protein kinase c-Jun NH2-terminal kinase, implicated in the ribotoxic stress response initiated by damage to ribosomal RNA, appeared to become phosphorylated in HeLa cells after CYN exposure, suggesting that ribotoxic stress may occur in response to CYN in at least some cell types. The expression of a reporter gene under the control of a response element specific for NF-?B was induced at the mRNA level but inhibited at the protein level. This shows that while transcription factors such as p53 and NF-?B are apparently activated in response to the toxin, transactivation of target genes may not necessarily manifest a corresponding increase at the protein level. The current work contributes significantly to the current understanding of cylindrospermopsin toxicity in human-derived cell types, and provides further insight into putative modes of action.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Physical Sciences
Faculty of Science, Environment, Engineering and Technology
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Djung, Jane F. "An approach toward the total synthesis of cylindrospermopsin /." The Ohio State University, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=osu1486397841223073.

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Catlin, Diane M. "DNA Aptamer Confirmation and Utilization for the Cyanotoxin, Cylindrospermopsin." FIU Digital Commons, 2016. http://digitalcommons.fiu.edu/etd/2552.

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Cyanotoxins are posing an increasing threat to the health of humans and wildlife. Cylindrospermopsin is a cyanotoxin that occurs in warm climates and is harmful when ingested. The toxic effects of CYN can affect multiple organ systems. The effects, coupled with the evidence of a mass contamination of a water supply in Australia, prove that CYN needs to be investigated further. Aptamers have become a desirable method for detection of CYN as a result of an aptamer’s high specificity and the ability to scale up experiments. Aptamers have been designed to bind with a variety of targets, including cyanotoxins. An aptamer for CYN was identified by Elshafey et al. This study aims to confirm the binding of the aptamer to CYN and the selectivity of the aptamer using fluorescent biosensing and circular dichroism. Aptamer affinity capture was used to investigate the possibility of a real world application of the aptamer.
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Littler, Benjamin Joseph. "Synthetic studies directed towards cylindrospermopsin : cyclisations of cyclic sulfates." Thesis, University of Bristol, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337289.

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Blanco, Carlos Andrey González. "A non-targeted proteomics investigation of cylindrospermopsin-induced hepatotoxicity." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/9/9143/tde-19102017-153400/.

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Cyanobacteria is perhaps the phylum that profit the most from the escalating hypereutrophication of continental waters. The resulting cyanobacterial blooms may accumulate a variety of potent toxins. Cylindrospermopsin (CYN) is a cyanotoxin known for inhibiting protein synthesis, and producing oxidative stress as well as DNA damage in eukaryotic cells. Since the toxin\'s molecular mechanisms and targets are still unclear, we purified the cyanotoxin from our lab strains and employed a shotgun proteomics approach to reveal the major changes in HepG2 cells at sublethal doses of CYN (1 µM for 6, 12 and 24h). Metabolically labeled cells were stimulated and lysed after each treatment, their tryptic digests were separated by nano HPLC and analyzed by high-resolution tandem mass spectrometry (HRMS) on data dependent acquisition mode. We scanned an average of 4000 proteins in every sample throughout the three timepoints. Cholesterol biosynthesis and transport was mostly downregulated throughout the timepooints of the experiment. Downregulation of proteins related to ubiquitination (e.g. UBE2L3) and proteolysis pathways (e.g. PSMA2) was observed in the proteomics dataset, and these results were validated by western blot. Transcription, translation and cell cycle processes showed convoluted regulation dynamics involving known cell cycle regulators like PCNA. Downregulation of mitochondrial enzymes, oxidative stress and damage to the mithochondrial inner membrane was early evidenced after a 6 hrs treatment and validated using a JC-1, a mitochondrial membrane potential probe. The resulting dataset gives us a first glimpse of the protein groups affected at the early stage of CYN cell intoxication.
Cianobactéria é o filo que mais se beneficia da crescente hipereutrofização das águas continentais. As florações de cianobactérias resultantes podem acumular potentes toxinas. A Cilindrospermopsina (CYN) é uma cianotoxina conhecida por inibir a síntese protéica e produzir estresse oxidativo, além de danos ao DNA em células eucarióticas. Os mecanismos moleculares e alvos de toxicidade aguda desta toxina ainda não são claros. Por esse motivo adoptamos uma abordagem de proteômica quantitativa baseada em descoberta para revelar as principais alterações nas células HepG2 em doses subletais de CYN (1 µM para 6, 12 e 24h). As proteinas dos hepatócitos foram marcadas metabolicamente, foram estimuladas com a toxina e os digestos trípticos foram analisados por espectrometria de massa em tandem de alta resolução (HRMS) no modo de aquisição dependente de dados. Escaneamos uma média de 4000 proteínas ao longo dos intervalos de tempo. A biosintese e transporte do colesterol foi inibida durante a maior parte do tratamento com a toxina. Proteínas e enzimas relacionadas com o processo de ubiquitinação (ex. UBE2L3) e proteólise (ex. PSMA2) foram inibidas, e alterações nas proteínas envolvidas nesses processos foram validadas por meio de Western Blot. Os processos de transcrição, tradução e ciclo celular mostraram uma dinâmica de regulação complexa, envolvendo reguladores e disruptores do ciclo celular como por exemplo PCNA. Danos à membrana mitocondrial e evidência de estresse oxidativo foram detectados após 6 horas de tratamento, e essas mudanças no proteoma foram validados por meio do corante JC-1 (test que detecta mudanças no potencial da membrana mitocondrial). O banco de dados resultante nos dá um primeiro vislumbre das proteinas afetados no estágio inicial da intoxicação celular pela CYN.
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Fituri, Hisham Saleh. "Synthesis of uracil containing precursors and analogues of cylindrospermopsin." Thesis, Bangor University, 2015. https://research.bangor.ac.uk/portal/en/theses/synthesis-of-uracil-containing-precursors-and-analogues-of-cylindrospermopsin(3d8eff07-e38b-4988-b4d6-b7942a797035).html.

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The thesis covers three topics: i) Synthesis of the uracil D-ring precursor of the cylindrospermopsin alkaloids: this study entailed the preparation of compounds I and II which were shown to be a RHS D-ring precursor in the synthesis of the cylindrospermopsin alkaloids. Compound I was prepared in 3 steps and in 24% overall yield from dibenzylurea whilst II was prepared from either diethyl 1,3-acetonedicarboxylate in 5 steps and 9% overall yield or barbituric acid in 5 steps and 16% overall yield. ii) Preparation of analogues of cylindrospermopsin: the synthesis of the cylindrospermopsin analogue III was achieved in 6 steps and 12% overall yield from the literature compound 2,6-dimethoxypyrimidine-4-carboxaldehyde. iii) Preparation and enzymatic studies on 2.4-dinitrobenzamide pro-drugs: the known pro-drugs IV (X = Cl, Br, I), were prepared and found to be good substrates for the enzyme NfsA NTR. These can thus be considered as alternative pro-drugs to the usually employed CB 1954 in combination with NfsA NTR for human chemotherapy.
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Thornhill, Andrew John. "Synthetic studies towards marine natural products." Thesis, Bangor University, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364987.

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Books on the topic "Cylindrospermopsin"

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Cyanobacterial toxins of drinking water supplies: Cylindrospermopsins and microcystins. Boca Raton, FL: CRC Press, 2005.

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Book chapters on the topic "Cylindrospermopsin"

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Rubiolo, Juan A., Diego Alberto Fernández, Henar López, and M. Carmen Louzao. "Pharmacology of cylindrospermopsin." In Phycotoxins, 317–41. Chichester, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118500354.ch14.

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Kokociński, Mikołaj, Ana Maria Cameán, Shmuel Carmeli, Remedios Guzmán-Guillén, Ángeles Jos, Joanna Mankiewicz-Boczek, James S. Metcalf, Isabel Maria Moreno, Ana Isabel Prieto, and Assaf Sukenik. "Cylindrospermopsin and Congeners." In Handbook of Cyanobacterial Monitoring and Cyanotoxin Analysis, 127–37. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781119068761.ch12.

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Triantis, Theodoros M., Triantafyllos Kaloudis, and Anastasia Hiskia. "Solid-Phase Extraction of Cylindrospermopsin from Filtered and Drinking Water." In Handbook of Cyanobacterial Monitoring and Cyanotoxin Analysis, 396–98. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781119068761.ch47.

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Triantis, Theodoros M., Triantafyllos Kaloudis, and Anastasia Hiskia. "Determination of Cylindrospermopsin in Filtered and Drinking Water by LC-MS/MS." In Handbook of Cyanobacterial Monitoring and Cyanotoxin Analysis, 399–404. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781119068761.ch48.

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Zhang, Weiying, Inchio Lou, Wai Kin Ung, Yijun Kong, and Kai Meng Mok. "Analysis of Cylindrospermopsin- and Microcystin-Producing Genotypes and Cyanotoxin Concentrations in the Macau Storage Reservoir." In Advances in Monitoring and Modelling Algal Blooms in Freshwater Reservoirs, 89–111. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-024-0933-8_6.

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Cerasino, Leonardo. "Analysis of Anatoxin-a and Cylindrospermopsin by Ultra High-Performance Liquid Chromatography Tandem Mass Spectrometry." In Handbook of Cyanobacterial Monitoring and Cyanotoxin Analysis, 413–17. Chichester, UK: John Wiley & Sons, Ltd, 2017. http://dx.doi.org/10.1002/9781119068761.ch51.

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Várkonyi, Zs, O. Zsiros, T. Farkas, G. Garab, B. Ughy, Zs Szegletes, and Z. Gombos. "Adaptation Mechanism of the Photosynthetic Apparatus of Cylindrospermopsis Raciborskii Act 9502 to Different Enviromental Effects." In Photosynthesis: Mechanisms and Effects, 1819–22. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_425.

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Padisák, Judit. "Estimation of minimum sedimentary inoculum (akinete) pool of Cylindrospermopsis raciborskii: a morphology and life-cycle based method." In Phytoplankton and Equilibrium Concept: The Ecology of Steady-State Assemblages, 389–94. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-2666-5_32.

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Zhang, Weiying, Inchio Lou, Wai Kin Ung, Yijun Kong, and Kai Meng Mok. "Application of PCR and Real-Time PCR for Monitoring Cyanobacteria, Microcystis spp. and Cylindrospermopsis raciborskii, in Macau Freshwater Reservoir." In Advances in Monitoring and Modelling Algal Blooms in Freshwater Reservoirs, 69–88. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-024-0933-8_5.

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Furey, Ambrose, Vaishali Bane, Mary Lehane, Christopher Elliott, and Clare Redshaw. "Cylindrospermopsin." In Seafood and Freshwater Toxins, 1031–60. CRC Press, 2014. http://dx.doi.org/10.1201/b16662-43.

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Conference papers on the topic "Cylindrospermopsin"

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Cordeiro, Rita, Rúben Luz, Joana Azevedo, Vitor Vasconcelos, Vítor Gonçalves, and Amélia Fonseca. "Expansion of Cylindrospermopsin in the Azores: Evidence for New Producing Taxa." In The 7th Iberian Congress on Cyanotoxins/3rd Iberoamerican Congress on Cyanotoxins. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/blsf2022014014.

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Huang, Winn-Jung, Hong-Xuan Lin, Hao-Wei Lin, and Kai-Wen Zheng. "Catalytic Ozonation Promoted by TiO2 Catalyst for the Removal of Cyanotoxin Cylindrospermopsin from Water." In The 4th World Congress on New Technologies. Avestia Publishing, 2018. http://dx.doi.org/10.11159/icepr18.156.

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Zin, Walter A., Vinicius R. Oliveira, Mariana B. Avila, Giovanna M. Carvalho, Joao L. Alves, Raquel M. Soares, Sandra M. Oliveira, Lidia M. Lima, Eliezer J. Barreiro, and Alysson R. Carvalho. "Can LASSBio 596 Attenuate Pulmonary Functional And Histological Impairments In Mice Exposed To Cylindrospermopsin?" In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a3547.

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Casas-Rodríguez, Antonio, Leticia Diez-Quijada, Ana Isabel Prieto, Angeles Jos, and Ana María Cameán. "Effects of Refrigeration and Freezing in Cylindrospermopsin and Microcystin Concentrations on Leaves of Lettuce (Lactuca sativa) and Spinach (Spinacia oleracea) †." In The 7th Iberian Congress on Cyanotoxins/3rd Iberoamerican Congress on Cyanotoxins. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/blsf2022014018.

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You might also be interested in the extended bibliographies on the topic 'Cylindrospermopsin' for particular source types:
Journal articles Dissertations / Theses
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