The Experts below are selected from a list of 327 Experts worldwide ranked by ideXlab platform
Ronge Xing - One of the best experts on this subject based on the ideXlab platform.
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in depth analysis of the in vivo toxicity of venom from the jellyfish stomolophus Meleagris
Toxicon, 2014Co-Authors: Yang Yue, Ronge Xing, Song Liu, Xiaolin Chen, Xueqin WangAbstract:Jellyfish Stomolophus Meleagris, a synonym of Nemopilema nomurai, which has often bloomed in the China Sea in recent years, is becoming an increasing threat to human health and life as a result of its strong toxicity. Each year, hundreds of thousands of people were stung, especially in the high season, and the victims suffered itch, edema, myalgia, dyspnea, hypotension, shock and even death. Here, we present the in-depth analysis of the in vivo toxicity of the venom from the jellyfish S. Meleagris by using both an acute toxicological approach and pathological analyses. The venom showed an LD50 of approximately 2.92 mu g/g body weight in mice following an intravenous injection and caused renal glomerular swelling, renal vesicle stricture, renal tubules dilatation, hepatic blood sinusoid dilatation, pulmonary edema and malignant pleural effusion. The pathological sections analysis showed that the kidney and liver were significantly damaged, but the heart, spleen and stomach had no observed changes. Additionally, the hemanalysis showed an increase of white blood cells (WBC), middle cells (Mid), alanine aminotransferase (ALT), blood urine nitrogen (BUN) and uric acid (UA) in the blood. Moreover, the mice also displayed convulsions, mouth bleeding, piloerection, dyspnea and death after the injection of the venom. In conclusion, this venom has a strong toxicity to the kidney of the mice and the acute renal failure might be one of the most important factors for the death after a severe sting. Hopefully, the present study will provide a significant reference for the treatment of stings by the jellyfish S. Meleagris in the future. (C) 2014 Elsevier Ltd. All rights reserved.
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efficacy of venom from tentacle of jellyfish stomolophus Meleagris nemopilema nomurai against the cotton bollworm helicoverpa armigera
BioMed Research International, 2014Co-Authors: Huahua Yu, Rongfeng Li, Xiangli Dong, Ronge Xing, Pengcheng LiAbstract:Efficacy of venom from tentacle of jellyfish Stomolophus Meleagris against the cotton bollworm Helicoverpa armigera was determined. Venom from tentacle of jellyfish Stomolophus Meleagris could inhibit the growth of Helicoverpa armigera and the weight inhibiting rate of sample NFr-2 was 60.53%. Of the six samples, only NFr-2 had high insecticidal activity against Helicoverpa armigera and the corrected mortality recorded at 7 d was 74.23%.
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jellyfish venomics and venom gland transcriptomics analysis of stomolophus Meleagris to reveal the toxins associated with sting
Journal of Proteomics, 2014Co-Authors: Wei Xue, Yang Yue, Song Liu, Ronge XingAbstract:Jellyfish Stomolophus Meleagris is a very dangerous animal because of its strong toxicity. However, the composition of the venom is still unclear. Both proteomics and transcriptomics approaches were applied in present study to investigate the major components and their possible relationships to the sting. The proteomics of the venom from S. Meleagris was conducted by tryptic digestion of the crude venom followed by RP-HPLC separation and MS/MS analysis of the tryptic peptides. The venom gland transcriptome was analyzed using a high-throughput Illumina sequencing platform HiSeq (TM) 2000 with de novo assembly. A total of 218 toxins were identified including C-type lectin, phospholipase A(2) (PLA(2)), potassium channel inhibitor, protease inhibitor, metalloprotease, hemolysin and other toxins, most of which should be responsible for the sting. Among them, serine protease inhibitor, PLA(2), potassium channel inhibitor and metalloprotease are predominant, representing 28.44%, 21.56%, 16.06% and 15.14% of the identified venom proteins, respectively. Overall, our combined proteomics and transcriptomics approach provides a systematic overview of the toxins in the venom of jellyfish S. Meleagris and it will be significant to understand the mechanism of the sting.
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isolation and in vitro partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish stomolophus Meleagris
Toxicology in Vitro, 2013Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Jellyfish venom contains various toxins and can cause itching, edema, muscle aches, shortness of breath, blood pressure depression, shock or even death after being stung. Hemolytic protein is one of the most hazardous components in the venom. The present study investigated the hemolytic activity of the nematocyst venom from jellyfish Stomolophus Meleagris. Anion exchange chromatography, DEAE Sepharose Fast Flow, and gel filtration chromatography, Superdex200 had been employed to isolate hemolytic proteins from the nematocyst venom of jellyfish S. Meleagris. Hemolysis of chicken red blood cells was used to quantify hemolytic potency of crude nematocyst venom and chromatography fractions during the purification process. Native-PAGE profile displayed one protein band in the purified hemolytic protein (SmTX); however, two protein bands with apparent molecular weights of similar to 45 kDa and 52 kDa were observed in the reducing SDS-PAGE analysis. Approximately 70 mu g/mL of SmTX caused 50% hemolysis (HU50) of the erythrocyte suspension. The hemolytic activity of SmTX was shown to be temperature and pH dependent, with the optimum temperature and pH being 37 degrees C and pH 5.0. The present study is the first report of isolation and partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish S. Meleagris. The mechanism of the hemolytic activity of SmTX is not clear and deserves further investigation. (C) 2013 Published by Elsevier Ltd.
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isolation identification and characterization of a novel antioxidant protein from the nematocyst of the jellyfish stomolophus Meleagris
International Journal of Biological Macromolecules, 2012Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Reactive oxygen species (ROS) can damage the lipids, proteins and DNA when produced excessively in cells. Here, we describe the isolation and identification of a novel antioxidant protein named SmP90 from the nematocyst of jellyfish Stomolophus Meleagris by 50% ammonium sulfate precipitation and gel filtration chromatography, superdex75. HPLC and SDS-PAGE analysis revealed >95% purity of SmP90 with apparent molecular weight of 90 kDa, approximately. The identification of SmP90 was confirmed by both N-terminal amino acids sequencing, with the sequences of NLDTPYCFYSGDYGG, and peptide mass fingerprint (PMF) analysis by MALDI-TOF-MS. However, no known protein had been completely matched in the database, which indicated that SmP90 might be a novel protein. The antioxidant assay result showed that it had strong superoxide anion radical-scavenging activity with the half-scavenging concentration (EC50) of about 16 mu g/mL. Therefore, the present study is the first time to demonstrate a high efficient method of isolating a novel antioxidant protein from the nematocyst of jellyfish S. Meleagris. (C) 2012 Elsevier B.V. All rights reserved.
Song Liu - One of the best experts on this subject based on the ideXlab platform.
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in depth analysis of the in vivo toxicity of venom from the jellyfish stomolophus Meleagris
Toxicon, 2014Co-Authors: Yang Yue, Ronge Xing, Song Liu, Xiaolin Chen, Xueqin WangAbstract:Jellyfish Stomolophus Meleagris, a synonym of Nemopilema nomurai, which has often bloomed in the China Sea in recent years, is becoming an increasing threat to human health and life as a result of its strong toxicity. Each year, hundreds of thousands of people were stung, especially in the high season, and the victims suffered itch, edema, myalgia, dyspnea, hypotension, shock and even death. Here, we present the in-depth analysis of the in vivo toxicity of the venom from the jellyfish S. Meleagris by using both an acute toxicological approach and pathological analyses. The venom showed an LD50 of approximately 2.92 mu g/g body weight in mice following an intravenous injection and caused renal glomerular swelling, renal vesicle stricture, renal tubules dilatation, hepatic blood sinusoid dilatation, pulmonary edema and malignant pleural effusion. The pathological sections analysis showed that the kidney and liver were significantly damaged, but the heart, spleen and stomach had no observed changes. Additionally, the hemanalysis showed an increase of white blood cells (WBC), middle cells (Mid), alanine aminotransferase (ALT), blood urine nitrogen (BUN) and uric acid (UA) in the blood. Moreover, the mice also displayed convulsions, mouth bleeding, piloerection, dyspnea and death after the injection of the venom. In conclusion, this venom has a strong toxicity to the kidney of the mice and the acute renal failure might be one of the most important factors for the death after a severe sting. Hopefully, the present study will provide a significant reference for the treatment of stings by the jellyfish S. Meleagris in the future. (C) 2014 Elsevier Ltd. All rights reserved.
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jellyfish venomics and venom gland transcriptomics analysis of stomolophus Meleagris to reveal the toxins associated with sting
Journal of Proteomics, 2014Co-Authors: Wei Xue, Yang Yue, Song Liu, Ronge XingAbstract:Jellyfish Stomolophus Meleagris is a very dangerous animal because of its strong toxicity. However, the composition of the venom is still unclear. Both proteomics and transcriptomics approaches were applied in present study to investigate the major components and their possible relationships to the sting. The proteomics of the venom from S. Meleagris was conducted by tryptic digestion of the crude venom followed by RP-HPLC separation and MS/MS analysis of the tryptic peptides. The venom gland transcriptome was analyzed using a high-throughput Illumina sequencing platform HiSeq (TM) 2000 with de novo assembly. A total of 218 toxins were identified including C-type lectin, phospholipase A(2) (PLA(2)), potassium channel inhibitor, protease inhibitor, metalloprotease, hemolysin and other toxins, most of which should be responsible for the sting. Among them, serine protease inhibitor, PLA(2), potassium channel inhibitor and metalloprotease are predominant, representing 28.44%, 21.56%, 16.06% and 15.14% of the identified venom proteins, respectively. Overall, our combined proteomics and transcriptomics approach provides a systematic overview of the toxins in the venom of jellyfish S. Meleagris and it will be significant to understand the mechanism of the sting.
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isolation and in vitro partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish stomolophus Meleagris
Toxicology in Vitro, 2013Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Jellyfish venom contains various toxins and can cause itching, edema, muscle aches, shortness of breath, blood pressure depression, shock or even death after being stung. Hemolytic protein is one of the most hazardous components in the venom. The present study investigated the hemolytic activity of the nematocyst venom from jellyfish Stomolophus Meleagris. Anion exchange chromatography, DEAE Sepharose Fast Flow, and gel filtration chromatography, Superdex200 had been employed to isolate hemolytic proteins from the nematocyst venom of jellyfish S. Meleagris. Hemolysis of chicken red blood cells was used to quantify hemolytic potency of crude nematocyst venom and chromatography fractions during the purification process. Native-PAGE profile displayed one protein band in the purified hemolytic protein (SmTX); however, two protein bands with apparent molecular weights of similar to 45 kDa and 52 kDa were observed in the reducing SDS-PAGE analysis. Approximately 70 mu g/mL of SmTX caused 50% hemolysis (HU50) of the erythrocyte suspension. The hemolytic activity of SmTX was shown to be temperature and pH dependent, with the optimum temperature and pH being 37 degrees C and pH 5.0. The present study is the first report of isolation and partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish S. Meleagris. The mechanism of the hemolytic activity of SmTX is not clear and deserves further investigation. (C) 2013 Published by Elsevier Ltd.
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isolation identification and characterization of a novel antioxidant protein from the nematocyst of the jellyfish stomolophus Meleagris
International Journal of Biological Macromolecules, 2012Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Reactive oxygen species (ROS) can damage the lipids, proteins and DNA when produced excessively in cells. Here, we describe the isolation and identification of a novel antioxidant protein named SmP90 from the nematocyst of jellyfish Stomolophus Meleagris by 50% ammonium sulfate precipitation and gel filtration chromatography, superdex75. HPLC and SDS-PAGE analysis revealed >95% purity of SmP90 with apparent molecular weight of 90 kDa, approximately. The identification of SmP90 was confirmed by both N-terminal amino acids sequencing, with the sequences of NLDTPYCFYSGDYGG, and peptide mass fingerprint (PMF) analysis by MALDI-TOF-MS. However, no known protein had been completely matched in the database, which indicated that SmP90 might be a novel protein. The antioxidant assay result showed that it had strong superoxide anion radical-scavenging activity with the half-scavenging concentration (EC50) of about 16 mu g/mL. Therefore, the present study is the first time to demonstrate a high efficient method of isolating a novel antioxidant protein from the nematocyst of jellyfish S. Meleagris. (C) 2012 Elsevier B.V. All rights reserved.
David Lecchini - One of the best experts on this subject based on the ideXlab platform.
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Simultaneous production of two kinds of sounds in relation with sonic mechanism in the boxfish Ostracion Meleagris and O. cubicus
Scientific Reports, 2019Co-Authors: Eric Parmentier, Laura Solagna, Frédéric Bertucci, Michael L. Fine, Masanori Nakae, Philippe Compère, Sarah Smeets, Xavier Raick, David LecchiniAbstract:In fishes, sonic abilities for communication purpose usually involve a single mechanism. We describe here the sonic mechanism and sounds in two species of boxfish, the spotted trunkfish Ostracion Meleagris and the yellow boxfish Ostracion cubicus . The sonic mechanism utilizes a T-shaped swimbladder with a swimbladder fenestra and two separate sonic muscle pairs. Extrinsic vertical muscles attach to the vertebral column and the swimbladder. Perpendicularly and below these muscles, longitudinal intrinsic muscles cover the swimbladder fenestra. Sounds are exceptional since they are made of two distinct types produced in a sequence. In both species, humming sounds consist of long series (up to 45 s) of hundreds of regular low-amplitude pulses. Hums are often interspersed with irregular click sounds with an amplitude that is ten times greater in O. Meleagris and forty times greater in O. cubicus . There is no relationship between fish size and many acoustic characteristics because muscle contraction rate dictates the fundamental frequency. We suggest that hums and clicks are produced by either separate muscles or by a combination of the two. The mechanism complexity supports an investment of boxfish in this communication channel and underline sounds as having important functions in their way of life.
Jinhui Cui - One of the best experts on this subject based on the ideXlab platform.
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isolation and in vitro partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish stomolophus Meleagris
Toxicology in Vitro, 2013Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Jellyfish venom contains various toxins and can cause itching, edema, muscle aches, shortness of breath, blood pressure depression, shock or even death after being stung. Hemolytic protein is one of the most hazardous components in the venom. The present study investigated the hemolytic activity of the nematocyst venom from jellyfish Stomolophus Meleagris. Anion exchange chromatography, DEAE Sepharose Fast Flow, and gel filtration chromatography, Superdex200 had been employed to isolate hemolytic proteins from the nematocyst venom of jellyfish S. Meleagris. Hemolysis of chicken red blood cells was used to quantify hemolytic potency of crude nematocyst venom and chromatography fractions during the purification process. Native-PAGE profile displayed one protein band in the purified hemolytic protein (SmTX); however, two protein bands with apparent molecular weights of similar to 45 kDa and 52 kDa were observed in the reducing SDS-PAGE analysis. Approximately 70 mu g/mL of SmTX caused 50% hemolysis (HU50) of the erythrocyte suspension. The hemolytic activity of SmTX was shown to be temperature and pH dependent, with the optimum temperature and pH being 37 degrees C and pH 5.0. The present study is the first report of isolation and partial characterization of hemolytic proteins from the nematocyst venom of the jellyfish S. Meleagris. The mechanism of the hemolytic activity of SmTX is not clear and deserves further investigation. (C) 2013 Published by Elsevier Ltd.
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isolation identification and characterization of a novel antioxidant protein from the nematocyst of the jellyfish stomolophus Meleagris
International Journal of Biological Macromolecules, 2012Co-Authors: Ronge Xing, Song Liu, Yukun Qing, Xiangtao Meng, Jinhui CuiAbstract:Reactive oxygen species (ROS) can damage the lipids, proteins and DNA when produced excessively in cells. Here, we describe the isolation and identification of a novel antioxidant protein named SmP90 from the nematocyst of jellyfish Stomolophus Meleagris by 50% ammonium sulfate precipitation and gel filtration chromatography, superdex75. HPLC and SDS-PAGE analysis revealed >95% purity of SmP90 with apparent molecular weight of 90 kDa, approximately. The identification of SmP90 was confirmed by both N-terminal amino acids sequencing, with the sequences of NLDTPYCFYSGDYGG, and peptide mass fingerprint (PMF) analysis by MALDI-TOF-MS. However, no known protein had been completely matched in the database, which indicated that SmP90 might be a novel protein. The antioxidant assay result showed that it had strong superoxide anion radical-scavenging activity with the half-scavenging concentration (EC50) of about 16 mu g/mL. Therefore, the present study is the first time to demonstrate a high efficient method of isolating a novel antioxidant protein from the nematocyst of jellyfish S. Meleagris. (C) 2012 Elsevier B.V. All rights reserved.
Dongya Y Yang - One of the best experts on this subject based on the ideXlab platform.
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earliest mexican turkeys Meleagris gallopavo in the maya region implications for pre hispanic animal trade and the timing of turkey domestication
PLOS ONE, 2012Co-Authors: Erin Kennedy Thornton, Kitty F Emery, David W Steadman, Camilla Speller, Ray Matheny, Dongya Y YangAbstract:Late Preclassic (300 BC–AD 100) turkey remains identified at the archaeological site of El Mirador (Peten, Guatemala) represent the earliest evidence of the Mexican turkey (Meleagris gallopavo) in the ancient Maya world. Archaeological, zooarchaeological, and ancient DNA evidence combine to confirm the identification and context. The natural pre-Hispanic range of the Mexican turkey does not extend south of central Mexico, making the species non-local to the Maya area where another species, the ocellated turkey (Meleagris ocellata), is indigenous. Prior to this discovery, the earliest evidence of M. gallopavo in the Maya area dated to approximately one thousand years later. The El Mirador specimens therefore represent previously unrecorded Preclassic exchange of animals from northern Mesoamerica to the Maya cultural region. As the earliest evidence of M. gallopavo found outside its natural geographic range, the El Mirador turkeys also represent the earliest indirect evidence for Mesoamerican turkey rearing or domestication. The presence of male, female and sub-adult turkeys, and reduced flight morphology further suggests that the El Mirador turkeys were raised in captivity. This supports an argument for the origins of turkey husbandry or at least captive rearing in the Preclassic.