In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai

Bae, Seong Kyeong; Lee, Hyunkyoung; Heo, Yunwi; Pyo, Min Jung; Choudhary, Indu; Han, Chang Hoon; Yoon, Won Duk; Kang, Changkeun; Kim, Euikyung

doi:10.1186/s40409-017-0125-8

Cited by 9 publications

(5 citation statements)

References 39 publications

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“…By functional assay (using fibrinolytic activity in zymography assay), Bae et al [ 99 ] reported venom proteins of Nemopilema nomurai as characterized by MW of approximately 70, 35, 30, and 28 kDa. These authors compared N. nomurai with Aurelia aurita venoms, with similar banding patterns, distributed in 60–80 kDa and 25–37 kDa size bands, and with the siphonophoran Physalia physalis venom, with MW > 25 kDa.…”

Section: Resultsmentioning

confidence: 99%

Barrel Jellyfish (Rhizostoma pulmo) as Source of Antioxidant Peptides

et al. 2019

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The jellyfish Rhizostoma pulmo, Macrì 1778 (Cnidaria, Rhizostomae) undergoes recurrent outbreaks in the Mediterranean coastal waters, with large biomass populations representing a nuisance or damage for marine and maritime activities. A preliminary overview of the antioxidant activity (AA) of R. pulmo proteinaceous compounds is provided here based on the extraction and characterization of both soluble and insoluble membrane-fractioned proteins, the latter digested by sequential enzymatic hydrolyses with pepsin and collagenases. All jellyfish proteins showed significant AA, with low molecular weight (MW) proteins correlated with greater antioxidant activity. In particular, collagenase-hydrolysed collagen resulted in peptides with MW lower than 3 kDa, ranging 3–10 kDa or 10–30 kDa, with AA inversely proportional to MW. No cytotoxic effect was detected on cultured human keratinocytes (HEKa) in a range of protein concentration 0.05–20 μg/mL for all tested protein fractions except for soluble proteins higher than 30 kDa, likely containing the jellyfish venom compounds. Furthermore, hydrolyzed jellyfish collagen peptides showed a significantly higher AA and provided a greater protective effect against oxidative stress in HEKa than the hydrolyzed collagen peptides from vertebrates. Due to a high reproductive potential, jellyfish may represent a potential socioeconomic opportunity as a source of natural bioactive compounds, with far-reaching beneficial implications. Eventually, improvements in processing technology will promote the use of untapped marine biomasses in nutraceutical, cosmeceutical, and pharmaceutical fields, turning marine management problems into a more positive perspective.

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Section: Resultsmentioning

confidence: 99%

Barrel Jellyfish (Rhizostoma pulmo) as Source of Antioxidant Peptides

et al. 2019

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“…The chromatography on DEAE-sepharose at pH = 10.0 has revealed the presence of active enzymes with a molecular weight of more than 45 kDa. Given our previous results on the presence in the tissues of hydrobionts of enzymes capable of cleaving fibrinogen [12], as well as the result of Bae et al [13], which revealed a chymotrypsin-like serine protease with fibrinolytic activity in the venom of jellyfish, all obtained fractions were tested by enzyme-electrophoresis with fibrinogen. To date, the search for available sources of fibrino(geno) lytic enzymes is quite relevant.…”

Section: Resultsmentioning

confidence: 99%

Isolation and partial characterization of serine proteases from jellyfish of the Antarctic region

Raksha¹,

Halenova²,

Vovk³

et al. 2022

J App Biol Biotech

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The growing demand for industrial proteases and enzyme-containing products substantiates the search for costeffective sources of enzymes. The aim of current research was to find a one-step approach for the isolation of the fraction of serine proteases from the jellyfish of the Antarctic region. Given our data, ion-exchange chromatography on diethylaminoethyl-sepharose carboxymethyl-sepharose was ineffective, in contrast to affinity chromatography on benzamidine-sepharose. The isolated fraction consists of enzymes with a molecular weight of more than 30 kDa and isoelectric points at pH = 3.0; 5.0-6.0 and pH = 9.0, which can break down gelatin, casein, and fibrinogen. The maximal proteolytic activity was found at pH = 12.0 and a temperature of +55°C. Serine proteases showed activity against the chromogenic substrate for trypsin and had no activity against substrates for chymotrypsin and elastase indicating that enzymes are trypsin-like proteases. The presence of enzymes with fibrino(geno)lytic activity and the ability of serine proteases from jellyfish to work at high pH and temperatures suggest their potential use as thrombolytics, as well as agents in the industries requiring a highly alkaline conditions.

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“…Rhizoprotease, a new metalloproteinase of 95 kDa, was isolated in the venom [ 61 ]. Nemopilema nomurai (scyphozoan) venom contains a chymotrypsin-like serine protease with fibrinolytic activity [ 62 ]. Aurelia aurita shows strong fibrinogenolytic activity [ 63 ].…”

Section: Pathophysiologymentioning

confidence: 99%

Raising Awareness on the Clinical and Forensic Aspects of Jellyfish Stings: A Worldwide Increasing Threat

Cunha

Dinis-Oliveira

2022

IJERPH

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Jellyfish are ubiquitous animals registering a high and increasing number of contacts with humans in coastal areas. These encounters result in a multitude of symptoms, ranging from mild erythema to death. This work aims to review the state-of-the-art regarding pathophysiology, diagnosis, treatment, and relevant clinical and forensic aspects of jellyfish stings. There are three major classes of jellyfish, causing various clinical scenarios. Most envenomations result in an erythematous lesion with morphological characteristics that may help identify the class of jellyfish responsible. In rare cases, the sting may result in delayed, persistent, or systemic symptoms. Lethal encounters have been described, but most of those cases happened in the Indo-Pacific region, where cubozoans, the deadliest jellyfish class, can be found. The diagnosis is mostly clinical but can be aided by dermoscopy, skin scrapings/sticky tape, confocal reflectance microscopy, immunological essays, among others. Treatment is currently based on preventing further envenomation, inactivating the venom, and alleviating local and systemic symptoms. However, the strategy used to achieve these effects remains under debate. Only one antivenom is currently used and covers merely one species (Chironex fleckeri). Other antivenoms have been produced experimentally but were not tested on human envenomation settings. The increased number of cases, especially due to climate changes, justifies further research in the study of clinical aspects of jellyfish envenoming.

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In vitro characterization of jellyfish venom fibrin(ogen)olytic enzymes from Nemopilema nomurai

Cited by 9 publications

References 39 publications

Barrel Jellyfish (Rhizostoma pulmo) as Source of Antioxidant Peptides

Barrel Jellyfish (Rhizostoma pulmo) as Source of Antioxidant Peptides

Isolation and partial characterization of serine proteases from jellyfish of the Antarctic region

Raising Awareness on the Clinical and Forensic Aspects of Jellyfish Stings: A Worldwide Increasing Threat

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