cyanea kauaulaensis/protease

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Discovery of an Unexplored Protein Structural Scaffold of Serine Protease from Big Blue Octopus (Octopus cyanea): A New Prospective Lead Molecule.

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Serine proteases are a group of enzymes that hydrolyses the peptide bonds in proteins. In mammals, these enzymes help in the regulation of several major physiological functions such as digestion, blood clotting, responses of immune system, reproductive functions and the complement system. Serine

An integrated transcriptomic and proteomic analysis reveals toxin arsenal of a novel Antarctic jellyfish Cyanea sp.

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Jellyfish is a common toxic zooplankton in ocean. We successfully captured a kind of jellyfish 200 m underwater in Antarctica, and identified it as a jellyfish Cyanea sp. through morphological examination and MT-CO1 phylogenetic analysis. A total of 40,468 unigenes were harvested through

Intervention effects of five cations and their correction on hemolytic activity of tentacle extract from the jellyfish Cyanea capillata.

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Cations have generally been reported to prevent jellyfish venom-induced hemolysis through multiple mechanisms by spectrophotometry. Little attention has been paid to the potential interaction between cations and hemoglobin, potentially influencing the antagonistic effect of cations. Here, we

Comparison of haemolytic activity of tentacle-only extract from jellyfish Cyanea capillata in diluted whole blood and erythrocyte suspension: diluted whole blood is a valid test system for haemolysis study.

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In this paper, we utilized two different test systems to compare the haemolysis of tentacle-only extract (TOE) devoid of nematocysts from jellyfish Cyanea capillata, the 1% whole blood and 0.45% erythrocyte suspension approximately with the same erythrocyte concentration from the blood samples of

Unique diversity of sting-related toxins based on transcriptomic and proteomic analysis of the jellyfish Cyanea capillata and Nemopilema nomurai (Cnidaria: Scyphozoa).

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The scyphozoan jellyfish Cyanea capillata and Nemopilema nomurai are common blooming species in China. They possess heterogeneous nematocysts and produce various types of venom that can elicit diverse sting symptoms in humans. However, the differences in venom composition between the two species

Functional Elucidation of Nemopilema nomurai and Cyanea nozakii Nematocyst Venoms' Lytic Activity Using Mass Spectrometry and Zymography.

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Medusozoans utilize explosively discharging penetrant nematocysts to inject venom into prey. These venoms are composed of highly complex proteins and peptides with extensive bioactivities, as observed in vitro. Diverse enzymatic toxins have been putatively identified in the venom of jellyfish,

Combined proteomics and transcriptomics identifies sting-related toxins of jellyfish Cyanea nozakii.

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Jellyfish sting has become a worldwide issue of critical concern to human health and safety in coastal areas in recent decades. Cyanea nozakii is one of the dominant blooming species and dangerous stingers in China. However, it remains unclear how many and what types of toxins are present in the

Combined Proteome and Toxicology Approach Reveals the Lethality of Venom Toxins from Jellyfish Cyanea nozakii.

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Jellyfish are a type of poisonous cnidarian invertebrate that secrete lethal venom for predation or defense. Human beings often become victims of jellyfish stings accidentally while swimming or fishing and suffer severe pain, itching, swelling, inflammation, shock, and even death. Jellyfish venom is

Global Transcriptome Analysis of the Tentacle of the Jellyfish Cyanea capillata Using Deep Sequencing and Expressed Sequence Tags: Insight into the Toxin- and Degenerative Disease-Related Transcripts.

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BACKGROUND Jellyfish contain diverse toxins and other bioactive components. However, large-scale identification of novel toxins and bioactive components from jellyfish has been hampered by the low efficiency of traditional isolation and purification methods. RESULTS We performed de novo

Antimicrobial activity of a newly identified Kazal-type serine proteinase inhibitor, CcKPI1, from the jellyfish Cyanea capillata.

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In this study, we reported a jellyfish-derived Kazal-type serine protease inhibitor, named CcKPI1, from Cyanea capillata. CcKPI1 has a calculated molecular mass of 19.02kDa and contains three typical Kazal domains. Soluble recombinant CcKPI1 (rCcKPI1) was successfully expressed and purified. rCcKPI1

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