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Background The importance of efficient denture deposit removal and oral hygiene has been further underscored by the continuous increase of denture wearers. Denture hygiene management has also become an important aspect associated with denture-induced stomatitis. This study aims to evaluate the denture cleaning effect of arazyme, the metalloprotease produced from the Serratia proteamaculans HY-3. We performed growth inhibition tests against oral opportunistic pathogens to be used as a potential oral health care agent. Methods The proteolytic activities of arazyme was evaluated over broad ranges of temperature, pH, and denture components compared to those of subtilisin in commercially available denture cleansers. The washing effects of arazyme were also measured by using homogeneously soiled EMPA 105 cottons. To investigate the denture cleaning capability of arazyme, artificially contaminated dentures were treated with arazyme, subtilisin (Everlase 6.0T), and Polident®, respectively. The growth kinetics of Candida albicans, Enterococcus faecalis, Staphylococcus epidermis, and Streptococcus mutans were evaluated in the presence of different concentrations of arazyme to estimate the prevention effects of arazyme against major oral opportunistic pathogens. Results Arazyme showed strong proteolytic activities over wide temperature and pH ranges compared with the serine protease of the subtilisin family. Arazyme demonstrated efficient removal and decomposition of artificially contaminated dentures and showed explicit washing effects against soiled cottons. Moreover arazyme inhibited the growth of oral opportunistic pathogens, including C. albicans, E. faecalis, S. epidermis, and S. mutans, with more than 80% inhibition against C. albicans, the major cause of denture stomatitis, with 250 mg/mL arazyme. Conclusions Arazyme shows promise as a biological oral health care agent with effective cleaning and antimicrobial activities and is a potential source for developing novel denture care agents.

Epithelial–mesenchymal transition (EMT) is a key initial step in metastasis for malignant cancer cells to obtain invasive and motile properties. Inhibiting EMT has become a new strategy for cancer therapy. In our previous in vivo study, Nemopilema nomurai jellyfish venom (NnV) -treated HepG2 xenograft mice group showed that E-cadherin expression was strongly detected compared with non-treated groups. Therefore, this study aimed to determine whether NnV could inhibit the invasive and migratory abilities of HepG2 human hepatocellular carcinoma cells and to examine its effect on EMT. Our results revealed that transforming growth factor (TGF)-β1 induced cell morphological changes and downregulated E-cadherin and β-catenin expression, but upregulated N-cadherin and vimentin expression through the Smad and NF-κB pathways in HepG2 cells. Treatment of TGF-β1-stimulated HepG2 cells with NnV reversed the EMT-related marker expression, thereby inhibiting cell migration and invasion. NnV also significantly suppressed the activation of p-Smad3, Smad4, and p-NF-κB in a dose-dependent manner. These data indicated that NnV can significantly suppress cell migration and invasion by inhibiting EMT in HepG2 cells, and therefore might be a promising target for hepatocellular carcinoma therapeutics.

This data article restrains data associated to the Choudhary et al. [1]. Nemopilema nomurai Jellyfish venom (NnV) can lead to cardiac toxicity. Here we analyzed the effect of NnV on rat cardiomyocytes cell line H9c2 at the proteome level using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). This analysis resulted in 34 proteins with differential expression. Here we provide the dataset for the proteins with amplified or reduced level as compare to control.

Nemopilema nomurai is one of the largest species of jellyfish in the world. It blooms mainly offshore of Korea, China, and Japan. Increasing population numbers of N. nomurai is increasing the risk of sea bathers to the jellyfish stings and accompanying envenomations. Cardiovascular effects, and cytotoxicity and hemolytic activities have been previously reported in rodent models. To understand the mechanism of cardiac toxicity, we examined the effect of N. nomurai jellyfish venom (NnV) at the proteome level on rat cardiomyocytes cell line H9c2 using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). Cells treated with NnV displayed dose-dependent inhibition of viability. Cellular changes at proteome level were investigated after 6h and 12h of venom treatment. Electrophoretic examination revealed 72 protein spots displaying significant quantitative changes. These proteins were analyzed by MALDI-TOF/MS. Thirty four differentially expressed proteins were successfully identified; 24 proteins increased in quantity and 10 proteins decreased, compared to the respective controls. Proteins altered in content in Western blot analyses included myosin VII, annexin A2, aldose reductase, suppressor of cytokine signaling 1 (SOCS1), and calumenin, which are well-known marker proteins of cardiac dysfunctions. BIOLOGICAL SIGNIFICANCE: This is the first report revealing the cardiac toxicity of NnV at the proteome level. NnV directly targeted proteins involved in cardiac dysfunction or maintenance. Suppressor of cytokine signaling 1 (SOCS1), which inhibits the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway, was upregulated by NnV. Other proteins related to cardiac arrest that were over-expressed included aldose reductase and calumenin. These results clarify the underlying mechanism of cardiomyocyte damage caused by NnV. By inhibiting these particular targets and more precisely identifying the components of NnV-mediated cardiac toxicity, jellyfish venom-associated poisoning could be reduced or prevented. Language: en

Background: Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. Methods: To determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with fibrinolytic activity were obtained by DEAE cation exchange column. Results: NnV displayed fibrinolytic activities with molecular masses of approximately 70, 35, 30, and 28 kDa. The fibrinolytic activity of NnV was completely obliterated by phenylmethylsulfonyl fluoride, a prototype serine protease inhibitor. Based on amidolytic assays using chromogenic substrates specific for various kinds of serine proteases, NnV predominantly manifested a chymotrypsin-like feature. Its activity was completely eliminated at low pH (< 6) and high temperatures (> 37 °C). Some metal ions (Co2+, Cu2+, Zn2+ and Ni2+) strongly suppressed its fibrinolytic activity, while others (Ca2+ and Mg2+) failed to do so. Isolation of a serine protease with fibrionolytic activity from NnV revealed that only p3 showed the fibrinolytic activity, which was completely inhibited by PMSF. Conclusion: The present study showed that N. nomurai jellyfish venom has a chymotrypsin-like serine protease with fibrinolytic activity. Such information might be useful for developing clinical management of jellyfish envenomation and pharmacological agents with therapeutic potential for thrombotic diseases in the future.

Bee venom (BV) has long been used in traditional Eastern and Western medicine for chronic inflammation, pain and skin therapy. Human exposure to BV, however, often causes unwanted adverse effects and is even fatal in some cases. Phospholipase A2 (PLA2) of BV is now suspected to play a key role in these adverse effects. We investigated the potential use of PLA2-free bee venom (PBV) as a replacement for BV in cosmetic products. PBV prepared by molecular weight cut-off ultrafiltration exhibits a superior profile in comparison with regular BV, by inhibiting elastase activity and suppressing the induction of nitric oxide (NO) and metalloproteinase-9 (MMP-9), while retaining the effects of cell proliferation and protection against ultraviolet B (UVB)-induced damage in human dermal fibroblast cells. PBV thus appears to be more promising than BV as a cosmetic ingredient with a reduced potential for adverse reactions in the recipient.

The use of bee venom (Apis mellifera L., BV) occasionally causes side effects such as inflammation and allergic reactions in the recipients. Several case reports also suggested the treatment of BV has some limitations in its clinical uses, due to the occurrence of dermal necrosis and anaphylatic reactions. It is generally understood that bee venom allergy is mainly the result of its allergic component, phospholipase A2 (PLA2). The present study was aimed to generate PLA2-free bee venom (PBV) and evaluate its efficacy as skin care and cosmetic preparation, comparing with original bee venom (BV). Our results showed that both BV and PBV exhibited significant protective effects in UVB-irradiated human keratinocyte (HaCaT) and human dermal fibroblast (HDF) cells and they also induced type I collagen synthesis in UVB-irradiated HDF cells except BV at 3 μg/ml. Furthermore, BV and PBV showed the inhibition of UVB-stimulated matrix metalloproteinase-1 (MMP-1), a major collagen degrading enzyme in skin. However, BV, unlike PBV, exhibited strong cytotoxicities in skin cells (both HaCaT and HDF) at its working concentrations of anti-wrinkle effect. The underlying cell signaling mechanisms of anti-wrinkle effects of BV and PBV were demonstrated by the activation of ERK1/2, and p38. Conclusively, PBV appears to be the bee venom of choice with less cytotoxicity and higher efficacy on UVB-irradiated skin cells in comparison with original bee venom (BV). Therefore, PBV can better be used as a cosmetic ingredient exhibiting excellent anti-wrinkle effect against photoaging than original BV.

An enzyme in a nematocyst extract of the Nemopilema nomurai jellyfish, caught off the coast of the Republic of Korea, catalyzed the cleavage of chymotrypsin substrate in an amidolytic kinetic assay, and this activity was inhibited by the serine protease inhibitor, phenylmethanesulfonyl fluoride. We isolated the full-length cDNA sequence of this enzyme, which contains 850 nucleotides, with an open reading frame of 801 encoding 266 amino acids. A blast analysis of the deduced amino acid sequence showed 41% identity with human chymotrypsin-like (CTRL) and the CTRL-1 precursor. Therefore, we designated this enzyme N. nomurai CTRL-1. The primary structure of N. nomurai CTRL-1 includes a leader peptide and a highly conserved catalytic triad of His(69), Asp(117), and Ser(216). The disulfide bonds of chymotrypsin and the substrate-binding sites are highly conserved compared with the CTRLs of other species, including mammalian species. Nemopilema nomurai CTRL-1 is evolutionarily more closely related to Actinopterygii than to Scyphozoan (Aurelia aurita) or Hydrozoan (Hydra vulgaris). The N. nomurai CTRL1 was amplified from the genomic DNA with PCR using specific primers designed based on the full-length cDNA, and then sequenced. The N. nomurai CTRL1 gene contains 2434 nucleotides and four distinct exons. The 5' donor splice (GT) and 3' acceptor splice sequences (AG) are wholly conserved. This is the first report of the CTRL1 gene and cDNA structures in the jellyfish N. nomurai.

Rumex japonicusHoutt. is traditionally used as a medicinal plant to treat patients suffering from skin disease in Korea. However, the beneficial effect ofRumex japonicusHoutt. on hair growth has not been thoroughly examined. Therefore, the present study aims to investigate the hair growth-promoting effect ofRumex japonicus(RJ) Houtt. root extract using human dermal papilla cells (DPCs), HaCaT cells, and C57BL/6 mice model. RJ induced antiapoptotic and proliferative effects on DPCs and HaCaT cells by increasing Bcl-2/Bax ratio and activating cellular proliferation-related proteins, ERK and Akt. RJ also increasedβ-catenin via the inhibition of GSK-3β. In C57BL/6 mice model, RJ promoted the anagen induction and maintained its period. Immunohistochemistry analysis demonstrated that RJ upregulated Ki-67 andβ-catenin expressions, suggesting that the hair growth effect of RJ may be mediated through the reinforcement of hair cell proliferation. These results provided important insights for the possible mechanism of action of RJ and its potential as therapeutic agent to promote hair growth.