In vitro angiotensin I converting enzyme inhibition by a peptide isolated from Chiropsalmus quadrigatus Haeckel (box jellyfish) venom hydrolysate

So, Pamela Berilyn; Rubio, Peter Yuosef M.; Lirio, Stephen; Macabeo, Allan Patrick G.; Huang, Hsi‐Ya; Corpuz, Mary Jho-Anne T; Villaflores, Oliver B.

doi:10.1016/j.toxicon.2016.04.050

Cited by 23 publications

(13 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ACE‐inhibitory activity was measured by ACE‐kit WST (Dojindo, Kumamoto, Japan) described previously and expressed in terms of half maximal inhibitory concentration (IC 50 ) values.…”

Section: Methodsmentioning

confidence: 99%

A Novel Antihypertensive Peptide Identified in Thermolysin‐Digested Rice Bran

Shobako

Ogawa

Ishikado

et al. 2018

Molecular Nutrition Food Res

View full text Add to dashboard Cite

show abstract

“…ACE‐inhibitory activity was measured by ACE‐kit WST (Dojindo, Kumamoto, Japan) described previously and expressed in terms of half maximal inhibitory concentration (IC 50 ) values.…”

Section: Methodsmentioning

confidence: 99%

A Novel Antihypertensive Peptide Identified in Thermolysin‐Digested Rice Bran

Shobako

Ogawa

Ishikado

et al. 2018

Molecular Nutrition Food Res

View full text Add to dashboard Cite

show abstract

“…Aurelia aurita venom has shown anticoagulant effect through strong fibrinogenolytic activity, by cleaving the Aα and Bβ chains of the fibrinogen molecule 11 . Chiropsalmus quadrigatus Haeckel venom has an active peptide with potential anti-angiotensin I-converting enzymatic activity 12 . Nemopilema nomurai is one of the largest jellyfish species and can grow up to a bell diameter of 2 m and weigh up to 200 kg.…”

Section: Introductionmentioning

confidence: 99%

Nemopilema nomurai jellyfish venom exerts an anti-metastatic effect by inhibiting Smad- and NF-κB-mediated epithelial–mesenchymal transition in HepG2 cells

Lee

Pyo

Bae

et al. 2018

Sci Rep

View full text Add to dashboard Cite

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.

show abstract

“…Extraction and hydrolysis with pepsin and papain of the tentacles of the jellyfish provided bioactive peptides. From further bioassay-guided fractionation, purification, and sequence analysis, a peptide with the sequence Ala-Cys-Pro-Gly-Pro-Asn-Pro-Gly-Arg-Pro was found to show ACE inhibitory action in vitro with an IC 50 value of 2.03 μM [81]. …”

Section: Classification Of Marine Resourcesmentioning

confidence: 99%

Peptides, Peptidomimetics, and Polypeptides from Marine Sources: A Wealth of Natural Sources for Pharmaceutical Applications

2017

View full text Add to dashboard Cite

Nature provides a variety of peptides that are expressed in most living species. Evolutionary pressure and natural selection have created and optimized these peptides to bind to receptors with high affinity. Hence, natural resources provide an abundant chemical space to be explored in peptide-based drug discovery. Marine peptides can be extracted by simple solvent extraction techniques. The advancement of analytical techniques has made it possible to obtain pure peptides from natural resources. Extracted peptides have been evaluated as possible therapeutic agents for a wide range of diseases, including antibacterial, antifungal, antidiabetic and anticancer activity as well as cardiovascular and neurotoxin activity. Although marine resources provide thousands of possible peptides, only a few peptides derived from marine sources have reached the pharmaceutical market. This review focuses on some of the peptides derived from marine sources in the past ten years and gives a brief review of those that are currently in clinical trials or on the market.

show abstract

In vitro angiotensin I converting enzyme inhibition by a peptide isolated from Chiropsalmus quadrigatus Haeckel (box jellyfish) venom hydrolysate

Cited by 23 publications

References 31 publications

A Novel Antihypertensive Peptide Identified in Thermolysin‐Digested Rice Bran

A Novel Antihypertensive Peptide Identified in Thermolysin‐Digested Rice Bran

Nemopilema nomurai jellyfish venom exerts an anti-metastatic effect by inhibiting Smad- and NF-κB-mediated epithelial–mesenchymal transition in HepG2 cells

Peptides, Peptidomimetics, and Polypeptides from Marine Sources: A Wealth of Natural Sources for Pharmaceutical Applications

Contact Info

Product

Resources

About