PURPOSE: Wound represents a major health challenge as they consume a large amount of healthcare resources to improve patient's quality of life. Many scientific studies have been conducted in search of ideal biomaterials with wound-healing activity for clinical use and collagen has been proven to be a suitable candidate biomaterial. This study intended to investigate the wound healing activity of collagen peptides derived from jellyfish following oral administration. METHODS: In this study, collagen was extracted from the jellyfish--Rhopilema esculentum using 1% pepsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and fourier transform infrared (FTIR) were used to identify and determine the molecular weight of the jellyfish collagen. Collagenase II, papain and alkaline proteinase were used to breakdown jellyfish collagen into collagen peptides. Wound scratch assay (in vitro) was done to determine migration potential of human umbilical vein endothelial cells (HUVEC) covering the artificial wound created on the cell monolayer following treatment with collagen peptides. In vivo studies were conducted to determine the effects of collagen peptides on wound healing by examining wound contraction, re-epithelialization, tissue regeneration and collagen deposition on the wounded skin of mice. Confidence level (p < 0.05) was considered significant using GraphPad Prism software. RESULTS: The yield of collagen was 4.31%. The SDS-PAGE and FTIR showed that extracted collagen from jellyfish was type I. Enzymatic hydrolysis of this collagen using collagenase II produced collagen peptides (CP) and hydrolysis with alkaline proteinase/papain resulted into collagen peptides (CP). Tricine SDS-PAGE revealed that collagen peptides consisted of protein fragments with molecular weight <25 kDa. Wound scratch assay showed that there were significant effects on the scratch closure on cells treated with collagen peptides at a concentration of 6.25 μg/mL for 48 h as compared to the vehicle treated cells. Overall treatment with collagen peptide on mice with full thickness excised wounds had a positive result in wound contraction as compared with the control. Histological assessment of peptides treated mice models showed remarkable sign of re-epithelialization, tissue regeneration and increased collagen deposition. Immunohistochemistry of the skin sections showed a significant increase in β-fibroblast growth factor (β-FGF) and the transforming growth factor-β (TGF-β) expression on collagen peptides treated group. CONCLUSION Collagen peptides derived from the jellyfish-Rhopilema esculentum can accelerate the wound healing process thus could be a therapeutic potential product that may be beneficial in wound clinics in the future.
Administration, Oral ; Animals ; Collagen ; administration & dosage ; isolation & purification ; metabolism ; pharmacology ; Fibroblast Growth Factors ; metabolism ; Human Umbilical Vein Endothelial Cells ; Humans ; Male ; Regeneration ; Scyphozoa ; chemistry ; Skin ; metabolism ; Skin Physiological Phenomena ; Stimulation, Chemical ; Transforming Growth Factor beta1 ; metabolism ; Wound Healing ; drug effects

Seabather's eruption (SBE) is characterized by pruritic erythematous papules on the covered areas of the body that appear within 24 hours after exposure to seawater. SBE is known to be caused by the planula of a thimble jellyfish (Linuche unguiculata) or a sea anemone (Edward siellalineata). We report cases of two adult male triathletes who developed pruritic erythematous papules on the chest and back after a swim training along the coastal waters of Samal island, Davao City. Examination of samples of the seawater revealed multiple planulae or larval forms of cnidarians. The histopathologic examination revealed moderately dense superficial and deep perivascular and periadnexal inflammatory infiltrates consisting predominantly of lymphocytes, few eosinophils and neutrophils. Treatment with a short course of systemic corticosteroids proved beneficial in both patients. A review of published literature regarding this interesting aquatic sports dermatosis was also conducted.

Human ; Male ; Adult ; Adrenal Cortex Hormones ; Eosinophils ; Lymphocytes ; Neutrophils ; Scyphozoa ; Sea Anemones ; Seawater ; Skin Diseases

In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an "accessory protein" whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an "antenna protein" altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca(2+)-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of Xray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.
Animals ; Anthozoa ; physiology ; Aquatic Organisms ; physiology ; Bacteria ; metabolism ; Binding Sites ; Calcium ; metabolism ; Crystallography, X-Ray ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins ; metabolism ; Hydrozoa ; physiology ; Imidazoles ; metabolism ; Luciferases ; metabolism ; Luminescent Measurements ; instrumentation ; methods ; Luminescent Proteins ; metabolism ; Models, Molecular ; Protein Binding ; Pteridines ; metabolism ; Pyrazines ; metabolism ; Scyphozoa ; physiology ; Spectrometry, Fluorescence

Tetracycline repressor gene (tetR) from E. coli transposon Tn10 was fused in frame with green fluorescent protein gene (gfp) from jellyfish Aequorea Victoria on an E. coli expression vector and the fusion protein (TR::GFP) was purified. The binding of TR::GFP with tetracycline (tc) was demonstrated by nitrocellulose filter binding assay. TR::GFP also maintained the fluorescence property of GFP. Most significantly, fluorescence emission intensity of TR::GFP increased by 2-fold in the presence of tc, from 1.132 to 2.214, while those of GFP and TetR showed little change under similar conditions. The results indicated TR::GFP possesses characteristics of a tetracycline biosensor.
Animals ; Bacterial Proteins ; biosynthesis ; genetics ; Carrier Proteins ; biosynthesis ; genetics ; Escherichia coli ; genetics ; metabolism ; Genetic Vectors ; genetics ; Green Fluorescent Proteins ; biosynthesis ; genetics ; isolation & purification ; Humans ; Recombinant Fusion Proteins ; biosynthesis ; genetics ; isolation & purification ; Repressor Proteins ; biosynthesis ; chemistry ; genetics ; Scyphozoa ; chemistry ; Spectrometry, Fluorescence ; Tetracycline ; metabolism ; Tetracycline Resistance