Fish collagen for skin wound healing: a systematic review in experimental animal studies

Souza, Amanda de; Cruz, Matheus de Almeida; Araújo, Tiago Akira Tashiro de; Parisi, Júlia Risso; Vale, Giovanna Caroline Aparecida do; Sousa, Karolyne dos Santos Jorge; Ribeiro, Daniel Araki; Granito, Renata Neves; Rennó, Ana Cláudia Muniz

doi:10.1007/s00441-022-03625-w

Cited by 13 publications

(6 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Also, the tilapia fish skin xenografts have demonstrated good efficacy in treating full-thickness skin wounds in animals [ 31 ] and burn wounds in phase II and phase III randomized controlled trials, which led to complete wound reepithelialization, improved burn-related pain, and decreased treatment-related costs [ 32 , 33 ]. Moreover, a systematic review showed that fish skin collagen can improve the wound-healing rate and reepithelization in animal studies [ 34 ]. In this study, we generated the wound dressing by a freeze-drying FC solution into a scaffold without physical or chemical crosslinking.…”

Section: Discussionmentioning

confidence: 99%

Assessment of Tilapia Skin Collagen for Biomedical Research Applications in Comparison with Mammalian Collagen

Huang,

Wong,

et al. 2024

Molecules

View full text Add to dashboard Cite

Collagen is an important material for biomedical research, but using mammalian tissue-derived collagen carries the risk of zoonotic disease transmission. Marine organisms, such as farmed tilapia, have emerged as a safe alternative source of collagen for biomedical research. However, the tilapia collagen products for biomedical research are rare, and their biological functions remain largely unexamined. In this study, we characterized a commercial tilapia skin collagen using SDS-PAGE and fibril formation assays and evaluated its effects on skin fibroblast adhesion, proliferation, and migration, comparing it with commercial collagen from rat tails, porcine skin, and bovine skin. The results showed that tilapia skin collagen is a type I collagen, similar to rat tail collagen, and has a faster fibril formation rate and better-promoting effects on cell migration than porcine and bovine skin collagen. We also confirmed its application in a 3D culture for kidney cells’ spherical cyst formation, fibroblast-induced gel contraction, and tumor spheroid interfacial invasion. Furthermore, we demonstrated that the freeze-dried tilapia skin collagen scaffold improved wound closure in a mouse excisional wound model, similar to commercial porcine or bovine collagen wound dressings. In conclusion, tilapia skin collagen is an ideal biomaterial for biomedical research.

show abstract

Section: Discussionmentioning

confidence: 99%

Assessment of Tilapia Skin Collagen for Biomedical Research Applications in Comparison with Mammalian Collagen

Huang,

Wong,

et al. 2024

Molecules

View full text Add to dashboard Cite

show abstract

“…Two milligrams of collagen extracted from the sea eel swim bladder (diluted at a ratio of 1:100) was mixed with dried KBr powder in a dry and clean agate mortar, ground unidirectionally [38], and subsequently pressed into tablets using a mold. The FTIR analysis involved recording the spectrum over a wave number range of 400~4000 cm −1 at a resolution of 4 cm −1 with 40 scans accumulated.…”

Section: Ftir Spectroscopymentioning

confidence: 99%

Preparation of Enzyme-Soluble Swim Bladder Collagen from Sea Eel (Muraenesox cinereus) and Evaluation Its Wound Healing Capacity

Li,

Tian,

Cao

et al. 2023

Marine Drugs

View full text Add to dashboard Cite

In the present research, the enzyme-facilitated collagen from sea eel (Muraenesox cinereus) swim bladder was isolated, and the collagen characteristics were analyzed. Then, the collagen sponge was prepared and its potential mechanism in promoting skin wound healing in mice was further investigated. Collagen was obtained from the swim bladder of sea eels employing the pepsin extraction technique. Single-factor experiments served as the basis for the response surface method (RSM) to optimize pepsin concentration, solid-liquid ratio, and hydrolysis period. With a pepsin concentration of 2067 U/g, a solid-liquid ratio of 1:83 g/mL, and a hydrolysis period of 10 h, collagen extraction achieved a yield of 93.76%. The physicochemical analysis revealed that the extracted collagen belonged to type I collagen, and the collagen sponge displayed a fibrous structure under electron microscopy. Furthermore, in comparison to the control group, mice treated with collagen sponge dressing exhibited elevated activities of superoxide dismutase (SOD), catalase (CAT), total antioxidant capacity (T-AOC), and glutathione peroxidase (GSH-Px), and decreased levels of malondialdehyde (MDA), interleukin (IL)-1β, interleukin (IL)-6, and tumor necrosis factor (TNF)-α. The collagen sponge dressing effectively alleviated inflammation in the wound area, facilitating efficient repair and rapid healing of the skin tissue. During the initial phase of wound healing, the group treated with collagen sponge dressing exhibited an enhancement in the expressions of cluster of differentiation (CD)31, epidermal growth factor (EGF), transforming growth factor (TGF)-β1, and type I collagen, leading to an accelerated rate of wound healing. In addition, this collagen sponge dressing could also downregulate the expressions of CD31, EGF, and type I collagen to prevent scar formation in the later stage. Moreover, this collagen treatment minimized oxidative damage and inflammation during skin wound healing and facilitated blood vessel formation in the wound. Consequently, it exhibits significant potential as an ideal material for the development of a skin wound dressing.

show abstract

“…The following supporting information can be downloaded at: https:// www.mdpi.com/article/10.3390/ma15248802/s1, Supplementary Material A: Cross-linking Method of Collagen (Col) (Page 1); Supplemenrary Material B: Tissue Engineering and Therapeutic Effects of b-FGF (Page 2); Supplementary Material C: Self-Preparation of Collagen (Col) Membranes (Pages 3-6). References [14][15][16][17] were cited in Supplementary Material A, References [28][29][30][31][32][33][34] were cited in Supplementary Materials B, and References [49,[54][55][56][57][58][59][60][61][62][63][64][65][66][67][68][69][70][71][72][73]…”

Section: Supplementary Materialsmentioning

confidence: 99%

“…The Col membrane was very important in assisting in forming bones by Col/Hap composite granules and was self-prepared in this study. Its usage, preparation method, and characterization are mentioned in Supplementary Material C: Self-Preparation of Collagen (Col) Membranes (Supplementary Materials) [49,[54][55][56][57][58][59][60][61][62][63][64][65][66][67][68][69][70][71][72][73]. The formed Col membranes were employed in animal studies, which are explained later.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Collagen/Hydroxyapatite Composites Using the Alternate Immersion Method and Evaluation of the Cranial Bone-Forming Capability of Composites Complexed with Acidic Gelatin and b-FGF

et al. 2022

View full text Add to dashboard Cite

Bone-substitute materials are essential in dental implantology. We prepared collagen (Col)/hydroxyapatite (Hap)/acidic gelatin (AG)/basic fibroblast growth factor (b-FGF) constructs with enhanced bone-forming capability. The Col/Hap apatite composites were prepared by immersing Col sponges alternately in calcium and phosphate ion solutions five times, for 20 and 60 min, respectively. Then, the sponges were heated to 56 °C for 48 h. Scanning electron microscopy/energy-dispersive X-ray spectroscopy, Fourier-transform infrared spectroscopy, and X-ray diffraction analyses showed that the Col/Hap composites contained poorly crystalline Hap precipitates on the Col matrix. Col/Hap composite granules were infiltrated by AG, freeze-dried, and immersed in b-FGF solution. The wet quaternary constructs were implanted in rat cranial bone defects for 8 weeks, followed by soft X-ray measurements and histological analysis. Animal studies have shown that the constructs moderately increase bone formation in cranial bone defects. We found that an alternate immersion time of 20 min led to the greatest bone formation (p < 0.05). Constructs placed inside defects slightly extend the preexisting bone from the defect edges and lead to the formation of small island-like bones inside the defect, followed by disappearance of the constructs. The combined use of Col, Hap, AG, and b-FGF might bring about novel bone-forming biomaterials.

show abstract

Fish collagen for skin wound healing: a systematic review in experimental animal studies

Cited by 13 publications

References 60 publications

Assessment of Tilapia Skin Collagen for Biomedical Research Applications in Comparison with Mammalian Collagen

Assessment of Tilapia Skin Collagen for Biomedical Research Applications in Comparison with Mammalian Collagen

Preparation of Enzyme-Soluble Swim Bladder Collagen from Sea Eel (Muraenesox cinereus) and Evaluation Its Wound Healing Capacity

Preparation of Collagen/Hydroxyapatite Composites Using the Alternate Immersion Method and Evaluation of the Cranial Bone-Forming Capability of Composites Complexed with Acidic Gelatin and b-FGF

Contact Info

Product

Resources

About