Elastin hydrolysate derived from fish enhances proliferation of human skin fibroblasts and elastin synthesis in human skin fibroblasts and improves the skin conditions

Sugawara, Eri; Nakaba, Misako; Yamada, Michio

doi:10.1002/jsfa.7270

Cited by 26 publications

(19 citation statements)

References 28 publications

(45 reference statements)

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“…On the other hand, histidine was absent in the jumbo squid’s skin elastin. Nakaba et al [ 34 ] analyzed the amino acid composition in whole and hydrolyzed elastin peptide from the bulbus arteriosus of Pacific yellowtail ( Seriola quiqueradiata ), while Shiratsuchi et al [ 18 ] performed a similar evaluation on bulbus arteriosus of skipjack tuna elastin hydrolysate. In both cases, the glycine and proline levels found in the fish elastin were higher, which was around 40% and 10%, respectively, than those measured in this present study.…”

Section: Resultsmentioning

confidence: 99%

“…In rare cases, bovine elastin has been linked to diseases such as bovine spongiform encephalopathy (BSE), and porcine elastin is severely forbidden in Judaism and Islam. Thus, elastin has also been extracted from marine animals like fish aorta [ 18 ] and jumbo squid skin [ 5 ]. Properties of elastin could vary depending on the habitat, species, and part of the body it is isolated from, demanding a need for characterization of this protein from different sources.…”

Section: Introductionmentioning

confidence: 99%

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Characterization and Toxicity Evaluation of Broiler Skin Elastin for Potential Functional Biomaterial in Tissue Engineering

Kamaruzaman

Yusop

2022

Polymers

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Broiler skin, a by-product of poultry processing, has been proven to contain essential elastin, a high-value protein with many applications. The present study reported the extraction of water-soluble elastin from broiler skin by using sodium chloride (NaCl), sodium hydroxide (NaOH), and oxalic acid treatment before freeze-drying. Chemical characterization such as protein and fat content, Fourier-transform infrared (FTIR) spectroscopy, amino acid composition and thermal gravimetric analysis (TGA) were performed and compared with commercial elastin from bovine neck ligament. The resultant elastin’s toxicity was analyzed using an MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) tetrazolium assay and primary skin irritation test. Results showed a high quality of the extracted-elastin with the presence of a high amount of proline (6.55 ± 0.40%) and glycine (9.65 ± 0.44%), low amount of hydroxyproline (0.80 ± 0.32%), methionine (2.04 ± 0.05%), and histidine (1.81 ± 0.05%) together with calculated 0.56 isoleucine/leucine ratio. FTIR analysis showed the presence of typical peaks of amide A, B, I, and II for protein with high denaturation temperature around 322.9 °C. The non-toxic effect of the extracted elastin was observed at a concentration lower than 0.5 mg/mL. Therefore, water-soluble elastin powder extracted from broiler skin can be an alternative source of elastin as a biomaterial for tissue engineering applications.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization and Toxicity Evaluation of Broiler Skin Elastin for Potential Functional Biomaterial in Tissue Engineering

Kamaruzaman

Yusop

2022

Polymers

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“…Collagen I has been extracted from various marine sources such as fish skin, jellyfish, sponges and squid ( Figure 2 ) [ 70 , 71 , 108 , 109 , 110 , 111 , 112 , 113 , 114 , 115 , 116 ]. Marine-derived collagen I was shown to promote wound healing in experimental (rodent models) and clinical studies [ 117 , 118 , 119 ].…”

Section: Collagen Formats and Applications In Wound Healingmentioning

confidence: 99%

Collagen in Wound Healing

2021

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Normal wound healing progresses through inflammatory, proliferative and remodeling phases in response to tissue injury. Collagen, a key component of the extracellular matrix, plays critical roles in the regulation of the phases of wound healing either in its native, fibrillar conformation or as soluble components in the wound milieu. Impairments in any of these phases stall the wound in a chronic, non-healing state that typically requires some form of intervention to guide the process back to completion. Key factors in the hostile environment of a chronic wound are persistent inflammation, increased destruction of ECM components caused by elevated metalloproteinases and other enzymes and improper activation of soluble mediators of the wound healing process. Collagen, being central in the regulation of several of these processes, has been utilized as an adjunct wound therapy to promote healing. In this work the significance of collagen in different biological processes relevant to wound healing are reviewed and a summary of the current literature on the use of collagen-based products in wound care is provided.

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“…Elastin hydrolysate and EP stimulate the proliferation of fibroblasts and SMC (Chatron-Colliet et al, 2015; Shiratsuchi et al, 2016) and enhance angiogenesis (Robinet et al, 2005). EP stimulate production of some MMPs (Robinet et al, 2005; Duca et al, 2007) and decrease elastin synthesis (Wachi et al, 1995).…”

Section: Regulatory Role Of Elastinmentioning

confidence: 99%

Elastin in the Liver

Kanta

2016

Front. Physiol.

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A characteristic feature of liver cirrhosis is the accumulation of large amounts of connective tissue with the prevailing content of type I collagen. Elastin is a minor connective tissue component in normal liver but it is actively synthesized by hepatic stellate cells and portal fibroblasts in diseased liver. The accumulation of elastic fibers in later stages of liver fibrosis may contribute to the decreasing reversibility of the disease with advancing time. Elastin is formed by polymerization of tropoelastin monomers. It is an amorphous protein highly resistant to the action of proteases that forms the core of elastic fibers. Microfibrils surrounding the core are composed of fibrillins that bind a number of proteins involved in fiber formation. They include microfibril-associated glycoproteins (MAGPs), microfibrillar-associated proteins (MFAPs) and fibulins. Lysyl oxidase (LOX) and lysyl oxidase-like proteins (LOXLs) are responsible for tropoelastin cross-linking and polymerization. TGF-β complexes attached to microfibrils release this cytokine and influence the behavior of the cells in the neighborhood. The role of TGF-β as the main profibrotic cytokine in the liver is well-known and the release of the cytokines of TGF-β superfamily from their storage in elastic fibers may affect the course of fibrosis. Elastic fibers are often studied in the tissues where they provide elasticity and resilience but their role is no longer viewed as purely mechanical. Tropoelastin, elastin polymer and elastin peptides resulting from partial elastin degradation influence fibroblastic and inflammatory cells as well as angiogenesis. A similar role may be performed by elastin in the liver. This article reviews the results of the research of liver elastic fibers on the background of the present knowledge of elastin biochemistry and physiology. The regulation of liver elastin synthesis and degradation may be important for the outcome of liver fibrosis.

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Elastin hydrolysate derived from fish enhances proliferation of human skin fibroblasts and elastin synthesis in human skin fibroblasts and improves the skin conditions

Abstract: Therefore, elastin hydrolysate activates human skin fibroblasts and has beneficial effects on skin conditions.

Cited by 26 publications

References 28 publications

Characterization and Toxicity Evaluation of Broiler Skin Elastin for Potential Functional Biomaterial in Tissue Engineering

Characterization and Toxicity Evaluation of Broiler Skin Elastin for Potential Functional Biomaterial in Tissue Engineering

Collagen in Wound Healing

Elastin in the Liver

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