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Oral Collagen Drink for Antiaging: Antioxidation, Facilitation of the Increase of Collagen Synthesis, and Improvement of Protein Folding and DNA Repair in Human Skin Fibroblasts.

ABSTRACT: This work unveils a fish collagen drink for improvement of skin aging. Previous studies frequently discussed the skin aging from the angle of the representative characteristics of collagen loss and the oxidative-induced expression of proteolytic enzymes matrix metalloproteinases (MMPs), but few groups comprehensively investigated the efficacy of oral hydrolyzed collagen for enhancing protein folding and DNA repair as well as improving notable cell behaviors. To delineate the broad perspective on delaying skin aging, we inspected the collagen drink-treated fibroblast cells from the molecular and cellular aspects. The results show that the collagen drink could perform the compact antiaging effects on ROS inhibition, the facilitation of the synthesis of extracellular matrix (ECM) proteins, the increase of mitochondrial activity, and improvement of the gene expression regarding correct protein folding, DNA mismatch repair (MMR) and base excision repair (BER). Although the experimental results are built on the cellular models, we believe that the positive outcomes can provide more details on the influence of oral hydrolyzed collagen supplement for antiaging. In short, we have successfully proved that the synergistic effect of the collagen drink could not only reduce the oxidative damage but also ameliorate the cell functionality to compensate the harmful effects induced by UVA.

SUBMITTER: Lin P

PROVIDER: S-EPMC7238338 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Oral Collagen Drink for Antiaging: Antioxidation, Facilitation of the Increase of Collagen Synthesis, and Improvement of Protein Folding and DNA Repair in Human Skin Fibroblasts.

Lin Ping P Hua Nan N Hsu Yu-Chen YC Kan Kai-Wen KW Chen Jia-Haur JH Lin Yung-Hao YH Lin Yung-Hsiang YH Kuan Chen-Meng CM

Oxidative medicine and cellular longevity 20200511

This work unveils a fish collagen drink for improvement of skin aging. Previous studies frequently discussed the skin aging from the angle of the representative characteristics of collagen loss and the oxidative-induced expression of proteolytic enzymes matrix metalloproteinases (MMPs), but few groups comprehensively investigated the efficacy of oral hydrolyzed collagen for enhancing protein folding and DNA repair as well as improving notable cell behaviors. To delineate the broad perspective on ...[more]

PMID: 32454944

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Project description:A comparison has been made of the synthesis of glycosaminoglycans by human skin fibroblasts cultured on plastic or collagen gel substrata. Confluent cultures were incubated with [3H]glucosamine and Na235SO4 for 48h. Radiolabelled glycosaminoglycans were then analysed in the spent media and trypsin extracts from cells on plastic and in the medium, trypsin and collagenase extracts from cells on collagen gels. All enzyme extracts and spent media contained hyaluronic acid, heparan sulphate and dermatan sulphate. Hyaluronic acid was the main 3H-labelled component in media and enzyme extracts from cells on both substrata, although it was distributed mainly to the media fractions. Heparan sulphate was the major [35S]sulphated glycosaminoglycan in trypsin extracts of cells on plastic, and dermatan sulphate was the minor component. In contrast, dermatan sulphate was the principal [35S]sulphated glycosaminoglycan in trypsin and collagenase extracts of cells on collagen gels. The culture substratum also influenced the amounts of [35S]sulphated glycosaminoglycans in media and enzyme extracts. With cells on plastic, the medium contained most of the heparan sulphate (75%) and dermatan sulphate (> 90%), whereas the collagenase extract was the main source of heparan sulphate (60%) and dermatan sulphate (80%) from cells on collagen gels; when cells were grown on collagen, the medium contained only 5-20% of the total [35S]sulphated glycosaminoglycans. Depletion of the medium pool was probably caused by binding of [35S]sulphated glycosaminoglycans to the network of native collagen fibres that formed the insoluble fraction of the collagen gel. Furthermore, cells on collagen showed a 3-fold increase in dermatan sulphate synthesis, which could be due to a positive-feedback mechanism activated by the accumulation of dermatan sulphate in the microenvironment of the cultured cells. For comparative structural analyses of glycosaminoglycans synthesized on different substrata labelling experiments were carried out by incubating cells on plastic with [3H]glucosamine, and cells on collagen gels with [14C]glucosamine. Co-chromatography on DEAE-cellulose of mixed media and enzyme extracts showed that heparan sulphate from cells on collagen gels eluted at a lower salt concentration than did heparan sulphate from cells on plastic, whereas with dermatan sulphate the opposite result was obtained, with dermatan sulphate from cells on collagen eluting at a higher salt concentration than dermatan sulphate from cells on plastic. These differences did not correspond to changes in the molecular size of the glycosaminoglycan chains, but they may be caused by alterations in polymer sulphation.

Dataset Information

Oral Collagen Drink for Antiaging: Antioxidation, Facilitation of the Increase of Collagen Synthesis, and Improvement of Protein Folding and DNA Repair in Human Skin Fibroblasts.

Publications

Oral Collagen Drink for Antiaging: Antioxidation, Facilitation of the Increase of Collagen Synthesis, and Improvement of Protein Folding and DNA Repair in Human Skin Fibroblasts.

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