Transdermal permeation effect of collagen hydrolysates of deer sinew on mouse skin, ex vitro, and antioxidant activity, increased type I collagen secretion of percutaneous proteins in NIH/3T3 cells.
3T3 Cells
Animals
Collagen Type I
/ metabolism
Cosmetics
/ pharmacology
Deer
Free Radical Scavengers
/ isolation & purification
Male
Medicine, Chinese Traditional
/ methods
Mice
Oxidative Stress
/ drug effects
Permeability
Protein Hydrolysates
/ isolation & purification
Skin
/ cytology
Skin Aging
/ drug effects
antioxidant activity
collagen hydrolysates
deer sinew
percutaneous proteins
percutaneous rate
type I collagen
Journal
Journal of cosmetic dermatology
ISSN: 1473-2165
Titre abrégé: J Cosmet Dermatol
Pays: England
ID NLM: 101130964
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
02
04
2019
revised:
19
05
2019
accepted:
20
05
2019
pubmed:
21
6
2019
medline:
20
11
2020
entrez:
21
6
2019
Statut:
ppublish
Résumé
The collagen hydrolysates as a cosmetic material have already been wide application. At present, few studies concern with transdermal behavior of collagen hydrolysates in vitro. Deer sinew contains rich collagen with a content of 82.12%. Thus, this article mainly studies the transdermal effect of collagen hydrolysates of deer sinew (DSCH) on mouse skin, ex vitro, and to explore skincare protection of percutaneous proteins. Collagen hydrolysates of deer sinew were extracted by 0.2% HCl and a two-step enzymatic method of pepsin-trypsin. The content of 17 amino acids of DSCH was detected by precolumn derivatization RP-HPLC. Using Franz diffusion cell systems studied the transdermal effect of DSCH and then examined the percutaneous rate and molecular weight distribution of percutaneous proteins (PP). Further, we studied the bioactivity of PP in vitro, such as the total antioxidant capacity and collagen secretion in NIH/3T3 cells. About 8.0% DSCH could penetrate skin of mouse, the molecular weight of PP mainly distributed in 5 ~ 13 kDa, accounted for 91.55%. Compared with the antioxidant activity of DSCH, PP had obvious antioxidant activity of scavenging radical cation. Meanwhile, PP promoted cell proliferation and collagen I secretion in fibroblast cells; however, level of type III collagen has no change. Collagen hydrolysates of deer sinew may be used as cosmetic material to protect the skin from oxidative stress, to prevent premature skin aging.
Sections du résumé
BACKGROUND
BACKGROUND
The collagen hydrolysates as a cosmetic material have already been wide application. At present, few studies concern with transdermal behavior of collagen hydrolysates in vitro.
OBJECTIVE
OBJECTIVE
Deer sinew contains rich collagen with a content of 82.12%. Thus, this article mainly studies the transdermal effect of collagen hydrolysates of deer sinew (DSCH) on mouse skin, ex vitro, and to explore skincare protection of percutaneous proteins.
METHODS
METHODS
Collagen hydrolysates of deer sinew were extracted by 0.2% HCl and a two-step enzymatic method of pepsin-trypsin. The content of 17 amino acids of DSCH was detected by precolumn derivatization RP-HPLC. Using Franz diffusion cell systems studied the transdermal effect of DSCH and then examined the percutaneous rate and molecular weight distribution of percutaneous proteins (PP). Further, we studied the bioactivity of PP in vitro, such as the total antioxidant capacity and collagen secretion in NIH/3T3 cells.
RESULTS
RESULTS
About 8.0% DSCH could penetrate skin of mouse, the molecular weight of PP mainly distributed in 5 ~ 13 kDa, accounted for 91.55%. Compared with the antioxidant activity of DSCH, PP had obvious antioxidant activity of scavenging radical cation. Meanwhile, PP promoted cell proliferation and collagen I secretion in fibroblast cells; however, level of type III collagen has no change.
CONCLUSION
CONCLUSIONS
Collagen hydrolysates of deer sinew may be used as cosmetic material to protect the skin from oxidative stress, to prevent premature skin aging.
Substances chimiques
Collagen Type I
0
Cosmetics
0
Free Radical Scavengers
0
Protein Hydrolysates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
519-528Subventions
Organisme : the National Key Research and Development Program of China
ID : 2017YFC1702106 and 2018YFC1706605
Organisme : the Science and Technology Development Plan Project of Jilin Province
ID : 20190101010JH and 20190304095YY
Organisme : the National Traditional Chinese Medicine Standardization Project of China
ID : ZYBZH-C-JL-22 and ZYBZH-Y-JL-26
Organisme : Jilin Provincial Key Laboratory of BioMacromolecules of Chinese Medicine
Informations de copyright
© 2019 Wiley Periodicals, Inc.
Références
Quan T, Fisher GJ. Role of age-associated alterations of the dermal extracellular matrix microenvironment in human skin aging: a mini-review. Gerontology. 2015;61(5):427-434.
Epstein EH, Munderloh NH. Human skin collagen. Presence of type I and type III at all levels of the dermis. J Biol Chem. 1978;253(5):1336-1337.
Chung JH, Seo JY, Choi HR, et al. Modulation of skin collagen metabolism in aged and photoaged human skin in vivo. J Invest Dermatol. 2001;117(5):1218-1224.
West MD, Pereira-Smith OM, Smith JR. Replicative senescence of human skin fibroblasts correlates with a loss of regulation and overexpression of collagenase activity. Exp Cell Res. 1989;184(1):138-147.
Fisher GJ, Quan T, Purohit T, et al. Collagen fragmentation promotes oxidative stress and elevates matrix metalloproteinase-1 in fibroblasts in aged human skin. Am J Pathol. 2009;174(1):101-114.
Qin Z, Worthen CA, Quan T. Cell-size-dependent upregulation of HGF expression in dermal fibroblasts: Impact on human skin connective tissue aging. J Dermatol Sci. 2017;88(3):289-297.
Uitto J. The role of elastin and collagen in cutaneous aging: intrinsic aging versus photoexposure. J Drugs Dermatol. 2008;7(suppl 2):s12-s16.
Schwartz E, Cruickshank FA, Christensen CC, Perlish JS, Lebwohl M. Collagen alterations in chronically sun-damaged human skin. Photochem Photobiol. 1993;58(6):841-844.
Talwar HS, Griffiths CE, Fisher GJ, Hamilton TA, Voorhees JJ. Reduced type I and type III procollagens in photodamaged adult human skin. J Invest Dermatol. 1995;105(2):285-290.
Zhang H, Zhao Y, Xu YF, Li YT, Zhao DQ. Study on the condition of tyrosinase hydrolyzing deer tendons collagen. Food Sci Technol. 2010;35(9):216-218, 222.
Wei GQ, Liu SH, Chen DY, Fan N, Zhao Y, Zhang LX. Research and application progress of collagen from the products of deer. J Econ Anim. 2014;34(4):198-205.
Shao P, Chen XX, Sun PL. Improvement of antioxidant and moisture-preserving activities of Sargassum horneri polysaccharide enzymatic hydrolyzates. Int J Biol Macromol. 2015;74:420-427.
Asserin J, Lati E, Shioya T, Prawitt J. The effect of oral collagen peptide supplementation on skin moisture and the dermal collagen network: evidence from an ex vivo model and randomized, placebo-controlled clinical trials. J Cosmet Dermatol 2015;14(4):291-301.
Oba C, Ohara H, Morifuji M, et al. Collagen hydrolysate intake improves the loss of epidermal barrier function and skin elasticity induced by UVB irradiation in hairless mouse. Photodermatol Photoimmunol Photomed. 2013;29(4):204-211.
Mendis E, Rajapakse N, Kim S-K. Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J Agric Food Chem. 2005;53(3):581-587.
Yang J-I, Ho H-Y, Chu Y-J, Chow C-J. Characteristic and antioxidant activity of retorted gelatin hydrolysates from cobia (Rachycentron canadum) skin. Food Chem. 2008;110(1):128-136.
Kim SK, Kim YT, Byun HG, Nam KS, Joo DS, Shahidi F. Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin. J Agric Food Chem. 2001;49(4):1984-1989.
Hou HU, Li B, Zhang Z, et al. Moisture absorption and retention properties, and activity in alleviating skin photodamage of collagen polypeptide from marine fish skin. Food Chem. 2012;135(3):1432-1439.
Morganti P, Randazzo SD, Cardillo A. Role of insoluble and soluble collagen as skin moisturizer. J Appl Cosmetol. 1986;4(4):141-152.
Ranjini HS, Padmanabha U, Kamath SU, Setty M, Hadapad B. A specific absorbance to estimate a protein by lowry's method. Adv Sci Lett. 2017;23(3):1889-1891.
Jiang W, Wang J. RP-HPLC coupling with precolumn derivatization for determination of amino acid in protein power. Chinese J Health Lab Tech. 2008;18(2):280-282.
Komsa-Penkova R, Spirova R, Bechev B. Modification of Lowry's method for collagen concentration measurement. J Biochem Biophys Methods. 1996;32(1):33-43.
Re R, Pellegrini N, Proteggente A, Pannala A, Yang M, Rice-Evans C. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Biol Med. 1999;26(9-10):1231-1237.
Myllyharju J, Kivirikko KI. Collagens and collagen-related diseases. Ann Med. 2001;33(1):7-21.
Li GY, Fukunaga S, Takenouchi K, Nakamura F. Comparative study of the physiological properties of collagen, gelatin and collagen hydrolysate as cosmetic materials. Int J Cosmet Sci. 2005;27(2):101-106.
Peng Y, Glattauer V, Werkmeister JA, Ramshaw JA. Evaluation for collagen products for cosmetic application. J Cosmet Sci. 2004;55(4):327-341.
Nagelschmidt M, Struck H. Kollagen als cosmeticum? Archiv Für Dermatologische Forschung. 1974;250(3):237-243.
Zhang ZK, Li GY. Comparison of functions of collagen, gelatin and collagen hydrolysate as skin-care cosmetic materials. China Surfact Det Cosmet. 2006;36(1):18-21,25.
Fan J, Zhuang Y, Li B. Effects of collagen and collagen hydrolysate from jellyfish umbrella on histological and immunity changes of mice photoaging. Nutrients. 2013;5(1):223-233.
Cooperman ES, Johnsen VL. Penetration of protein hydrolysates into human hair strands. Cosmet Perfu. 1973;88:19-22.
Chvapli M, Eckmayer Z. Role of proteins in cosmetics. Int J Cosmet Sci. 1985;7(2):41-49.
Herce HD, Garcia AE. Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc Natl Acad Sci U S A. 2007;104(52):20805-20810.
Huang K, Garcia AE. Free energy of translocating an arginine-rich cell-penetrating peptide across a lipid bilayer suggests pore formation. Biophys J. 2013;104(2):412-420.
SMejkalova D, Huerta Angeles G, Ehlova T. Hyaluronan (Hyaluronic Acid): a natural moisturizer for skin care. In Chen CW, ed. Harry's 9th Edition, vol 2. Doln Dobrouc, Europe: Chemical Publishing company;2015:605-622.
Cai F. A comparative study on physicochemical properties of the oviducts in bull frog R. Catesbiana, common giant toad Bufo bufo gargarizans and Northeast brown frog R. dybowskii. Changchun, China: Agricultural University; 2007.
Li B, Chen F, Wang X, Ji B, Wu Y. Isolation and identification of antioxidative peptides from porcine collagen hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chem. 2007;102(4):1135-1143.
Saiga A, Tanabe S, Nishimura T. Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. J Agric Food Chem. 2003;51(12):3661-3667.
Sriram G, Bigliardi PL, Bigliardi-qi M. Fibroblast heterogeneity and its implications for engineering organotypic skin models in vitro. Eur J Cell Biol. 2015;94(11):483-512.
Geng M, Miao H, Liu KL, Han YT, Chen XH, Wang CB. Collagen hydrolysate Gly-Pro-Hyp on osteoblastic proliferation and differentiation of MC3T3-E1 cells. J Clin Nurs Res. 2017;1(3):40-46.
Zague V, do Amaral JB, Rezende Teixeira P, de Oliveira Niero EL, Lauand C, Machado-Santelli GM. Collagen peptides modulate the metabolism of extracellular matrix by human dermal fibroblasts derived from sun-protected and sun-exposed body sites. Cell Biol Int. 2018;42(1):95-104.