Korean J Nutr.  2012 Apr;45(2):113-120. 10.4163/kjn.2012.45.2.113.

Dietary effect of silk protein on epidermal levels of free sphingoid bases and phosphate metabolites in NC/Nga mice

Affiliations
  • 1Department of Medical Nutrition, Graduate School of East-West Medical Science, Kyung Hee University, Yongin 449-701, Korea. choyunhi@khu.ac.kr
  • 2College of Pharmacy, Chungbuk National University, Cheongju 361-763, Korea.

Abstract

In our previous studies, dietary supplements of silk protein, sericin, and fibroin, were beneficial for improving epidermal levels of ceramides, which are the major lipids for maintaining the epidermal barrier. In this study, we investigated the dietary effects of silk protein on epidermal levels of free sphingoid bases and their phosphates such as C18 sphingosine (So), C18 sphinganine (Sa), C18 sphingosine-1-phosphate (S1P), and C18 sphinganine-1-phosphate (Sa1P), which are either synthetic substrate or degradative metabolites of ceramides. Forty-five male NC/Nga mice, an animal model of atopic dermatitis (AD), were divided into three groups: group CA was an atopic control and fed a control diet, group S was fed a 1% sericin diet, and group F was fed a 1% fibroin diet. Fifteen male BALB/c mice served as group C (control group) and were fed the control diet. All mice were fed with diets and water ad libitum for 10 weeks. Sa in group CA was lower than that in group C, but So in group CA was similar to that in group C. So and Sa were higher in groups S and F than those in group CA; So level was even higher than that in group C, and Sa level was similar to that of group C. The So/Sa ratio in group CA, which is reported to increase in AD, was significantly higher than that of group C. The So/Sa ratio was lower in groups S and F than that in group CA, and decreased further in group F. However, S1P and Sa1P in groups S and F were similar to those in group CA. Taken together, we demonstrated that silk protein, sericin and fibroin dietary supplements, increased So and Sa levels, and decreased the So/Sa ratio.

Keyword

silk protein; sphingosine; sphinganine; NC/Nga mice; atopic dermatitis

MeSH Terms

Animals
Ceramides
Dermatitis, Atopic
Diet
Dietary Supplements
Fibroins
Humans
Lysophospholipids
Male
Mice
Models, Animal
Phosphates
Sericins
Silk
Sphingosine
Water
Ceramides
Fibroins
Lysophospholipids
Phosphates
Sericins
Silk
Sphingosine
Water

Figure

  • Fig. 1 Levels of C18 Sphingoid bases in the epidermis of mice. C: BALB/c mice were fed with a control diet, group CA, S and F: NC/Nga mice were fed with a control diet (group CA) or diets containing 1% sericin extract (group S) or 1% fibroin extract (group F) for 10 weeks. Sphingoid bases were extracted from epidermal homogenates of each groups and analyzed using HPLC. Values are presented as Means ± SEM (n = 10). Means with different alphabetical letters are significantly different according to duncan's multiple comparison at p < 0.05.

  • Fig. 2 Ratio of C18So/Sa in the epidermis of mice. Group C: BALB/c mice were fed with a control diet, group CA, S and F: NC/Nga mice were fed with a control diet (group CA) or diets containing 1% sericin extract (group S) or 1% fibroin extract (group F) for 10 weeks. Values are presented as Means ± SEM (n = 10). Means with different alphabetical letters are significantly different according to duncan's multiple range test at p < 0.05.

  • Fig. 3 Levels of C18 Sphingoidbase-1-phosphates in the epidermis of mice. Group C: BALB/c mice were fed with a control diet, group CA. S and F: NC/Nga mice were fed with a control diet (group CA) or diets containing 1% sericin extract (group S) or 1% fibroin extract (group F) for 10 weeks. Sphingoid base-1-phosphates of epidermal homogenates were first dephosphorylated by alkaline phosphatase at 37℃ then separated sphingoid bases were extracted and analyzed using HPLC. Values are presented as means ± SEM (n = 10). Means with different alphabetical letters are significantly different according to duncan's multiple range test at p < 0.05.


Cited by  1 articles

Comparative effect of dietary borage oil and safflower oil on anti-proliferation and ceramide metabolism in the epidermis of essential fatty acid deficient guinea pigs
Se Ryung Lee, Yunhi Cho
J Nutr Health. 2015;48(4):319-326.    doi: 10.4163/jnh.2015.48.4.319.


Reference

1. Coderch L, López O, de la Maza A, Parra JL. Ceramides and skin function. Am J Clin Dermatol. 2003. 4(2):107–129.
Article
2. Bartke N, Hannun YA. Bioactive sphingolipids: metabolism and function. J Lipid Res. 2009. 50:S91–S96.
Article
3. Bibel DJ, Aly R, Shinefield HR. Antimicrobial activity of sphingosines. J Invest Dermatol. 1992. 98(3):269–273.
Article
4. Vogler R, Sauer B, Kim DS, Schäfer-Korting M, Kleuser B. Sphingosine-1-phosphate and its potentially paradoxical effects on critical parameters of cutaneous wound healing. J Invest Dermatol. 2003. 120(4):693–700.
Article
5. Elias PM, Wood LC, Feingold KR. Epidermal pathogenesis of inflammatory dermatoses. Am J Contact Dermat. 1999. 10(3):119–126.
Article
6. Horn EJ, Domm S, Katz HI, Lebwohl M, Mrowietz U, Kragballe K. International Psoriasis Council. Topical corticosteroids in psoriasis: strategies for improving safety. J Eur Acad Dermatol Venereol. 2010. 24(2):119–124.
Article
7. Majoie IM, Oldhoff JM, van Weelden H, Laaper-Ertmann M, Bousema MT, Sigurdsson V, Knol EF, Bruijnzeel-Koomen CA, de Bruin-Weller MS. Narrowband ultraviolet B and medium-dose ultraviolet A1 are equally effective in the treatment of moderate to severe atopic dermatitis. J Am Acad Dermatol. 2009. 60(1):77–84.
Article
8. Warren RB, Griffiths CE. Systemic therapies for psoriasis: methotrexate, retinoids, and cyclosporine. Clin Dermatol. 2008. 26(5):438–447.
Article
9. Kim J, Kim H, Jeong do H, Kim SH, Park SK, Cho Y. Comparative effect of gromwell (Lithospermum erythrorhizon) extract and borage oil on reversing epidermal hyperproliferation in guinea pigs. Biosci Biotechnol Biochem. 2006. 70(9):2086–2095.
Article
10. Lee KG, Yeo JH, Lee YW, Kweon HY, Kim JH. Bioactive and skin-compatible properties of silk sericin. Korean J Sericult Sci. 2001. 43(2):109–115.
11. Padamwar MN, Pawar AP, Daithankar AV, Mahadik KR. Silk sericin as a moisturizer: an in vivo study. J Cosmet Dermatol. 2005. 4(4):250–257.
Article
12. Kato N, Sato S, Yamanaka A, Yamada H, Fuwa N, Nomura M. Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity. Biosci Biotechnol Biochem. 1998. 62(1):145–147.
Article
13. Zhaorigetu S, Yanaka N, Sasaki M, Watanabe H, Kato N. Silk protein, sericin, suppresses DMBA-TPA-induced mouse skin tumorigenesis by reducing oxidative stress, inflammatory responses and endogenous tumor promoter TNF-alpha. Oncol Rep. 2003. 10(3):537–543.
14. Nagai N, Murao T, Ito Y, Okamoto N, Sasaki M. Enhancing effects of sericin on corneal wound healing in rat debrided corneal epithelium. Biol Pharm Bull. 2009. 32(5):933–936.
Article
15. Choi MJ, Maibach HI. Role of ceramides in barrier function of healthy and diseased skin. Am J Clin Dermatol. 2005. 6(4):215–223.
Article
16. Farwanah H, Raith K, Neubert RH, Wohlrab J. Ceramide profiles of the uninvolved skin in atopic dermatitis and psoriasis are comparable to those of healthy skin. Arch Dermatol Res. 2005. 296(11):514–521.
Article
17. Imokawa G, Abe A, Jin K, Higaki Y, Kawashima M, Hidano A. Decreased level of ceramides in stratum corneum of atopic dermatitis: an etiologic factor in atopic dry skin? J Invest Dermatol. 1991. 96(4):523–526.
Article
18. Meguro S, Arai Y, Masukawa Y, Uie K, Tokimitsu I. Relationship between covalently bound ceramides and transepidermal water loss (TEWL). Arch Dermatol Res. 2000. 292(9):463–468.
Article
19. Motta S, Monti M, Sesana S, Caputo R, Carelli S, Ghidoni R. Ceramide composition of the psoriatic scale. Biochim Biophys Acta. 1993. 1182(2):147–151.
Article
20. Reiter LV, Torres SM, Wertz PW. Characterization and quantification of ceramides in the nonlesional skin of canine patients with atopic dermatitis compared with controls. Vet Dermatol. 2009. 20(4):260–266.
Article
21. Madyarov S, Lee KG, Yeo JH, Nam J, Lee YW. Improved method for the preparation of silk fibroin hydrolysates. Korean J Sericult Sci. 1999. 41(2):108–115.
22. Suto H, Matsuda H, Mitsuishi K, Hira K, Uchida T, Unno T, Ogawa H, Ra C. NC/Nga mice: a mouse model for atopic dermatitis. Int Arch Allergy Immunol. 1999. 120:Suppl 1. 70–75.
Article
23. Takagi Y, Nakagawa H, Yaginuma T, Takema Y, Imokawa G. An accumulation of glucosylceramide in the stratum corneum due to attenuated activity of beta-glucocerebrosidase is associated with the early phase of UVB-induced alteration in cutaneous barrier function. Arch Dermatol Res. 2005. 297(1):18–25.
Article
24. Doering T, Holleran WM, Potratz A, Vielhaber G, Elias PM, Suzuki K, Sandhoff K. Sphingolipid activator proteins are required for epidermal permeability barrier formation. J Biol Chem. 1999. 274(16):11038–11045.
Article
25. Min JK, Yoo HS, Lee EY, Lee WJ, Lee YM. Simultaneous quantitative analysis of sphingoid base 1-phosphates in biological samples by o-phthalaldehyde precolumn derivatization after dephosphorylation with alkaline phosphatase. Anal Biochem. 2002. 303(2):167–175.
Article
26. Flamand N, Justine P, Bernaud F, Rougier A, Gaetani Q. In vivo distribution of free long-chain sphingoid bases in the human stratum corneum by high-performance liquid chromatographic analysis of strippings. J Chromatogr B Biomed Appl. 1994. 656(1):65–71.
Article
27. Caligan TB, Peters K, Ou J, Wang E, Saba J, Merrill AH Jr. A high-performance liquid chromatographic method to measure sphingosine 1-phosphate and related compounds from sphingosine kinase assays and other biological samples. Anal Biochem. 2000. 281(1):36–44.
Article
28. Park KH, Choi YS, Kim HA, Lee KG, Yeo JH, Jung DH, Kim SH, Cho YH. Dietary effect of silk protein on ceramide synthesis and the expression of ceramide metabolic enzymes in the epidermis of NC/Nga mice. J Korean Soc Food Sci Nutr. 2007. 36(5):554–562.
Article
29. Macheleidt O, Kaiser HW, Sandhoff K. Deficiency of epidermal protein-bound omega-hydroxyceramides in atopic dermatitis. J Invest Dermatol. 2002. 119(1):166–173.
Article
30. Arikawa J, Ishibashi M, Kawashima M, Takagi Y, Ichikawa Y, Imokawa G. Decreased levels of sphingosine, a natural antimicrobial agent, may be associated with vulnerability of the stratum corneum from patients with atopic dermatitis to colonization by Staphylococcus aureus. J Invest Dermatol. 2002. 119(2):433–439.
Article
31. Elias PM, Menon GK. Structural and lipid biochemical correlates of the epidermal permeability barrier. Adv Lipid Res. 1991. 24:1–26.
32. Melnik B. Disturbances of antimicrobial lipids in atopic dermatitis. J Dtsch Dermatol Ges. 2006. 4(2):114–123.
Article
33. Bibel DJ, Aly R, Shinefield HR. Inhibition of microbial adherence by sphinganine. Can J Microbiol. 1992. 38(9):983–985.
Article
34. Loiseau N, Moradian S, Elias PM, Holleran WM, Uchida Y. Ceramide metabolites in epidermal permeability barrier function and atopic dermatitis [abstract]. J Invest Dermatol. 2009. 129:Suppl 1. S68. Abstract no.405.
35. Stewart ME, Downing DT. Free sphingosines of human skin include 6-hydroxysphingosine and unusually long-chain dihydrosphingosines. J Invest Dermatol. 1995. 105(4):613–618.
Article
36. Hait NC, Oskeritzian CA, Paugh SW, Milstien S, Spiegel S. Sphingosine kinases, sphingosine 1-phosphate, apoptosis and diseases. Biochim Biophys Acta. 2006. 1758(12):2016–2026.
Article
37. Gómez-Muñoz A. Ceramide 1-phosphate/ceramide, a switch between life and death. Biochim Biophys Acta. 2006. 1758(12):2049–2056.
Article
38. Prieschl EE, Csonga R, Novotny V, Kikuchi GE, Baumruker T. The balance between sphingosine and sphingosine-1-phosphate is decisive for mast cell activation after Fc epsilon receptor I triggering. J Exp Med. 1999. 190(1):1–8.
Article
39. Mondal M, Trivedy K, Nirmal Kumar S. The silk proteins, sericin and fibroin in silkworm, Bombyx mori Linn., -a review. Casp J Environ Sci. 2007. 5(2):63–76.
40. Voegeli R, Meier J, Blust R. Sericin silk protein: unique structure and properties. Cosmet Toilet. 1993. 108:101–108.
41. Aramwit P, Sangcakul A. The effects of sericin cream on wound healing in rats. Biosci Biotechnol Biochem. 2007. 71(10):2473–2477.
Article
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