A potential role for endogenous proteins as sacrificial sunscreens and antioxidants in human tissues

被引:34
|
作者
Hibbert, Sarah A. [1 ]
Watson, Rachel E. B. [1 ]
Gibbs, Neil K. [1 ]
Costello, Patrick [1 ]
Baldock, Clair [3 ]
Weiss, Anthony S. [4 ,5 ,6 ]
Griffiths, Christopher E. M. [1 ]
Sherratt, Michael J. [2 ]
机构
[1] Univ Manchester, Ctr Dermatol Res, Inst Inflammat & Repair, Manchester Acad Hlth Sci Ctr, Manchester, Lancs, England
[2] Univ Manchester, Ctr Tissue Injury & Repair, Inst Inflammat & Repair, Manchester Acad Hlth Sci Ctr, Manchester, Lancs, England
[3] Univ Manchester, Fac Life Sci, Wellcome Trust Ctr Cell Matrix Res, Manchester, Lancs, England
[4] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia
[5] Univ Sydney, Charles Perkins Ctr, Sydney, NSW 2006, Australia
[6] Univ Sydney, Bosch Inst, Sydney, NSW 2006, Australia
来源
REDOX BIOLOGY | 2015年 / 5卷
基金
英国生物技术与生命科学研究理事会;
关键词
Photodecomposition; UVA radiation; Photoageing; Sunscreen; Solar simulated radiation; Chromophores; ABSORBING AMINO-ACIDS; EXTRACELLULAR-MATRIX; VI COLLAGEN; HUMAN SKIN; SUPRAMOLECULAR ORGANIZATION; MACROPHAGE METALLOELASTASE; ULTRAVIOLET-IRRADIATION; C IRRADIATION; UV-RADIATION; FIBRILLIN;
D O I
10.1016/j.redox.2015.04.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Excessive ultraviolet radiation (UVR) exposure of the skin is associated with adverse clinical outcomes. Although both exogenous sunscreens and endogenous tissue components (including melanins and tryptophan-derived compounds) reduce UVR penetration, the role of endogenous proteins in absorbing environmental UV wavelengths is poorly defined. Having previously demonstrated that proteins which are rich in UVR-absorbing amino acid residues are readily degraded by broadband UVB-radiation (containing UVA, UVB and UVC wavelengths) here we hypothesised that UV chromophore (Cys, Trp and Tyr) content can predict the susceptibility of structural proteins in skin and the eye to damage by physiologically relevant doses (up to 15.4 J/cm(2)) of solar UVR (95% UVA, 5% UVB). We show that: i) purified suspensions of UV-chromophore-rich fibronectin dimers, fibrillin microfibrils and beta- and gamma-lens crystallins undergo solar simulated radiation (SSR)-induced aggregation and/or decomposition and ii) exposure to identical doses of SSR has minimal effect on the size or ultrastructure of UV chromophore-poor tropoelastin, collagen I, collagen VI microfibrils and alpha-crystallin. If UV chromophore content is a factor in determining protein stability in vivo, we would expect that the tissue distribution of Cys, Trp and Tyr-rich proteins would correlate with regional UVR exposure. From bioinformatic analysis of 244 key structural proteins we identified several biochemically distinct, yet UV chromophore-rich, protein families. The majority of these putative UV-absorbing proteins (including the late cornified envelope proteins, keratin associated proteins, elastic fibre-associated components and beta- and gamma-crystallins) are localised and/or particularly abundant in tissues that are exposed to the highest doses of environmental UVR, specifically the stratum corneum, hair, papillary dermis and lens. We therefore propose that UV chromophore-rich proteins are localised in regions of high UVR exposure as a consequence of an evolutionary pressure to express sacrificial protein sunscreens which reduce UVR penetration and hence mitigate tissue damage. (C) 2015 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
引用
收藏
页码:101 / 113
页数:13
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