Abstract
Chronic exposure to ultraviolet (UV) radiation causes remodelling of the dermal extracellular matrix (ECM) leading to photoageing. This remodelling may be driven by cell-derived proteases and/or photochemical mechanisms. We have previously shown that the amino acid composition of dermal ECM proteins correlates with their relative susceptibility to degradation by broadband UVB radiation. UV-chromophore-rich proteins such as fibrillin and fibronectin were preferentially degraded but not chromophore-poor collagen I and tropoelastin. In this study, we determine whether physiological doses of the UVA (315-400nm) component of solar radiation are capable of differentially degrading these ECM proteins. Suspensions of bovine collagen I and fibronectin, recombinant tropoelastin and human dermal fibroblast-derived fibrillin microfibrils were exposed to full spectrum Solar Simulated Radiation (SSR; 290-400nm: 0.8, 7.7 and 15.4J/cm2 and UVA (315-400nm): 1, 10 and 20J/cm2. The effects of SSR and UVA exposure on molecular structure were determined by reducing SDS-PAGE (collagen I, tropoelastin and fibronectin) and atomic force microscopy (fibrillin). Neither SSR nor UVA radiation affected the electrophoretic mobility of chromophore-poor collagen I and tropoelastin. However, both UV spectra induced dose-dependent aggregation of fibronectin (SSR: r2 0.99, UVA: r2 0.98). Similarly, both SSR and UVA radiation also significantly reduced the bead-to-bead distance of fibrillin microfibrils (SSR: mean±SD, 56.6±9.7nm [0J/cm2], 53.2±10.3nm [15.4J/cm2], p
Original language | English |
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Title of host publication | host publication |
Pages | S118-S118 |
Volume | 132 |
Publication status | Published - 7 Sept 2012 |
Event | 42nd Annual Meeting of the European Society for Dermatological Research - Venice, ITALY Duration: 7 Sept 2012 → 10 Sept 2012 |
Conference
Conference | 42nd Annual Meeting of the European Society for Dermatological Research |
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City | Venice, ITALY |
Period | 7/09/12 → 10/09/12 |