Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 425219
Title UVA1 radiation inhibits calcineurin through oxidative damage mediated by photosensitization
Author(s) Musson, R.E.A.; Hensbergen, P.J.; Westphal, A.H.; Temmink, W.P.M.; Deelder, A.M.; Pelt, J. van; Mullenders, L.H.F.; Smit, N.P.M.
Source Free Radical Biology and Medicine 50 (2011)10. - ISSN 0891-5849 - p. 1392 - 1399.
DOI http://dx.doi.org/10.1016/j.freeradbiomed.2011.02.019
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) singlet molecular-oxygen - light-emission measurements - transcription factor nfat - human skin fibroblasts - kappa-b activity - hydrogen-peroxide - cyclosporine-a - ultraviolet-radiation - phosphatase-activity - human keratinocytes
Abstract The protein phosphatase calcineurin has been gradually revealing itself as the central controller of our immune response, although it is involved in a wide array of signaling pathways related to cellular development and cell cycle progression. As such, calcineurin is an attractive, yet delicate, therapeutic target for the prevention of allograft rejection and treatment of several inflammatory skin conditions. However, calcineurin activity is not only sensitive to immunosuppressants such as cyclosporin A and tacrolimus, but also subject to modulation by reactive oxygen species. We have recently shown, both in vivo and in vitro, that UVA1 radiation suppresses calcineurin activity. In this paper, we present evidence that this activity loss is due to singlet oxygen and superoxide generated by photosensitization and show that a closely related phosphatase, PP2A, is not affected. Furthermore, a survey of this damage reveals oxidation of several Met and Cys residues as well as an overall conformational change. These findings provide a mechanistic basis for the hypothesis that UVA1 and calcineurin inhibitors both affect the same signal transduction pathway in skin.
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