UV-induced protein alterations and lipid oxidation in erythrocyte membranes.
Certain ultraviolet radiation-induced effects in skin may result from primary photochemical alterations in cell membranes. We have studied isolated erythrocyte membranes in order to determine the UV-fluence and wavelength dependence for protein alterations and lipid oxidation. Protein crosslinking was detected as high molecular weight protein (greater than 200,000 DA) on polyacrylamide/agarose gel electrophoresis. Spectrin decreased more rapidly than the other membrane proteins upon exposure to lambda = 250-380 nm radiation. Nitrogen-purging inhibited the UV-induced decrease in spectrin by 60% and decreased crosslinking to an even greater degree. The decrease in spectrin was not inhibited by superoxide dismutase, catalase, or sodium azide. Radiation at 280 nm was most effective for spectrin loss, 265 and 297 nm were less effective and 254 and 313 nm were not effective. Prior irradiation at 280 nm did not sensitize the membranes to subsequent irradiation at 313 nm indicating that photodecomposition products of tryptophan are not involved. Lipid photooxidation was measured with the thiobarbituric acid assay and was induced at higher fluences of UV radiations than those required for loss of spectrin. These results indicate that the major effects of UV radiation on cell membranes are alterations of proteins and suggest that tryptophan is the major chromophore for these alterations.
Kochevar
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Wellman Laboratories, Department of Dermatology, Massachusetts General Hospital, Harvard Medical School, Boston 02114.
D004910:Erythrocyte Membrane / Q000528:radiation effects*; D006801:Humans; D066298:In Vitro Techniques; D008563:Membrane Lipids / Q000528:radiation effects*; D008565:Membrane Proteins / Q000528:radiation effects*; D010084:Oxidation-Reduction; D014466:Ultraviolet Rays
D008563:Membrane Lipids; D008565:Membrane Proteins