Cross-linking of dermal collagen induced by singlet oxygen.
Changes were studied in dermal collagen induced by singlet oxygen, which was generated by a bilirubin-photosensitized reaction. An increase in the ratio of high-molecular-weight components (beta- and r-components) against the alpha-chain of collagen after irradiation manifested in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium azide, a singlet oxygen quencher, inhibits the alteration of the molecular size by the photochemical reaction. These data suggest that chronic sunlight irradiation may contribute to cross-links of dermal collagen.
Schepens Eye Research Institute, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts 02114.
T
T
Hikichi
N
N
Ueno
C L
CL
Trempe
B
B
Chakrabarti
D000818:Animals; D001663:Bilirubin / Q000378:metabolism; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000378:metabolism / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D008027:Light; D046911:Macromolecular Substances; D008353:Mannitol / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism* / Q000494:pharmacology*; D012867:Skin / Q000187:drug effects / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate
D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D017382:Reactive Oxygen Species; D012967:Sodium Dodecyl Sulfate; D008353:Mannitol; D003094:Collagen; D001663:Bilirubin; D010100:Oxygen