Formation of protein-bound 3,4-dihydroxyphenylalanine in collagen types I and IV exposed to ultraviolet light.

Abstract:

:Collagen was exposed to an ultraviolet (UV) lamp that emitted predominantly in the UVB range. The cross-linking of collagen type I and type IV by UV irradiation was observed. Amino acid analyses revealed that Tyr residues in both collagen types I and IV were decreased by irradiation. In collagen type IV, losses of His and Met residues were also observed. These losses of collagen type IV may be due to the degradation of Trp, which exists in collagen type IV and decreased drastically during UV irradiation. To clarify the mechanism of Tyr modification in both types of collagen, the degradation products of Tyr were analyzed. Dityrosine, which is a dimer of the Tyr residue, could not be detected in the acid hydrolysates of UV-irradiated collagen. However, 3,4-dihydroxyphenylalanine, DOPA, was detected in the hydrolysates using HPLC with an electrochemical detector. The amounts of DOPA in the acid hydrolysates of collagen exposed to UV light for 24 h were approximately 350 pmol/mg protein (collagen type IV) and 80 pmol/mg protein (collagen type I). The DOPA formed may partially contribute to photoaging of the skin.

journal_name

Photochem Photobiol

authors

Kato Y,Nishikawa T,Kawakishi S

doi

10.1111/j.1751-1097.1995.tb08624.x

subject

Has Abstract

pub_date

1995-04-01 00:00:00

pages

367-72

issue

4

eissn

0031-8655

issn

1751-1097

journal_volume

61

pub_type

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