Biochemical and Biophysical Research Communications
The presence of d-β-aspartic acid-containing peptides in elastic fibers of sun-damaged skin: a potent marker for ultraviolet-induced skin aging
Section snippets
Methods
Antibody againstd-β-Asp-containing peptide. The preparation and characterization of the antibody we used were described in the previous paper [15]. The polyclonal antibody against the peptide; Gly–Leu–d-β-Asp–Ala–Thr–Gly–Leu–d-β-Asp–Ala–Thr–Gly–Leu–d-β-Asp–Ala–Thr (designated peptide 3R), containing three repeats of position 149–153 of the human αA-crystallin optic isomer in rabbit serum, was purified by affinity chromatography using peptide 3R and bovine αA-crystallin as ligands. The antibody
Immunohistochemical staining
The antibody for peptide 3R recognized fibrous network in the upper to mid-dermis of the sun-exposed skin (face) taken from 59-year-old individual (Fig. 1B), but not in the sun-exposed skin (face) of 9-year-old individual (Fig. 1A). The antibody strongly reacted with the elastotic materials of actinic elastosis in the upper dermis of the sun-exposed skin (face) taken from 86-year-old individual (Fig. 1C). In contrast, there was a minimum immunoreactivity of the antibody with fibrous network in
Discussion
We have reported that the configuration of the Asp-151 residue of human αA-crystallin converted to a d-β-Asp isomer during aging [6], [8], [9], [10]. To detect the locality of d-β-Asp-containing αA-crystallin in the lens, we prepared an antibody (anti-peptide 3R antibody) which reacts specifically with d-β-Asp-containing peptides [15]. The antibody crossreacted specifically to d-β-Asp-151-containing αA-crystallin. Immunohistochemical staining of human lens with the antibody demonstrated that d
Acknowledgements
This work was supported by a grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
References (21)
- et al.
Atherosclerosis
(1992) - et al.
J. Biol. Chem.
(1993) Methods Enzymol.
(1984)- et al.
Biochim. Biophys. Acta
(1994) - et al.
Biophys. Biochem. Res. Commun.
(1997) - et al.
Biophys. Biochem. Res. Commun.
(1999) - et al.
Biochem. Biophys. Res. Commun.
(1999) - et al.
Biochim. Biophys. Acta
(2001) - et al.
FEBS Lett.
(1990) - et al.
Exp. Eye Res.
(1997)
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