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Ornithine Is a Novel Amino Acid and a Marker of Arginine Damage by Oxoaldehydes in Senescent Proteins
Author(s) -
SELL DAVID R.,
MONNIER VINCENT M.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1333.015
Subject(s) - glycation , arginine , ornithine , lysine , chemistry , amino acid , hydrolysis , biochemistry , acid hydrolysis , in vivo , biology , genetics , receptor
A bstract : Long‐lived proteins undergo age‐related postsynthetic modifications by glycation and advanced glycation end products (AGEs), which destabilize them by altering their conformation and charge. It was accidentally discovered that ornithine (orn) increased with age in acid hydrolyzates of human skin collagen and lens crystallins which led us to investigate the source of orn. Here, we detected such modifications of orn in these proteins. Acid hydrolysis of arginine (arg)‐base AGE standards produced orn at different yields. The data provide unequivocal evidence for the in vivo formation of orn and its own AGEs in aging proteins, and suggest that arg‐based AGEs serve as precursors of orn.