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Ornithine Is a Novel Amino Acid and a Marker of Arginine Damage by Oxoaldehydes in Senescent Proteins
aInstitute of Pathology and bDepartment of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, USA
Address for correspondence: David R. Sell, Institute of Pathology, Case Western Reserve University, 2085 Adelbert Rd., Cleveland, OH 44106. Voice: 216-368-2930; fax: 216-368-0495. drs7{at}po.cwru.edu
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.
Key Words: ornithine • arginine • skin • collagen • lens crystallins • aging • advanced glycation end product (AGE) • glycation • Maillard reaction This article has been cited by other articles:
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