Abstract:
: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.
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Sell DR,Monnier VMdoi
10.1196/annals.1333.015subject
Has Abstractpub_date
2005-06-01 00:00:00pages
118-28eissn
0077-8923issn
1749-6632pii
1043/1/118journal_volume
1043pub_type
杂志文章abstract::A sensitive, accurate, and simple method, called shifted termination assay (STA), was developed for detection of genetic mutations. The STA technology can be used to detect genetic mutations in polymerase chain reaction (PCR)-amplified samples of tissue, and plasma and serum that include circulating DNA containing poi...
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journal_title:Annals of the New York Academy of Sciences
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journal_title:Annals of the New York Academy of Sciences
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