Journal
EXPERIMENTAL EYE RESEARCH
Volume 209, Issue -, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exer.2021.108679
Keywords
Protein crosslinking; Mass spectrometry; Dehydroalanine; Long-lived proteins; Succinimide
Categories
Funding
- Mass Spectrometry Research Center at Vanderbilt University [R01 EY013462, R01 EY024258, P30 EY008126, R01 EY013570]
Ask authors/readers for more resources
Recent research has revealed that certain amino acids can lead to protein crosslinking through non-enzymatic mechanisms in long-lived proteins in aged individuals. The lens serves as a valuable model tissue for studying crosslinking mechanisms that may also occur in other human tissues.
Although protein crosslinking is often linked with aging as well as some age-related diseases, very few molecular details are available on the nature of the amino acids involved, or mechanisms that are responsible for crosslinking. Recent research has shown that several amino acids are able to generate reactive intermediates that ultimately lead to covalent crosslinking through multiple non-enzymatic mechanisms. This information has been derived from proteomic investigations on aged human lenses and the mechanisms of crosslinking, in each case, have been elucidated using model peptides. Residues involved in spontaneous protein-protein crosslinking include aspartic acid, asparagine, cysteine, lysine, phosphoserine, phosphothreonine, glutamic acid and glutamine. It has become clear, therefore, that several amino acids can act as potential sites for crosslinking in the long-lived proteins that are present in aged individuals. Moreover, the lens has been an invaluable model tissue and source of crosslinked proteins from which to determine crosslinking mechanisms that may lead to crosslinking in other human tissues.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available