Biosynthesis and turnover of DOPA-containing proteins by human cells

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dc.contributor.author Rodgers, KJ
dc.contributor.author Hume, PM
dc.contributor.author Dunlop, RA
dc.contributor.author Dean, RT
dc.date.accessioned 2012-02-02T05:38:38Z
dc.date.issued 2004-12-01
dc.identifier.citation Free Radical Biology and Medicine, 2004, 37 (11), pp. 1756 - 1764
dc.identifier.issn 0891-5849
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/14668
dc.description.abstract Protein-bound 3,4-dihydroxyphenylalanine (PB-DOPA) is a major product of hydroxyl radical attack on tyrosine residues of proteins. Levels of PB-DOPA in cells and tissues have been shown to be greatly elevated in age-related diseases. We demonstrate for the first time that l-DOPA (levodopa) can be biosynthetically incorporated into cell proteins by human cells (THP-1 monocytes and monocyte-derived macrophages). The DOPA-containing proteins generated were selectively visualized on PVDF membranes using a redox-cycling staining method. Many cell proteins contained DOPA and seemed to be synthesized as their full-length forms. The cellular removal of DOPA-containing proteins by THP-1 cells was by proteolysis involving both the proteasomal and the lysosomal systems. The rate of cellular proteolysis of DOPA-containing proteins increased at lower levels of DOPA incorporation but decreased at higher levels of DOPA incorporation. The decreased rate of degradation was accompanied by an increase in the activity of cathepsins B and L but the activity of cathepsin S increased only at lower levels of DOPA incorporation. These data raise the possibility that PB-DOPA could be generated in vivo from l-DOPA, which is the most widely used treatment for Parkinson disease. © 2004 Elsevier Inc. All rights reserved.
dc.language eng
dc.relation.isbasedon 10.1016/j.freeradbiomed.2004.08.009
dc.title Biosynthesis and turnover of DOPA-containing proteins by human cells
dc.type Journal Article
dc.description.version Published
dc.parent Free Radical Biology and Medicine
dc.journal.volume 11
dc.journal.volume 37
dc.journal.number 11 en_US
dc.publocation Oxford, UK en_US
dc.identifier.startpage 1756 en_US
dc.identifier.endpage 1764 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 0601 Biochemistry and Cell Biology
dc.for 0304 Medicinal and Biomolecular Chemistry
dc.personcode 111642
dc.personcode 115899
dc.percentage 50 en_US
dc.classification.name Medicinal and Biomolecular Chemistry en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity ISI:000225366500009 en_US
dc.description.keywords Cathepsin
dc.description.keywords DOPA
dc.description.keywords Free radicals
dc.description.keywords Lysosome
dc.description.keywords Proteasome
dc.description.keywords Protein oxidation
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - Health Technologies
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc false
utslib.collection.history Closed (ID: 3)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)


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