PMID- 20083224
OWN - NLM
STAT- MEDLINE
DCOM- 20100611
LR  - 20161125
IS  - 1878-5875 (Electronic)
IS  - 1357-2725 (Linking)
VI  - 42
IP  - 5
DP  - 2010 May
TI  - Radical sequestration by protein-bound 3,4-dihydroxyphenylalanine.
PG  - 755-61
LID - 10.1016/j.biocel.2010.01.015 [doi]
AB  - Protein-bound 3,4-dihydroxyphenylalanine (PB-DOPA), a redox-active product of 
      protein oxidation, is capable of functioning as both a pro- and antioxidant. A 
      number of in vitro and in vivo studies have demonstrated a toxic, non-toxic or 
      even beneficial effect of free DOPA, however little investigation has examined 
      the physiological activity of PB-DOPA. Being the major treatment available for 
      Parkinson's disease, most studies have focused on the effect of DOPA within 
      neurological cells or tissues, although the presence of PB-DOPA in other 
      locations, for example within atherosclerotic plaques, suggests that broader 
      research is needed to fully understand the physiological effects of both free and 
      PB-DOPA. We hypothesise that the generation of PB-DOPA can trigger an enhancement 
      of the cellular antioxidant defence system, thus enabling PB-DOPA to restrict and 
      potentially terminate the initiating oxidative stress, minimising the level of 
      oxidative damage. Using luminol-enhanced chemiluminescence, we demonstrate that 
      free DOPA is capable of direct peroxyl radical scavenging, even in the presence 
      of competing scavengers, and has a different effect to that of the parent amino 
      acid, tyrosine. Furthermore, we show that both free and PB-DOPA, in combination 
      or individually, were able to protect monocytes and macrophages from peroxyl 
      radical-induced oxidative stress in vitro. These results confirm a role for both 
      free and PB-DOPA in cellular antioxidant defences and suggest the possibility of 
      using DOPA as a potential therapeutic for the treatment of diseases involving 
      oxidative stress or the accumulation of oxidative damage.
CI  - 2010 Elsevier Ltd. All rights reserved.
FAU - Nelson, Michelle
AU  - Nelson M
AD  - Faculty of Applied Science, University of Canberra, Canberra, ACT 2601, 
      Australia. michelle.nelson@canberra.edu.au
FAU - Foxwell, A Ruth
AU  - Foxwell AR
FAU - Tyrer, Peter
AU  - Tyrer P
FAU - Dean, Roger T
AU  - Dean RT
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100118
PL  - Netherlands
TA  - Int J Biochem Cell Biol
JT  - The international journal of biochemistry & cell biology
JID - 9508482
RN  - 0 (Amidines)
RN  - 0 (Free Radical Scavengers)
RN  - 0 (Luminescent Agents)
RN  - 0 (Oxidants)
RN  - 0 (Proteins)
RN  - 42HK56048U (Tyrosine)
RN  - 46627O600J (Levodopa)
RN  - 7381JDR72F (2,2'-azobis(2-amidinopropane))
SB  - IM
MH  - Amidines/toxicity
MH  - Animals
MH  - Atherosclerosis/prevention & control
MH  - Cell Differentiation
MH  - Cell Line
MH  - Cell Survival/drug effects
MH  - Cytoprotection/drug effects
MH  - Dose-Response Relationship, Drug
MH  - Free Radical Scavengers/chemistry/*metabolism/pharmacology
MH  - Humans
MH  - Levodopa/chemistry/*metabolism/pharmacology
MH  - Luminescent Agents
MH  - Mice
MH  - Monocytes/cytology/drug effects/metabolism
MH  - Oxidants/toxicity
MH  - Oxidation-Reduction
MH  - Oxidative Stress/*drug effects
MH  - Protein Transport
MH  - Proteins/chemistry/*metabolism
MH  - Tyrosine/chemistry
EDAT- 2010/01/20 06:00
MHDA- 2010/06/12 06:00
CRDT- 2010/01/20 06:00
PHST- 2009/10/08 00:00 [received]
PHST- 2009/12/17 00:00 [revised]
PHST- 2010/01/12 00:00 [accepted]
PHST- 2010/01/20 06:00 [entrez]
PHST- 2010/01/20 06:00 [pubmed]
PHST- 2010/06/12 06:00 [medline]
AID - S1357-2725(10)00033-6 [pii]
AID - 10.1016/j.biocel.2010.01.015 [doi]
PST - ppublish
SO  - Int J Biochem Cell Biol. 2010 May;42(5):755-61. doi: 
      10.1016/j.biocel.2010.01.015. Epub 2010 Jan 18.