PMID- 14670006
OWN - NLM
STAT- MEDLINE
DCOM- 20040520
LR  - 20190922
IS  - 1071-5762 (Print)
IS  - 1029-2470 (Linking)
VI  - 37
IP  - 9
DP  - 2003 Sep
TI  - Protein hydroperoxides are a major product of low density lipoprotein oxidation 
      during copper, peroxyl radical and macrophage-mediated oxidation.
PG  - 983-91
AB  - Damage to apoB100 on low density lipoprotein (LDL) has usually been described in 
      terms of lipid aldehyde derivatisation or fragmentation. Using a modified FOX 
      assay, protein hydroperoxides were found to form at relatively high 
      concentrations on apoB100 during copper, 2,2'-azobis(amidinopropane) 
      dihydrochloride (AAPH) generated peroxyl radical and cell-mediated LDL oxidation. 
      Protein hydroperoxide formation was tightly coupled to lipid oxidation during 
      both copper and AAPH-mediated oxidation. The protein hydroperoxide formation was 
      inhibited by lipid soluble alpha-tocopherol and the water soluble antioxidant, 
      7,8-dihydroneopterin. Kinetic analysis of the inhibition strongly suggests 
      protein hydroperoxides are formed by a lipid-derived radical generated in the 
      lipid phase of the LDL particle during both copper and AAPH mediated oxidation. 
      Macrophage-like THP-1 cells were found to generate significant protein 
      hydroperoxides during cell-mediated LDL oxidation, suggesting protein 
      hydroperoxides may form in vivo within atherosclerotic plaques. In contrast to 
      protein hydroperoxide formation, the oxidation of tyrosine to protein bound 
      3,4-dihydroxyphenylalanine (PB-DOPA) or dityrosine was found to be a relatively 
      minor reaction. Dityrosine formation was only observed on LDL in the presence of 
      both copper and hydrogen peroxide. The PB-DOPA formation appeared to be 
      independent of lipid peroxidation during copper oxidation but tightly associated 
      during AAPH-mediated LDL oxidation.
FAU - Gieseg, Steven P
AU  - Gieseg SP
AD  - Free Radical Biochemistry Laboratory, Department of Zoology, University of 
      Canterbury, Private Bag 4800, Christchurch, New Zealand. 
      s.gieseg@zool.canterbury.ac.nz
FAU - Pearson, Joseph
AU  - Pearson J
FAU - Firth, Carole A
AU  - Firth CA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Free Radic Res
JT  - Free radical research
JID - 9423872
RN  - 0 (Amidines)
RN  - 0 (Apolipoprotein B-100)
RN  - 0 (Apolipoproteins B)
RN  - 0 (Lipoproteins, LDL)
RN  - 0 (Peroxides)
RN  - 3170-83-0 (perhydroxyl radical)
RN  - 7381JDR72F (2,2'-azobis(2-amidinopropane))
RN  - 789U1901C5 (Copper)
RN  - BBX060AN9V (Hydrogen Peroxide)
SB  - IM
MH  - Adult
MH  - Amidines/metabolism
MH  - Apolipoprotein B-100
MH  - Apolipoproteins B/metabolism
MH  - Cells, Cultured
MH  - Copper/*metabolism
MH  - Female
MH  - Humans
MH  - Hydrogen Peroxide/*metabolism
MH  - *Lipid Peroxidation
MH  - Lipoproteins, LDL/*metabolism
MH  - Macrophages/*metabolism
MH  - Male
MH  - Middle Aged
MH  - Peroxides/*metabolism
EDAT- 2003/12/13 05:00
MHDA- 2004/05/21 05:00
CRDT- 2003/12/13 05:00
PHST- 2003/12/13 05:00 [pubmed]
PHST- 2004/05/21 05:00 [medline]
PHST- 2003/12/13 05:00 [entrez]
AID - 10.1080/10715760310001603612 [doi]
PST - ppublish
SO  - Free Radic Res. 2003 Sep;37(9):983-91. doi: 10.1080/10715760310001603612.