PMID- 2302415
OWN - NLM
STAT- MEDLINE
DCOM- 19900319
LR  - 20190609
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1042
IP  - 2
DP  - 1990 Feb 6
TI  - Sensitivity of tryptophan and related compounds to oxidation induced by lipid 
      autoperoxidation. Application to human serum low- and high-density lipoproteins.
PG  - 159-67
AB  - Tryptamine, serotonin and tryptophan are readily oxidized during the 
      Cu2+-catalyzed peroxidation of arachidonic acid (AA) at neutral pH and under 
      certain experimental conditions which determine their relative susceptibility to 
      oxidation. Thus, in AA micelles, fluorescence spectroscopy demonstrates that 
      positively-charged indoles interact with negatively-charged micelles while Trp 
      remains in the aqueous phase. As a result, serotonin and tryptamine are 
      preferentially oxidized. In egg phosphatidylcholine liposomes loaded with AA, the 
      three substrates interact with vesicles and undergo lipid-induced oxidation. EDTA 
      inhibits the formation of thiobarbituric-reactive substances (TBARS) and prevents 
      the indoles from oxidation. Owing to the intricate contact between the lipidic 
      core and the apolipoproteins, the Trp residues of human serum LDL and HDL3 are 
      very rapidly oxidized, i.e., at least one order of magnitude faster than Tyr HDL 
      and Lys LDL, which are believed to be involved in the binding of these 
      lipoproteins to their cell receptors. Cupric ions are rather specific for the 
      lipid-induced autoxidation of Trp residues of lipoproteins whereas in micelles 
      and liposomes, Mn2+ and Fe2+ can lead to TBARS production and to oxidation of 
      indoles. This specificity is surprising considering the known ability of Fe2+ to 
      catalyze LDL modification (measured by TBARS production) during their incubation 
      with various cells. Biological consequences of the easy lipid-induced oxidation 
      of biologically important indoles are discussed.
FAU - Reyftmann, J P
AU  - Reyftmann JP
AD  - Laboratoire de Physico-Chimie de l'Adaptation Biologique, INSERM U 312, Museum 
      National d'Histoire Naturelle, Paris, France.
FAU - Santus, R
AU  - Santus R
FAU - Maziere, J C
AU  - Maziere JC
FAU - Morliere, P
AU  - Morliere P
FAU - Salmon, S
AU  - Salmon S
FAU - Candide, C
AU  - Candide C
FAU - Maziere, C
AU  - Maziere C
FAU - Haigle, J
AU  - Haigle J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Indoles)
RN  - 0 (Lipoproteins, HDL)
RN  - 0 (Lipoproteins, LDL)
RN  - 0 (Liposomes)
RN  - 0 (Micelles)
RN  - 0 (Tryptamines)
RN  - 333DO1RDJY (Serotonin)
RN  - 422ZU9N5TV (tryptamine)
RN  - 8DUH1N11BX (Tryptophan)
SB  - IM
MH  - Humans
MH  - Indoles/metabolism
MH  - Kinetics
MH  - *Lipid Peroxidation
MH  - Lipoproteins, HDL/*blood
MH  - Lipoproteins, LDL/*blood
MH  - Liposomes
MH  - Micelles
MH  - Oxidation-Reduction
MH  - Serotonin/metabolism
MH  - Spectrometry, Fluorescence
MH  - Tryptamines/metabolism
MH  - Tryptophan/*metabolism
EDAT- 1990/02/06 00:00
MHDA- 1990/02/06 00:01
CRDT- 1990/02/06 00:00
PHST- 1990/02/06 00:00 [pubmed]
PHST- 1990/02/06 00:01 [medline]
PHST- 1990/02/06 00:00 [entrez]
AID - 0005-2760(90)90002-F [pii]
AID - 10.1016/0005-2760(90)90002-f [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1990 Feb 6;1042(2):159-67. doi: 
      10.1016/0005-2760(90)90002-f.