Distribution and breakdown of labeled coenzyme Q10 in rat

被引:116
作者
Bentinger, M [1 ]
Dallner, G
Chojnacki, T
Swiezewska, E
机构
[1] Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden
[2] Polish Acad Sci, Inst Biochem & Biophys, Warsaw, Poland
关键词
labeled coenzyme Q(10); coenzyme Q(10) uptake; intracellular localization; cellular breakdown; phosphorylation; excretion of metabolites; free radicals;
D O I
10.1016/S0891-5849(02)01357-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Radioactive coenzyme Q(10) ([H-3]CoQ) was synthesized in a way that the metabolites produced retained the radioactivity. Administration of the lipid to rats intraperitoneally resulted in an efficient uptake into the circulation, with high concentrations found in spleen, liver, and white blood cells; lower concentrations in adrenals, ovaries, thymus, and heart; and practically no uptake in kidney, muscle, and brain. In liver homogenate most [H-3]CoQ appeared in the organelles, but it was also present in the cytosol and transport vesicles. Mitochondria, purified on a metrizamide gradient, had a very low concentration of [H-3]CoQ, which was mainly present in the lysosomes. All organs that took up the labeled lipid also contained water-soluble metabolites. The majority of metabolites excreted through the kidney and appeared in the urine. Some metabolites were also present in the feces, which further contained nonmetabolized [H-3]CoQ, excreted through the bile. The major metabolites were purified from the urine, and the mass spectrometric fragmentation showed that these compounds, containing the ring with a short side chain, are phosphorylated. Thus, the results demonstrate that CoQ is metabolized in all tissues, the metabolites are phosphorylated in the cells, transported in the blood to the kidney, and excreted into the urine. (C) 2003 Elsevier Science Inc.
引用
收藏
页码:563 / 575
页数:13
相关论文
共 43 条
[31]   MEASUREMENT OF PROTEIN USING BICINCHONINIC ACID [J].
SMITH, PK ;
KROHN, RI ;
HERMANSON, GT ;
MALLIA, AK ;
GARTNER, FH ;
PROVENZANO, MD ;
FUJIMOTO, EK ;
GOEKE, NM ;
OLSON, BJ ;
KLENK, DC .
ANALYTICAL BIOCHEMISTRY, 1985, 150 (01) :76-85
[32]   UBIQUINOL-10 PROTECTS HUMAN LOW-DENSITY-LIPOPROTEIN MORE EFFICIENTLY AGAINST LIPID-PEROXIDATION THAN DOES ALPHA-TOCOPHEROL [J].
STOCKER, R ;
BOWRY, VW ;
FREI, B .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (05) :1646-1650
[33]   HALF-LIFE OF UBIQUINONE-9 IN RAT-TISSUES [J].
THELIN, A ;
SCHEDIN, S ;
DALLNER, G .
FEBS LETTERS, 1992, 313 (02) :118-120
[34]  
TOLLBOM O, 1988, J BIOL CHEM, V263, P1347
[35]  
Turunen M, 1999, J NUTR, V129, P2113
[36]   Elevation of ubiquinone content by peroxisomal inducers in rat liver during aging [J].
Turunen, M ;
Dallner, G .
CHEMICO-BIOLOGICAL INTERACTIONS, 1998, 116 (1-2) :79-91
[37]   β2-integrin and lipid modifications indicate a non-antioxidant mechanism for the anti-atherogenic effect of dietary coenzyme Q10 [J].
Turunen, M ;
Wehlin, L ;
Sjöberg, M ;
Lundahl, J ;
Dallner, G ;
Brismar, K ;
Sindelar, PJ .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2002, 296 (02) :255-260
[38]   Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human:: a gene required for ubiquinone biosynthesis with potential implications for aging [J].
Vajo, Z ;
King, LM ;
Jonassen, T ;
Wilkin, DJ ;
Ho, N ;
Munnich, A ;
Clarke, CF ;
Francomano, CA .
MAMMALIAN GENOME, 1999, 10 (10) :1000-1004
[39]   Subcellular localization of plastoquinane and ubiquinone synthesis in spinach cells [J].
Wanke, M ;
Dallner, G ;
Swiezewska, E .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2000, 1463 (01) :188-194
[40]   ISOLATION OF RAT-LIVER LYSOSOMES BY ISOPYCNIC CENTRIFUGATION IN A METRIZAMIDE GRADIENT [J].
WATTIAUX, R ;
WATTIAUXDECONINCK, S ;
RONVEAUXDUPAL, MF ;
DUBOIS, F .
JOURNAL OF CELL BIOLOGY, 1978, 78 (02) :349-368