Metabolic fate of an oral tracer dose of [13C]docosahexaenoic acid triglycerides in the rat
Autor: | Jean Lecerf, Martine Croset, J. L. Tayot, Veronique Chirouze, N. Brossard, Jean-Paul Riou, Michel Lagarde, Christiane Pachiaudi, O. Macovschi, Sylvie Normand |
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Rok vydání: | 1996 |
Předmět: |
Blood lipoprotein
Male medicine.medical_specialty Time Factors Docosahexaenoic Acids Physiology Lipoproteins Administration Oral Biology Blood cell Rats Sprague-Dawley chemistry.chemical_compound Physiology (medical) Internal medicine medicine Animals Platelet Phospholipids Serum Albumin Triglycerides Carbon Isotopes Blood Cells Triglyceride Albumin Brain Metabolism Lipids Rats Endocrinology medicine.anatomical_structure Biochemistry chemistry Docosahexaenoic acid Lipoprotein |
Zdroj: | The American journal of physiology. 270(4 Pt 2) |
ISSN: | 0002-9513 |
Popis: | The appearance of 13C in rat lipoprotein, blood cells, and brain lipids was followed as a function of time after the ingestion of triglycerides (TG) containing [13C]22:6n-3. The time course of 13C abundance in 22:6n-3 of various lipid pools, measured by gas chromatography combustion-isotope mass spectrometry, established precursor-product relationships within lipids. The [13C]22:6n-3 was rapidly incorporated into very low density lipoprotein-chylomicron-TG and unesterified fatty acids bound to albumin, with a concomitant maximal appearance at 3 h and further decline. Lysophosphatidylcholines (lysoPC) bound to albumin were also enriched in [13C]22:6n-3, and their labeling appeared to be mainly due to hepatic secretion at the earliest time points. From 12 h postingestion, the synthesis of [13C]22:6n-3-lysoPC was twice as high as that of unesterified [13C]22:6n-3, making lysoPC a potential source of 22:6n-3 supply for tissues. The labeling of platelets, red blood cells, and brain phospholipids presented different kinetics, presumably involving the two lipid forms of [13C]22:6n-3 bound to albumin, to different extents. We conclude that [13C]22:6n-3 esterified in TG is rapidly redistributed within blood lipoproteins and the albumin fraction and that its incorporation in lipid species bound to albumin influences its uptake by target tissues. |
Databáze: | OpenAIRE |
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