The effect of high intensity interval exercise on postprandial triacylglycerol and leukocyte activation - monitored for 48h post exercise

Peer reviewedPublisher PD

Plasma Cholesteryl Ester Transfer Protein (CETP) in Relation to Human Pathophysiology

Plasma CETP was initially isolated as a highly purified 74 kD protein. The human CETP gene is located at chromosome 16q13, near the locus of the lecithin cholesterol acyltransferase (LCAT) gene. The CETP gene consists of 16 exons, spanning 25 kb. The CETP mRNA encodes 476 amino acids. The mature CETP contains four N-linked sugars with a variable glycosylation site of 341Asn. CETP mRNA is expressed in various tissues, but liver cells, adipocytes, and macrophages are abundant sources. One of the determinants of high density lipoprotein (HDL) neutral lipid composition is plasma CETP. In incubated human plasma, transfer and equilibration of (LCAT)-generated cholesteryl ester (CE) is found. Humans, hamsters, guinea pigs, and chickens belong to a group with intermediate CETP activity. Plasma CETP binds neutral lipids CE or triglyceride (TG), and phospholipid (PL) on HDL3, but CETP selectively promotes an exchange of CE and TG among lipoproteins. On the one hand, HDL-TG can be hydrolyzed by hepatic lipase, and on the other hand, plasma CETP decreases HDL particle size via CE/TG exchange between chylomicron/VLDL and HDL. Thus, CETP thereby accelerates the catabolic rate of HDL apolipoproteins. CETP enhances HDL remodeling from large HDL to small subclasses including pre-HDL. However, CETP deficiency would decrease cholesterol esterification rate, thereby inhibiting maturation of preb-HDL to α-migrating spherical HDL. Therefore, in CETP deficiency, large-to-small HDL remodeling is decreased and preb-HDL catabolism is also decreased. © 2010 Elsevier Inc. All rights reserved.[Book Chapter

MISE EN EVIDENCE DE NOUVELLES FONCTIONS DE LA LIPOPROTEINE LIPASE LIEE AUX LIPOPROTEINES DE TRES BASSE DENSITE

LYON1-BU Santé (693882101) / SudocPARIS-BIUM (751062103) / SudocPARIS-BIUP (751062107) / SudocSudocFranceF

The transfer of VLDL-associated phospholipids to activated platelets depends upon cytosolic phospholipase A2 activity.: Mechanism of VLDL phospholipid transfer to platelets

International audienceWe previously reported that VLDL could transfer phospholipids (PLs) to activated platelets. To identify the metabolic pathway involved in this process, the transfer of radiolabeled PLs from VLDL (200 microM PL) to platelets (2 x 10(8)/ml) was measured after incubations of 1 h at 37 degrees C, with or without thrombin (0.1 U/ml) or LPL (500 ng/ml), in the presence of various inhibitors, including aspirin, a cyclooxygenase inhibitor (300 microM); esculetin, a 12-lipoxygenase inhibitor (20 microM); methyl-arachidonyl-fluorophosphonate (MAFP), a phospholipase A(2) (PLA(2)) inhibitor (100 microM); 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetrakis (acetoxymethyl) ester (BAPTA-AM), a Ca(2+) chelator (20 microM); bromoenol lactone (BEL), a Ca(2+)- independent phospholipase A(2) (iPLA(2)) inhibitor (100 nM); and 1-[6-[[17beta-3-methoxyestra-1,3,5(10)-trien-17-yl-]amino]hexyl]1H-pyrrole-2,5-dione (U73122), a phospholipase C (PLC) inhibitor (20 microM). Aspirin and esculetin had no effect, showing that PL transfer was not dependent upon cyclooxygenase or lipoxygenase pathways. The transfer of PL was inhibited by MAFP, U73122, and BAPTA-AM. Although MAFP inhibited both cytosolic phospholipase A(2) (cPLA(2)) and iPLA(2), only cPLA(2) is a calcium-dependent enzyme. Because calcium mobilization is favored by PLC and inhibited by BAPTA-AM, the transfer of PL from VLDL to platelets appeared to result from a cPLA(2)-dependent process. The inhibition of iPLA(2) by BEL had no effect on PL transfers

Binding of anti lipoprotein lipase immunoglobulins to chylomicrons in autoimmune type I hyperlipidemia

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Alterations in the transfer of phospholipids from very-low density lipoproteins to activated platelets in type 2 diabetes

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