Lipoprotein apoC-III activation of lipoprotein lipase. Modulation by apolipoprotein A-IV

Lipoprotein lipase (LPL)-mediated hydrolysis of triglycerides (TG) contained in chylomicrons requires the presence of a cofactor, apolipoprotein (apo) C-II. The physiological mechanism by which chylomicrons gain apoC-II necessary for LPL activation in whole plasma is not known. Using a gum arabic st...

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Veröffentlicht in:The Journal of biological chemistry 1990-01, Vol.265 (8), p.4266-4272
Hauptverfasser: Goldberg, I J, Scheraldi, CA, Yacoub, L K, Saxena, U, Bisgaier, CL
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container_end_page 4272
container_issue 8
container_start_page 4266
container_title The Journal of biological chemistry
container_volume 265
creator Goldberg, I J
Scheraldi, CA
Yacoub, L K
Saxena, U
Bisgaier, CL
description Lipoprotein lipase (LPL)-mediated hydrolysis of triglycerides (TG) contained in chylomicrons requires the presence of a cofactor, apolipoprotein (apo) C-II. The physiological mechanism by which chylomicrons gain apoC-II necessary for LPL activation in whole plasma is not known. Using a gum arabic stabilized TC emulsion, activation of LPL by lipoprotein apoC-II was studied. Hydrolysis of TG by LPL was greater in the presence of serum than with addition of either high density lipoproteins (HDL) or very low density lipoproteins (VLDL). Our studies demonstrate that apoA-IV increases LPL activation in the presence of lipoproteins. We hypothesize that apoA-IV is required for efficient release of apoC-II from either HDL or VLDL, which then allows for LPL-mediated hydrolysis of TG in nascent chylomicrons.
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source EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects apolipoprotein A-IV
apolipoprotein C-II
title Lipoprotein apoC-III activation of lipoprotein lipase. Modulation by apolipoprotein A-IV
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