PPARα L162V polymorphism alters the potential of n-3 fatty acids to increase lipoprotein lipase activity

2009 ◽  
Vol 54 (4) ◽  
pp. 543-550 ◽  
Author(s):  
Iwona Rudkowska ◽  
Dominique Caron-Dorval ◽  
Mélanie Verreault ◽  
Patrick Couture ◽  
Yves Deshaies ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Lipase Activity

Heparin-released lipolytic and esterolytic activities of human and rabbit plasmas

1961 ◽  
Vol 201 (5) ◽  
pp. 915-922 ◽  
Author(s):  
B. Shore ◽  
V. Shore
Keyword(s):  
Fatty Acids ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Ethyl Esters ◽  
Lipoprotein Lipase Activity ◽  
Hydrolysis Of

The enzymes released into both human and rabbit plasmas by heparin injection hydrolyzed, in addition to triglyceride moieties of lipoproteins, a number of mono- and diglycerides of C16 and C18 fatty acids after in vitro addition of the unemulsified glycerides to the plasma. In human postheparin plasma, these enzymes also hydrolyzed glycerides of butyric and caproic acids. The pure triglycerides and methyl or ethyl esters of C16 and C18 fatty acids were not substrates. The heparin-released activities for the hydrolysis of glycerides added in vitro persisted after all activity for the lipolysis of lipoproteins had been destroyed by heat. These activities also differed from lipoprotein lipase activity with respect to the effects of 1 m NaCl, dialysis, and aging the plasma at 4 C. It appears that heparin releases into the blood more than one enzyme or more than one form of an enzyme which may be involved in a stepwise degradation to fatty acids and glycerol of the triglyceride moieties of lipoproteins of density less than 1.007 g/ml.

Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8

2021 ◽  
Author(s):  
Kelli L. Sylvers-Davie ◽  
Brandon S.J. Davies
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Lipoprotein Metabolism ◽  
Fatty Acid Uptake ◽  
Extracellular Proteins ◽  
Current Understanding ◽  
Acid Uptake ◽  
Lipoprotein Lipase Activity

Triglyceride-rich lipoproteins deliver fatty acids to tissues for oxidation and for storage. Release of fatty acids from circulating lipoprotein triglycerides is carried out by lipoprotein lipase (LPL), thus LPL serves as a critical gatekeeper of fatty acid uptake into tissues. LPL activity is regulated by a number of extracellular proteins including three members of the angiopoietin-like family of proteins. In this review we discuss our current understanding of how, where, and when ANGPTL3, ANGPTL4, and ANGPTL8 regulate lipoprotein lipase activity, with a particular emphasis on how these proteins interact with each other to coordinate triglyceride metabolism and fat partitioning.

Long-chain fatty acids decrease lipoprotein lipase activity of cultured rat adipocyte precursors

Metabolism ◽  
1994 ◽  
Vol 43 (2) ◽  
pp. 144-151 ◽  
Author(s):  
James L. Kirkland ◽  
Charles H. Hollenberg ◽  
Sarah Kindler ◽  
Daniel A.K. Roncari
Keyword(s):  
Fatty Acids ◽  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Long Chain Fatty Acids ◽  
Lipoprotein Lipase Activity ◽  
Long Chain ◽  
Chain Fatty Acids

Effect of Triton on Lipoprotein Lipase of Rat Plasma

1957 ◽  
Vol 188 (2) ◽  
pp. 399-402 ◽  
Author(s):  
Michael C. Schotz ◽  
A. Scanu ◽  
Irvine H. Page
Keyword(s):  
Fatty Acids ◽  
Lipoprotein Lipase ◽  
Intravenous Injection ◽  
Optical Density ◽  
Lipase Activity ◽  
Coconut Oil ◽  
Rat Plasma ◽  
Plasma Lipoproteins ◽  
Lipoprotein Lipase Activity ◽  
Oil Emulsion

When postheparin plasma was incubated with a coconut oil substrate, a decrease in optical density and an increase in unesterified fatty acids occurred. The increase in unesterified acids was prevented by previous intravenous injection of Triton to rats. Addition of post-Triton plasma to a system containing postheparin plasma and coconut oil emulsion inhibited the lipoprotein lipase activity. Incubation of Triton with coconut oil substrate before addition of postheparin plasma caused inhibition of lipoprotein lipase activity. It is concluded that inhibition of lipoprotein lipase activity by Triton is due to modification of the substrate such that the enzyme can no longer act. Further, it is suggested that the chief cause of Triton hyperlipemia is coating of the plasma lipoproteins by Triton resulting in their faulty catabolism.

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