Free Fatty Acids in Plasma May Exert Feed-Back Control of Lipoprotein Lipase Activity

2009 ◽  
Vol 51 (1) ◽  
pp. 18-19
Author(s):  
John G. Coniglio
Keyword(s):  
Fatty Acids ◽  
Free 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.

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

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
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