Structure, function and role of lipoprotein lipase in lipoprotein metabolism. 1994

S Santamarina-Fojo, and K A Dugi
Molecular Disease Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland.

In the past several years the importance of lipoprotein lipase (LPL) as a multifunctional protein, involved in several different aspects of lipid and lipoprotein metabolism, has become evident. Thus, in addition to its traditional role in mediating the initial hydrolysis of circulating plasma triglycerides, recent studies implicate LPL in the binding of lipoproteins to cell surfaces and receptors, as well as indicating a potential role for LPL in the pathogenesis of atherosclerosis. Enhanced understanding of LPL structure, function and mechanism of action has provided insights into new potential pathways by which defects in LPL function may result in the development of different hyperlipidemic disorders and/or atherosclerosis.

UI MeSH Term Description Entries
D006949 Hyperlipidemias Conditions with excess LIPIDS in the blood. Hyperlipemia,Hyperlipidemia,Lipemia,Lipidemia,Hyperlipemias,Lipemias,Lipidemias
D008071 Lipoprotein Lipase An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and diacylglycerols. It occurs on capillary endothelial surfaces, especially in mammary, muscle, and adipose tissue. Genetic deficiency of the enzyme causes familial hyperlipoproteinemia Type I. (Dorland, 27th ed) EC 3.1.1.34. Heparin-Clearing Factor,Lipemia-Clearing Factor,Diacylglycerol Lipase,Diglyceride Lipase,Post-Heparin Lipase,Postheparin Lipase,Postheparin Lipoprotein Lipase,Factor, Heparin-Clearing,Factor, Lipemia-Clearing,Heparin Clearing Factor,Lipase, Diacylglycerol,Lipase, Diglyceride,Lipase, Lipoprotein,Lipase, Post-Heparin,Lipase, Postheparin,Lipase, Postheparin Lipoprotein,Lipemia Clearing Factor,Lipoprotein Lipase, Postheparin,Post Heparin Lipase
D008074 Lipoproteins Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes. Circulating Lipoproteins,Lipoprotein,Lipoproteins, Circulating
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001161 Arteriosclerosis Thickening and loss of elasticity of the walls of ARTERIES of all sizes. There are many forms classified by the types of lesions and arteries involved, such as ATHEROSCLEROSIS with fatty lesions in the ARTERIAL INTIMA of medium and large muscular arteries. Arterioscleroses
D014280 Triglycerides An ester formed from GLYCEROL and three fatty acid groups. Triacylglycerol,Triacylglycerols,Triglyceride

Related Publications

S Santamarina-Fojo, and K A Dugi
December 2002, Journal of molecular medicine (Berlin, Germany),
S Santamarina-Fojo, and K A Dugi
July 1997, The Proceedings of the Nutrition Society,
S Santamarina-Fojo, and K A Dugi
January 1983, Progress in lipid research,
S Santamarina-Fojo, and K A Dugi
January 1987, Przeglad lekarski,
S Santamarina-Fojo, and K A Dugi
June 2016, Current opinion in lipidology,
S Santamarina-Fojo, and K A Dugi
September 2000, Arteriosclerosis, thrombosis, and vascular biology,
S Santamarina-Fojo, and K A Dugi
March 1981, Journal of lipid research,
S Santamarina-Fojo, and K A Dugi
January 1994, International journal of clinical & laboratory research,
S Santamarina-Fojo, and K A Dugi
August 1999, Clinica chimica acta; international journal of clinical chemistry,
Copied contents to your clipboard!