Polysaccharide interactions with plasma lipoproteins and lipoprotein lipase.

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by , [Uppsala
Blood lipoproteins., Lipoprotein lipase., Polysacchar
SeriesAbstracts of Uppsala dissertations from the Faculty of Medicine ;, 113, Acta Universitatis Upsaliensis, Acta Universitatis Upsaliensis., 113.
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LC ClassificationsQP99.3.L52 I9
The Physical Object
Pagination19 p.
ID Numbers
Open LibraryOL3136683M
LC Control Number82463729

Polysaccharide interactions with plasma lipoproteins and lipoprotein lipase Iverius, Per-Henrik Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine. While we are reasonably certain that lipoprotein lipase is available for action extracellularly at the capillary endothelium we do not know how it gets there or how it is bound there.

This report will focus on the possibility that the enzyme is attached to the endothelium through interaction with a sulfated by: 8. obtained with milk lipoprotein lipase. However, the interaction between the hepatic Theability ofthe polysaccharides to release lipoprotein lipase to triacylglycerol of plasma lipoproteins.

Interaction of lipoprotein lipase with native and modified heparin-like polysaccharides Article (PDF Available) in Biochemical Journal (3) October with 25 Reads How we measure 'reads'.

Lipoprotein lipase (LPL) is a key enzyme in lipid and lipoprotein metabolism. The canonical role of LPL involves the hydrolysis of triglyceride-rich lipoproteins for the provision of FFAs to metabolic tissues. However, LPL may also contribute to lipoprotein uptake by acting as a molecular bridge between lipoproteins and cell surface : Kimberley D.

Bruce, Maoping Tang, Philip Reigan, Robert H. Eckel. The primary function of plasma lipoproteins is to transport hydrophobic, water-insoluble lipids within the circulation to other tissues. The TG-rich lipoproteins contain apo B and deliver TGs made in the liver and intestine to other tissues in the body for either storage or utilization as an energy source.

This may be due to a defective interaction of chylomicrons and very low density lipoproteins with lipoprotein lipase. Since the glycosaminoglycan, heparan sulfate, was found to stimulate the. Insulin resistance and type 2 diabetes are associated with a clustering of interrelated plasma lipid and lipoprotein abnormalities, which include reduced HDL cholesterol, a predominance of small dense LDL particles, and elevated triglyceride levels.

Each of these dyslipidemic features Polysaccharide interactions with plasma lipoproteins and lipoprotein lipase. book associated with an increased risk of cardiovascular disease. Low-Mrheparin, lipoprotein lipase and hepatic lipase E a Eg en 0 coi 10 20 30 40 50 60 70 0 0 10 20 30 40 Time(min) Fig.

Effect of size-fractionated. Interaction of lipoprotein lipase with heparin–Sepharose. Evaluation of conditions for affinity binding Article (PDF Available) in Biochemical Journal (1) November with 22 Reads.

Details Polysaccharide interactions with plasma lipoproteins and lipoprotein lipase. FB2

One of these enzymes, lipoprotein lipase (LPL), has been found in several tissue homogenates, including adipose tissue, heart and mammary gland (Korn, ) as well as milk (Quigley et al., ).

LPL is released from its membrane site by high molecular weight polyanions, in particular sulfated polysaccharides (Robinson, ). Lipoprotein lipase (LPL) is a key enzyme in the regulation of the flux of fatty acids.

LPL hydrolyses triglycerides in chylomicrons and very-low-density lipoproteins (VLDL), forming intermediate- (IDL) and low-density lipoproteins (LDL).

Hepatic lipase (HL) is a related enzyme with a more restricted. Lipoprotein lipase (LPL) (EC ) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins, such as those found in chylomicrons and very low-density lipoproteins (VLDL), into two free fatty acids and one monoacylglycerol molecule.

Musliner TA, Herbert PN, Kingston MJ. Lipoprotein substrates of lipoprotein lipase and hepatic triacylglycerol lipase from human post-heparin plasma. Biochim Biophys Acta. Nov 21; (2)– Kuusi T, Kinnunen PK, Nikkilä EA. Hepatic endothelial lipase antiserum influences rat plasma low and high density lipoproteins in vivo.

Iverius PH. The interaction between human plasma lipoproteins and connective tissue glycosaminoglycans. J Biol Chem. Apr 25; (8)– [Google Scholar] Iverius PH, Ostlund-Lindqvist AM. Lipoprotein lipase from bovine milk.

Isolation procedure, chemical characterization, and molecular weight analysis. This hydrophobic core is surrounded by a hydrophilic membrane consisting of phospholipids, free cholesterol, and apolipoproteins (Figure 1). Plasma lipoproteins are divided into seven classes based on size, lipid composition, and apolipoproteins (Table 1 and Figure 2).

Figure 1: Lipoprotein Structure (figure modified from Biochemistry Alcohol consumption affects a number of steps in plasma lipoprotein metabolism: it serves as a substrate for lipoprotein triglyceride synthesis, alters synthesis of apolipoproteins, and affects the activity of the key enzymes of lipoprotein metabolism, namely lipoprotein lipase and hepatic lipase, and cholesterol ester transfer protein.

The polycation protamine impedes the catabolism of triglyceride-rich lipoproteins and this has been suggested to be due to intravascular inactivation of lipoprotein lipase. We have made intravenous injections of protamine to rats and found that both lipoprotein lipase and hepatic lipase activities were released to plasma.

LIVER IN LIPOPROTEIN METABOLISM Pages with reference to book, From To Anjum Shahid (PMRC Research Centre, Jinnah Postgraduate Medical Centre, Karachi.) Ever plays a major role in cholesterol and lipoprotein metabolism and is the major site of production and removal of cholesterol rich lipoproteins and bile acids.

lipoprotein metabolism is the process by which hydrophobic lipids, namely triglycerides and cholesterol, are transported within the interstitial fluid and plasma.

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It includes the transport of energy in the form of triglycerides from intestine and liver to muscles and adipose, as well as the transport of cholesterol both from intestine and liver. This book includes problems of lipoprotein heterogeneity and quantitation.

It discusses apolipoproteins B and B, because of interest in post-prandial lipoproteins and their contribution to risk for atherosclerosis and coronary disease. Plasma from individuals with remnant removal disease exhibit a broad band of material that migrates between β-lipoproteins (LDL) and pre-β-lipoproteins (VLDL) on electrophoresis.

Hence, the term broad β disease also has been used to describe remnant removal disease (31). β-Migrating VLDLs also are believed to be enriched in RLPs. Introduction. Recently, elevated plasma triglyceride levels have been shown to be an independent risk factor for cardiovascular disease.[] It has long been recognized that lipoprotein lipase (LPL) is the essential enzyme involved in the lipolytic processing of triglycerides in chylomicrons and very low density lipoproteins (VLDL) in peripheral tissues.[2–6] Indeed, some patients with.

Information on EC - lipoprotein lipase for references in articles please use BRENDA:EC   Lipoprotein lipases from a variety of sources have been shown previously to bind to heparin and some related polysaccharides. For the present studies lipoprotein lipase purified from bovine milk was used.

In batch experiments binding of the enzyme activity to heparin–Sepharose occurred relatively slowly, so that 30min was required for the. Lipid profile of individuals with complete hepatic lipase deficiency is characterized by elevated plasma cholesterol and triglyceride levels, triglyceride enrichment of lipoprotein fractions with a density > g/Ml, the presence of a β-VLDL, and an impaired metabolism of postprandial triglyceride-rich lipoproteins [, ].

Apolipoprotein C-II (apoC-II), a 78 amino acid protein found in chylomicrons, VLDL and high density lipoproteins (HDL) is metabolically important as the activator for lipoprotein lipase.

The precise molecular mechanism by which apoC-II enhances triglyceride hydrolysis by the enzyme is not yet known. Abstract The aim of this study was to investigate the potential interaction between the lipoprotein lipase (LPL) HindIII polymorphism and visceral adipose tissue (AT) accumulation in the modulation of triglyceride levels in visceral LPL-HindIII genotype was determined by polymerase chain reaction in 52 -three subjects were heterozygous (+/−) and 28 were homozygous.

Background. Lipoprotein lipase (LPL) hydrolyses triglycerides (TG) in circulating lipoproteins [1,2].This is a necessary first step in catabolism of the TG-rich lipoproteins as evidenced by the massive hypertriglyceridemia in patients with genetic deficiency of the enzyme [].Fine-tuned regulation of LPL activity is an important aspect of energy homeostasis [].

Plasma Lipoproteins.

Description Polysaccharide interactions with plasma lipoproteins and lipoprotein lipase. FB2

Part A. Preparation, Structure and Molecular Biology, Academic Press, New York, () 70– Google Scholar Cryer, A. Tissue lipoprotein lipase activity and its action in lipoprotein metabolism.

beta-lipoproteins to beta-lipoprotein, leading to relatively low plasma pre-beta-lipoprotein and high plasma beta-lipoprotein levels. Indeed, reciprocal changes in the concentration of serum beta- and pre-beta-lipoproteins have been shown to occur in the plasma of patients undergoing weight reduction or treatment with Atromid-S (36).

Both.[Source 2)]. The origin of circulating lipoproteins is less understood than is their uptake, transport, and degradation 3).The lipoprotein lipid transport system in plasma has been described as involving two pathways: an exogenous route for the transport of cholesterol and triglycerides absorbed from dietary fat in the intestine, and an endogenous system through which cholesterol and.Robert A.

Hegele, in Emery and Rimoin's Principles and Practice of Medical Genetics, Plasma Lipoproteins and Cardiovascular Disease Risk. Plasma lipid and lipoprotein concentrations generally follow a right-skewed normal distribution in the general population (Figure ) (3).Median levels vary by age and sex: in general, older age and male sex are associated with a less.