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Lipoprotein lipase in the kidney: activity varies widely among animal species.
Umeå University, Faculty of Medicine, Medical Biosciences, Physiological chemistry.
Umeå University, Faculty of Medicine, Surgical and Perioperative Sciences, Clinical Physiology.
Umeå University, Faculty of Medicine, Medical Biosciences, Physiological chemistry.
Umeå University, Faculty of Medicine, Medical Biosciences, Physiological chemistry.
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2004 (English)In: American Journal of Physiology - Renal Physiology, ISSN 0363-6127, Vol. 287, no 6, F1131-1139 p.Article in journal (Refereed) Published
Abstract [en]

Much evidence points to a relationship among kidney disease, lipoprotein metabolism, and the enzyme lipoprotein lipase (LPL), but there is little information on LPL in the kidney. The range of LPL activity in the kidney in five species differed by >500-fold. The highest activity was in mink, followed by mice, Chinese hamsters, and rats, whereas the activity was low in guinea pigs. In contrast, the ranges for LPL activities in heart and adipose tissue were less than six- and fourfold, respectively. The activity in the kidney (in mice) decreased by >50% on food deprivation for 6 h without corresponding changes in mRNA or mass. This decrease in LPL activity did not occur when transcription was blocked with actinomycin D. Immunostaining for kidney LPL in mice and mink indicated that the enzyme is produced in tubular epithelial cells. To explore the previously suggested possibility that the negatively charged glomerular filter picks up LPL from the blood, bovine LPL was injected into rats and mice. This resulted in decoration of the glomerular capillary network with LPL. This study shows that in some species LPL is produced in the kidney and is subject to nutritional regulation by a posttranscriptional mechanism. In addition, LPL can be picked up from blood in the glomerulus.

Place, publisher, year, edition, pages
2004. Vol. 287, no 6, F1131-1139 p.
Keyword [en]
Adipose Tissue/enzymology, Animal Nutrition Physiology, Animals, Cricetinae, Cricetulus, Female, Food Deprivation, Guinea Pigs, Kidney/*enzymology, Lipoprotein Lipase/genetics/*metabolism, Male, Mice, Mink, Myocardium/enzymology, RNA; Messenger/analysis, Rats, Rats; Sprague-Dawley, Species Specificity
URN: urn:nbn:se:umu:diva-15203DOI: 10.1152/ajprenal.00089.2004PubMedID: 15292043OAI: diva2:154875
Available from: 2008-01-11 Created: 2008-01-11 Last updated: 2009-10-13Bibliographically approved
In thesis
1. Aspects on lipoprotein lipase and atherosclerosis
Open this publication in new window or tab >>Aspects on lipoprotein lipase and atherosclerosis
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Lipoprotein lipase (LPL) hydrolyses blood lipids at the vascular endothelium. This action makes fatty acids available for tissue metabolic requirements. LPL is anchored to the endothelium by electrostatic forces and may act as a bridge connecting lipoproteins to cell surfaces. Clusters of positively charged amino acid residues in LPL interact with anionic groups on oligosaccharides covering the cell surfaces. Heparin competes with cell surface oligosaccharides for binding to LPL. Interaction of LPL with soluble and cell surface- ound oligosaccharides influences the activity and catabolism of the enzyme. LPL has a dual role in the development of atherosclerosis. Hydrolysis of lipoproteins by LPL contributes to clearance of lipids from plasma, resulting in an anti-atherogenic lipid profile. On the other hand, trough its bridging function, LPL contributes to lipoprotein retention at the endothelium and in the connective tissue of the artery wall. Furthermore LPL may stimulate uptake of lipoproteins in cells, converting them to foam cells. In this way LPL is considered to be proatherogenic.

We have investigated the effects caused by a synthetic heparin analogue, RG-13577, developed for treatment of tumors by anti-angiogenesis theraphy (Paper I) and by heparin (Paper II) on the turnover and biological role of LPL. The variation of LPL activity in kidney among animal species was studied in Paper III. Localization of LPL in healthy and atherosclerotic human arteries in relation to two other heparin-binding proteins (extracellular superoxide dismutase and apolipoprotein B) was studied in Paper IV.

54 p.
National Category
urn:nbn:se:umu:diva-564 (URN)91-7305-8998 (ISBN)
Public defence
2005-09-07, sal E04, NUS, 09:00 (English)
Available from: 2005-08-18 Created: 2005-08-18 Last updated: 2009-10-13Bibliographically approved

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Ruge, ToralphOlivecrona, Gunilla
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