Lipoprotein lipase in the kidney: activity varies widely among animal species.
2004 (English)In: American Journal of Physiology - Renal Physiology, ISSN 0363-6127, Vol. 287, no 6, F1131-1139 p.Article in journal (Refereed) Published
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.
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
IdentifiersURN: urn:nbn:se:umu:diva-15203DOI: 10.1152/ajprenal.00089.2004PubMedID: 15292043OAI: oai:DiVA.org:umu-15203DiVA: diva2:154875