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Am J Physiol Renal Physiol (August 3, 2004). doi:10.1152/ajprenal.00089.2004
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Submitted on March 18, 2004
Accepted on July 7, 2004

Lipoprotein lipase in kidney; activity varies widely between animal species

Toralph Ruge1, Lucyna Neuger2, Valentina Sukonina1, Gengshu Wu1, Stefan Barath1, Jitendra Gupta1, Barbara Frankel3, Bjorn Christophersen4, Knut Nordstoga5, Thomas Olivecrona1, and Gunilla Olivecrona1*

1 Department of Medical biosciences, Physiological Chemistry, Umea University, Umea, Sweden
2 Department of perioperative sciences, Clinical Physiology, Umea University, Umea, Sweden
3 Department of Integrative medical biology, Histology and Cell Biology, Umea University, Umea, Sweden
4 Institute of Clinical Biochemistry, University of Oslo, Oslo, Norway
5 Norwegian College of Veterinary medicine, Oslo, Norway

* To whom correspondence should be addressed. E-mail: gunilla.olivecrona{at}medbio.umu.se.

Much evidence points to a relation between 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 kidney in five species differed by more than 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 four-fold, respectively. The activity in kidney (in mice) decreased by more than 50 % on food deprivation for 6 hours, without corresponding changes in mRNA or mass. This decrease of 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 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 post-transcriptional mechanism. In addition LPL can be picked up from blood in the glomerulus.






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