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Localization of lipoprotein lipase and GPIHBP1 in mouse pancreas: effects of diet and leptin deficiency

Rakel Nyrén1, Chuchun L Chang2, Per Lindström3, Anastasia Barmina3, Evelina Vorrsjö1, Yusuf Ali4, Lisa Juntti-Berggren4, André Bensadoun5, Stephen G Young6, Thomas Olivecrona1 and Gunilla Olivecrona1*

Author affiliations

1 Department of Medical Biosciences/Physiological Chemistry, Umeå University, Umeå, Sweden

2 Institute of Human Nutrition, College of Physicians and Surgeons, Columbia University, New York, NY, USA

3 Department of Integrative Medical Biology (IMB), Umeå University, Umeå, Sweden

4 The Rolf Luft Research Center for Diabetes and Endocrinology, Karolinska Institutet, Stockholm, Sweden

5 Division of Nutritional Science, Cornell University, Ithaca, NY, USA

6 Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA

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Citation and License

BMC Physiology 2012, 12:14  doi:10.1186/1472-6793-12-14

Published: 27 November 2012



Lipoprotein lipase (LPL) hydrolyzes triglycerides in plasma lipoproteins and enables uptake of lipolysis products for energy production or storage in tissues. Our aim was to study the localization of LPL and its endothelial anchoring protein glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) in mouse pancreas, and effects of diet and leptin deficiency on their expression patterns. For this, immunofluorescence microscopy was used on pancreatic tissue from C57BL/6 mouse embryos (E18), adult mice on normal or high-fat diet, and adult ob/ob-mice treated or not with leptin. The distribution of LPL and GPIHBP1 was compared to insulin, glucagon and CD31. Heparin injections were used to discriminate between intracellular and extracellular LPL.


In the exocrine pancreas LPL was found in capillaries, and was mostly co-localized with GPIHBP1. LPL was releasable by heparin, indicating localization on cell surfaces. Within the islets, most of the LPL was associated with beta cells and could not be released by heparin, indicating that the enzyme remained mostly within cells. Staining for LPL was found also in the glucagon-producing alpha cells, both in embryos (E18) and in adult mice. Only small amounts of LPL were found together with GPIHBP1 within the capillaries of islets. Neither a high fat diet nor fasting/re-feeding markedly altered the distribution pattern of LPL or GPIHBP1 in mouse pancreas. Islets from ob/ob mice appeared completely deficient of LPL in the beta cells, while LPL-staining was normal in alpha cells and in the exocrine pancreas. Leptin treatment of ob/ob mice for 12 days reversed this pattern, so that most of the islets expressed LPL in beta cells.


We conclude that both LPL and GPIHBP1 are present in mouse pancreas, and that LPL expression in beta cells is dependent on leptin.

Lipoprotein lipase; Diabetes mellitus; Islet cells; Exocrine pancreas; Endothelium; Ob/ob mice; High fat diet; Heparin; qPCR; Immunofluorescence