Lipoprotein lipase in mouse kidney

effects of nutritional status and high-fat diet

Rakel Nyrén, Elena Makoveichuk, Sandhya Malla, Sander Kersten, Stefan K. Nilsson, Madelene Ericsson, Gunilla Olivecrona*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Activity of lipoprotein lipase (LPL) is high in mouse kidney, but the reason is poorly understood. The aim was to characterize localization, regulation, and function of LPL in kidney of C57BL/6J mice. We found LPL mainly in proximal tubules, localized inside the tubular epithelial cells, under all conditions studied. In fed mice, some LPL colocalized with the endothelial markers CD31 and GPIHBP1 and could be removed by perfusion with heparin, indicating a vascular location. The role of angiopoietin-like protein 4 (ANGPTL4) for nutritional modulation of LPL activity was studied in wild-type and Angptl4-/- mice. In Angptl4-/- mice, kidney LPL activity remained high in fasted animals, indicating that ANGPTL4 is involved in suppression of LPL activity on fasting, like in adipose tissue. The amount of ANGPTL4 protein in kidney was low, and the protein appeared smaller in size, compared with ANGPTL4 in heart and adipose tissue. To study the influence of obesity, mice were challenged with high-fat diet for 22 wk, and LPL was studied after an overnight fast compared with fasted mice given food for 3 h. High-fat diet caused blunting of the normal adaptation of LPL activity to feeding/fasting in adipose tissue, but in kidneys this adaptation was lost only in male mice. LPL activity increases to high levels in mouse kidney after feeding, but as no difference in uptake of chylomicron triglycerides in kidneys is found between fasted and fed states, our data confirm that LPL appears to have a minor role for lipid uptake in this organ.

Original languageEnglish
Pages (from-to)F558-F571
JournalAmerican journal of physiology. Renal physiology
Volume316
Issue number3
DOIs
Publication statusPublished - 1 Mar 2019

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Lipoprotein Lipase
High Fat Diet
Nutritional Status
Kidney
Angiopoietins
Adipose Tissue
Proteins
Fasting
Chylomicrons
Inbred C57BL Mouse
Blood Vessels
Heparin
Triglycerides
Perfusion
Obesity
Epithelial Cells
Lipids
Food

Keywords

  • angiopoietin-like protein 4
  • high-fat diet
  • lipoprotein lipase
  • mouse
  • triglyceride uptake

Cite this

Nyrén, Rakel ; Makoveichuk, Elena ; Malla, Sandhya ; Kersten, Sander ; Nilsson, Stefan K. ; Ericsson, Madelene ; Olivecrona, Gunilla. / Lipoprotein lipase in mouse kidney : effects of nutritional status and high-fat diet. In: American journal of physiology. Renal physiology. 2019 ; Vol. 316, No. 3. pp. F558-F571.
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abstract = "Activity of lipoprotein lipase (LPL) is high in mouse kidney, but the reason is poorly understood. The aim was to characterize localization, regulation, and function of LPL in kidney of C57BL/6J mice. We found LPL mainly in proximal tubules, localized inside the tubular epithelial cells, under all conditions studied. In fed mice, some LPL colocalized with the endothelial markers CD31 and GPIHBP1 and could be removed by perfusion with heparin, indicating a vascular location. The role of angiopoietin-like protein 4 (ANGPTL4) for nutritional modulation of LPL activity was studied in wild-type and Angptl4-/- mice. In Angptl4-/- mice, kidney LPL activity remained high in fasted animals, indicating that ANGPTL4 is involved in suppression of LPL activity on fasting, like in adipose tissue. The amount of ANGPTL4 protein in kidney was low, and the protein appeared smaller in size, compared with ANGPTL4 in heart and adipose tissue. To study the influence of obesity, mice were challenged with high-fat diet for 22 wk, and LPL was studied after an overnight fast compared with fasted mice given food for 3 h. High-fat diet caused blunting of the normal adaptation of LPL activity to feeding/fasting in adipose tissue, but in kidneys this adaptation was lost only in male mice. LPL activity increases to high levels in mouse kidney after feeding, but as no difference in uptake of chylomicron triglycerides in kidneys is found between fasted and fed states, our data confirm that LPL appears to have a minor role for lipid uptake in this organ.",
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Lipoprotein lipase in mouse kidney : effects of nutritional status and high-fat diet. / Nyrén, Rakel; Makoveichuk, Elena; Malla, Sandhya; Kersten, Sander; Nilsson, Stefan K.; Ericsson, Madelene; Olivecrona, Gunilla.

In: American journal of physiology. Renal physiology, Vol. 316, No. 3, 01.03.2019, p. F558-F571.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Lipoprotein lipase in mouse kidney

T2 - effects of nutritional status and high-fat diet

AU - Nyrén, Rakel

AU - Makoveichuk, Elena

AU - Malla, Sandhya

AU - Kersten, Sander

AU - Nilsson, Stefan K.

AU - Ericsson, Madelene

AU - Olivecrona, Gunilla

PY - 2019/3/1

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N2 - Activity of lipoprotein lipase (LPL) is high in mouse kidney, but the reason is poorly understood. The aim was to characterize localization, regulation, and function of LPL in kidney of C57BL/6J mice. We found LPL mainly in proximal tubules, localized inside the tubular epithelial cells, under all conditions studied. In fed mice, some LPL colocalized with the endothelial markers CD31 and GPIHBP1 and could be removed by perfusion with heparin, indicating a vascular location. The role of angiopoietin-like protein 4 (ANGPTL4) for nutritional modulation of LPL activity was studied in wild-type and Angptl4-/- mice. In Angptl4-/- mice, kidney LPL activity remained high in fasted animals, indicating that ANGPTL4 is involved in suppression of LPL activity on fasting, like in adipose tissue. The amount of ANGPTL4 protein in kidney was low, and the protein appeared smaller in size, compared with ANGPTL4 in heart and adipose tissue. To study the influence of obesity, mice were challenged with high-fat diet for 22 wk, and LPL was studied after an overnight fast compared with fasted mice given food for 3 h. High-fat diet caused blunting of the normal adaptation of LPL activity to feeding/fasting in adipose tissue, but in kidneys this adaptation was lost only in male mice. LPL activity increases to high levels in mouse kidney after feeding, but as no difference in uptake of chylomicron triglycerides in kidneys is found between fasted and fed states, our data confirm that LPL appears to have a minor role for lipid uptake in this organ.

AB - Activity of lipoprotein lipase (LPL) is high in mouse kidney, but the reason is poorly understood. The aim was to characterize localization, regulation, and function of LPL in kidney of C57BL/6J mice. We found LPL mainly in proximal tubules, localized inside the tubular epithelial cells, under all conditions studied. In fed mice, some LPL colocalized with the endothelial markers CD31 and GPIHBP1 and could be removed by perfusion with heparin, indicating a vascular location. The role of angiopoietin-like protein 4 (ANGPTL4) for nutritional modulation of LPL activity was studied in wild-type and Angptl4-/- mice. In Angptl4-/- mice, kidney LPL activity remained high in fasted animals, indicating that ANGPTL4 is involved in suppression of LPL activity on fasting, like in adipose tissue. The amount of ANGPTL4 protein in kidney was low, and the protein appeared smaller in size, compared with ANGPTL4 in heart and adipose tissue. To study the influence of obesity, mice were challenged with high-fat diet for 22 wk, and LPL was studied after an overnight fast compared with fasted mice given food for 3 h. High-fat diet caused blunting of the normal adaptation of LPL activity to feeding/fasting in adipose tissue, but in kidneys this adaptation was lost only in male mice. LPL activity increases to high levels in mouse kidney after feeding, but as no difference in uptake of chylomicron triglycerides in kidneys is found between fasted and fed states, our data confirm that LPL appears to have a minor role for lipid uptake in this organ.

KW - angiopoietin-like protein 4

KW - high-fat diet

KW - lipoprotein lipase

KW - mouse

KW - triglyceride uptake

U2 - 10.1152/ajprenal.00474.2018

DO - 10.1152/ajprenal.00474.2018

M3 - Article

VL - 316

SP - F558-F571

JO - American Journal of Physiology : Renal Physiology

JF - American Journal of Physiology : Renal Physiology

SN - 1931-857X

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ER -