Skip to main content Accessibility help
×
Home

Lipoprotein lipase and the disposition of dietary fatty acids

  • Barbara A. Fielding (a1) and Keith N. Frayn (a1)

Abstract

Lipoprotein lipase (EC 3.1.1.34; LPL) is a key enzyme regulating the disposal of lipid fuels in the body. It is expressed in a number of peripheral tissues including adipose tissue, skeletal and cardiac muscle and mammary gland. Its role is to hydrolyse triacylglycerol (TG) circulating in the TG-rich lipoprotein particles in order to deliver fatty acids to the tissue. It appears to act preferentially on chylomicron-TG, and therefore may play a particularly important role in regulating the disposition of dietary fatty acids. LPL activity is regulated according to nutritional state in a tissue-specific manner according to the needs of the tissue for fatty acids. For instance, it is highly active in lactating mammary gland; in white adipose tissue it is activated in the fed state and suppressed during fasting, whereas the reverse is true in muscle. Such observations have led to the view of LPL as a metabolic gatekeeper, especially for dietary fatty acids. However, closer inspection of its action in white adipose tissue reveals that this picture is only partially true. Normal fat deposition in adipose tissue can occur in the complete absence of LPL, and conversely, if LPL activity is increased by pharmacological means, increased fat storage does not necessarily follow. LPL appears to act as one member of a series of metabolic steps which are regulated in a highly coordinated manner. In white adipose tissue, it is clear that there is a major locus of control of fatty acid disposition downstream from LPL. This involves regulation of the pathway of fatty acid uptake and esterification, and appears to be regulated by a number of factors including insulin, acylation-stimulating protein and possibly leptin.

    • Send article to Kindle

      To send this article to your Kindle, first ensure no-reply@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about sending to your Kindle. Find out more about sending to your Kindle.

      Note you can select to send to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be sent to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

      Find out more about the Kindle Personal Document Service.

      Lipoprotein lipase and the disposition of dietary fatty acids
      Available formats
      ×

      Send article to Dropbox

      To send this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Dropbox.

      Lipoprotein lipase and the disposition of dietary fatty acids
      Available formats
      ×

      Send article to Google Drive

      To send this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Google Drive.

      Lipoprotein lipase and the disposition of dietary fatty acids
      Available formats
      ×

Copyright

Corresponding author

*Dr Keith Frayn, fax +44 (0)1865 224652, email keith.frayn@oxlip.ox.ac.uk

References

Hide All
Baldo, A, Sniderman, AD, St-Luce, S, Avramoglu, RK, Maslowska, M, Hoang, B, Monge, JC, Bell, A, Mulay, S & Cianflone, K (1993) The adipsin–acylation stimulating protein system and regulation of intracellular triglyceride synthesis. Journal of Clinical Investigation 92, 15431547.
Beisiegel, U (1996) New aspects on the role of plasma lipases in lipoprotein catabolism and atherosclerosis. Atherosclerosis 124, 18.
Beisiegel, U & Heeren, J (1997) Lipoprotein lipase (EC 3.1.1.34) targeting of lipoproteins to receptors. Proceedings of the Nutrition Society 56, 731737.
Bensadoun, A (1991) Lipoprotein lipase. Annual Review of Nutrition 11, 217237.
Bergö, M, Olivecrona, G & Olivecrona, T (1996) Forms of lipoprotein lipase in rat tissues: in adipose tissue the proportion of inactive lipase increases on fasting. Biochemical Journal 313, 893898.
Borensztajn, J (1987) Heart and skeletal muscle lipoprotein lipase. In Lipoprotein Lipase, pp. 133148 [Borensztajn,, J editor]. Chicago, IL: Evener.
Braun, JEA & Severson, DL (1992) Regulation of the synthesis, processing and translocation of lipoprotein lipase. Biochemical Journal 287, 337347.
Brun, L-D, Gagne, C, Julien, P, Tremblay, A, Moorjani, S, Bouchard, C & Lupien, P-J (1989) Familial lipoprotein lipase-activity deficiency: study of total body fatness and subcutaneous fat tissue distribution. Metabolism 38, 10051009.
Campbell, PJ, Carlson, MG, Hill, JO & Nurjhan, N (1992) Regulation of free fatty acid metabolism by insulin in humans: role of lipolysis and reesterification. American Journal of Physiology 263, E1063E1069.
Carroll, R, Ben-Zeev, O, Doolittle, MK & Severson, DL (1992) Activation of lipoprotein lipase in cardiac myocytes by glycosylation requires trimming of glucose residues in the endoplasmic reticulum. Biochemical Journal 285, 693696.
Chen, G, Koyama, K, Yuan, X, Lee, Y, Zhou, Y-T, O'Doherty, R, Newgard, CB & Unger, RH (1996) Disappearance of body fat in normal rats induced by adenovirus-mediated leptin gene therapy. Proceedings of the National Academy of Sciences USA 93, 1479514799.
Coppack, SW, Evans, RD, Fisher, RM, Frayn, KN, Gibbons, GF, Humphreys, SM, Kirk, MJ, Potts, JL & Hockaday, TDR (1992) Adipose tissue metabolism in obesity: lipase action in vivo before and after a mixed meal. Metabolism 41, 264272.
Coppack, SW, Fisher, RM, Gibbons, GF, Humphreys, SM, McDonough, MJ, Potts, JL & Frayn, KN (1990) Postprandial substrate deposition in human forearm and adipose tissues in vivo. Clinical Science 79, 339348.
Cryer, A (1981) Tissue lipoprotein lipase activity and its action in lipoprotein metabolism. International Journal of Biochemistry 13, 525541.
Cryer, A, Riley, SE, Williams, ER & Robinson, DS (1976) Effect of nutritional status on rat adipose tissue, muscle and post-heparin plasma clearing factor lipase activities: their relationship to triglyceride fatty acid uptake by fat-cells and to plasma insulin concentrations. Clinical Science and Molecular Medicine 50, 213221.
Eckel, RH (1989) Lipoprotein lipase. A multifunctional enzyme relevant to common metabolic diseases. New England Journal of Medicine 320, 10601068.
Enerbäck, S & Gimble, JM (1993) Lipoprotein lipase gene expression: physiological regulators at the transcriptional and post-transcriptional level. Biochimica et Biophysica Acta 1169, 107125.
Frayn, KN (1997) Nutrient partitioning: is LPL the gatekeeper? International Journal of Obesity 21, S5.
Frayn, KN, Coppack, SW, Fielding, BA & Humphreys, SM (1995) Coordinated regulation of hormone-sensitive lipase and lipoprotein lipase in human adipose tissue in vivo: implications for the control of fat storage and fat mobilization. Advances in Enzyme Regulation 35, 163178.
Frayn, KN, Humphreys, SM & Coppack, SW (1996a) Net carbon flux across subcutaneous adipose tissue after a standard meal in normal-weight and insulin-resistant obese subjects. International Journal of Obesity 20, 795800.
Frayn, KN, Shadid, S, Hamlani, R, Humphreys, SM, Clark, ML, Fielding, BA, Boland, O & Coppack, SW (1994) Regulation of fatty acid movement in human adipose tissue in the postabsorptive-to-postprandial transition. American Journal of Physiology 266, E308E317.
Frayn, KN, Williams, CM & Arner, P (1996b) Are increased plasma non-esterified fatty acid concentrations a risk marker for coronary heart disease and other chronic diseases? Clinical Science 90, 243253.
Frühbeck, G, Aguado, M & Martínez, JA (1997) In vitro lipolytic effect of leptin on mouse adipocytes: evidence for a possible autocrine/paracrine role of leptin. Biochemical and Biophysical Research Communications 240, 590594.
Goldberg, IJ (1996) Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis. Journal of Lipid Research 37, 693707.
Goresky, CA, Stremmel, W, Rose, CP, Guirguis, S, Schwab, AJ, Diede, HE & Ibrahim, E (1994) The capillary transport system for free fatty acids in the heart. Circulation Research 74, 10151026.
Greenwood, MR (1985) The relationship of enzyme activity to feeding behavior in rats: lipoprotein lipase as the metabolic gatekeeper. International Journal of Obesity 9, Suppl. 1, 6770.
Grundy, SM & Mok, HYI (1976) Chylomicron clearance in normal and hyperlipidemic man. Metabolism 25, 12251239.
Hara, T, Cameron-Smith, D, Cooney, GJ, Kusunoki, M, Tsutsumi, K & Storlien, LH (1998) The actions of a novel lipoprotein lipase activator, NO-1886, in hypertriglyceridemic fructose-fed rats. Metabolism 47, 149153.
Havel, R (1994) McCollum Award Lecture, 1993: Triglyceride-rich lipoproteins and atherosclerosis – new perspectives. American Journal of Clinical Nutrition 59, 795799.
Jensen, DR, Schlaepfer, IR, Morin, CL, Pennington, DS, Marcel, T, Ammon, SM, Gutierrez-Hartman, A & Eckel, RH (1997) Prevention of diet-induced obesity in transgenic mice overexpressing skeletal muscle lipoprotein lipase. American Journal of Physiology 273, R683R689.
Julien, P, Despres, J-P & Angel, A (1989) Scanning electron microscopy of very small fat cells and mature fat cells in human obesity. Journal of Lipid Research 30, 293299.
Kaciuba-Uscilko, H, Dudley, GA & Terjung, RL (1980) Influence of thyroid status on skeletal muscle LPL activity and TG uptake. American Journal of Physiology 238, E518E523.
Kiens, B, Lithell, H, Mikines, KJ & Richter, EA (1989) Effects of insulin and exercise on muscle lipoprotein lipase activity in man and its relationship to insulin action. Journal of Clinical Investigation 84, 11241129.
Langin, D, Holm, C & Lafontan, M (1996) Adipocyte hormone-sensitive lipase: a major regulator of lipid metabolism. Proceedings of the Nutrition Society 55, 93109.
Leboeuf, B (1965) Regulation of fatty acid esterification in adipose tissue incubated in vitro. In Handbook of Physiology, section 5: Adipose Tissue, pp. 385391 [Renold, AE and Cahill, GF, editors]. Washington, DC: American Physiological Society.
Levak-Frank, S, Radner, H, Walsh, A, Stollberger, R, Knipping, G, Hoefler, G, Sattler, W, Weinstock, PH, Breslow, JL & Zechner, R (1995) Muscle-specific overexpression of lipoprotein lipase causes severe myopathy characterized by proliferation of mitochondria and peroxisomes in transgenic mice. Journal of Clinical Investigation 96, 976986.
Maslowska, M, Scantlebury, T, Germinario, R & Cianflone, K (1997) Acute in vitro production of acylation stimulating protein in differentiated human adipocytes. Journal of Lipid Research 38, 111.
Muoio, DM, Dohn, GL, Fiedorek, FT, Tapscott, EM & Coleman, RA (1997) Leptin directly alters lipid partitioning in skeletal muscle. Diabetes 46, 13601363.
Murthy, V, Julien, P & Gagné, C (1996) Molecular pathology of the human lipoprotein lipase gene. Pharmocology and Therapeutics 70, 101135.
Nikkilä, EA, Taskinen, M-R, Rehunen, S & Harkonen, M (1978) Lipoprotein lipase activity in adipose tissue and skeletal muscle of runners: relation to serum lipoproteins. Metabolism 27, 16611671.
Olivecrona, T, Liu, G, Hultin, M & Bengtsson-Olivecrona, G (1993) Regulation of lipoprotein lipase. Biochemical Society Transactions 21, 509513.
Peeva, E, Brun, DL, Ven Murthy, MR, Després, J-P, Normand, T, Gagné, C, Lupien, P-J & Julien, P (1992) Adipose cell size and distribution in familial lipoprotein lipase deficiency. International Journal of Obesity 16, 737744.
Pradines-Figueres, A, Vannier, C & Ailhaud, G (1990) Lipoprotein lipase stored in adipocytes and muscle cells is a cryptic enzyme. Journal of Lipid Research 31, 14671476.
Robinson, DS, Cryer, A & Davies, P (1975) The role of clearing-factor lipase (lipoprotein lipase) in the transport of plasma triglycerides. Proceedings of the Nutrition Society 34, 211215.
Saleh, J, Summers, L, Cianflone, K, Fielding, B, Sniderman, A & Frayn, K (1998) Coordinated release of acylation stimulating protein and triacylglycerol clearance by human adipose tisue in vivo in the postprandial period. Journal of Lipid Research 39, 884891.
Salmivirta, M, Lidholt, K & Lindahl, U (1996) Heparan sulfate: a piece of information. FASEB Journal 10, 12701279.
Samra, JS, Simpson, EJ, Clark, ML, Forster, CD, Humphreys, SM, Macdonald, IA & Frayn, KN (1996) Effect of epinephrine infusion on adipose tissue: interactions between blood flow and lipid metabolism. American Journal of Physiology 271, E834E839.
Santamarina-Fojo, S & Dugi, KA (1994) Structure, function and role of lipoprotein lipase in lipoprotein metabolism. Current Opinion in Lipidology 5, 117125.
Saxena, U, Witte, LD & Goldberg, IJ (1989) Release of endothelial cell lipoprotein lipase by plasma lipoproteins and free fatty acids. Journal of Biological Chemistry 264, 43494355.
Scow, RO & Chernick, SS (1987) Role of lipoprotein lipase during lactation. In Lipoprotein Lipase, pp. 149185 [Borensztajn,, J editor]. Chicago, IL: Evener.
Scow, RO & Olivecrona, T (1977) Effect of albumin on products formed from chylomicron triacylglycerol by lipoprotein lipase in vitro. Biochimica et Biophysica Acta 487, 472486.
Shimabukuro, M, Koyama, K, Chen, G, Wang, M-Y, Trieu, F, Lee, Y, Newgard, CG & Unger, RH (1997) Direct antidiabetic effect of leptin through triglyceride depletion of tissues. Proceedings of the National Academy of Sciences USA 94, 46374641.
Siegrist-Kaiser, CA, Pauli, V, Juge-Aubry, CE, Boss, O, Pernin, A, Chin, WW, Cusin, I, Rohner-Jeanrenaud, F, Burger, AG, Zapf, J & Meier, CA (1997) Direct effects of leptin on brown and white adipose tissue. Journal of Clinical Investigation 100, 28582864.
Sniderman, AD & Cianflone, K (1997) The adipsin–acylation-stimulating protein pathway and microenvironmental metabolic regulation. World Review of Nutrition and Dietetics 80, 4481.
Taskinen, M-R (1987) Lipoprotein lipase in hypertriglyceridemias. In Lipoprotein Lipase, pp. 201228 [Borensztajn,, J editor]. Chicago, IL: Evener.
van der, Vusse GJ & Reneman, RS (1996) Lipid metabolism in muscle. In Handbook of Physiology, section 12, pp. 952994 [Rowell, LB and Shepherd, JT, editors]. New York, NY: American Physiological Society.
Van Nieuwenhoven, FA, Verstijnen, CP, Abumrad, NA, Willemsen, PH, Van Eys, GJ, Van der, Vusse GJ & Glatz, JF (1995) Putative membrane fatty acid translocase and cytoplasmic fatty acid-binding protein are co-expressed in rat heart and skeletal muscles. Biochemical and Biophysical Research Communications 207, 747752.
Vilella, E, Joven, J, Fernández, M, Vilaró, S, Brunzell, JD, Olivecrona, T & Bengtsson-Olivecrona, G (1993) Lipoprotein lipase in human plasma is mainly inactive and associated with cholesterol-rich lipoproteins. Journal of Lipid Research 34, 15551564.
Weinstock, PH, Bisgaier, CL, Aalto-Setälä, K, Radner, H, Ramakrishnan, R, Levak-Frank, S, Essenburg, AD, Zechner, R & Breslow, JL (1995) Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Journal of Clinical Investigation 96, 25552568.
Yokoyama, T, Izumi, H, Endoh, M, Izawa, T, Ogawa, N & Okada, Y (1997) Effects of KRN4884, a novel pyridinecarboxamidine type KATP channel opener, on serum triglyceride levels in rats. British Journal of Pharmacology 120, 14711476.
Zechner, R (1997) The tissue-specific expression of lipoprotein lipase; implications for energy and lipoprotein metabolism. Current Opinion in Lipidology 8, 7788.

Keywords

Lipoprotein lipase and the disposition of dietary fatty acids

  • Barbara A. Fielding (a1) and Keith N. Frayn (a1)

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed.