Comprehensive Physiology Wiley Online Library

Lipoproteins and Lipoprotein Lipase

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 History
2 Lipoproteins
2.1 Chylomicrons
2.2 Very‐Low‐Density Lipoproteins
2.3 Low‐Density Lipoproteins
2.4 High‐Density Lipoproteins
3 Lipoprotein Lipase
3.1 History of Lipoprotein Lipase
3.2 Distribution of Lipoprotein Lipase
3.3 Regulation of Lipoprotein Lipase Activity
3.4 Ontogeny of Lipoprotein Lipase
3.5 Characteristics of Lipoprotein Lipase
3.6 Mechanisms of Hydrolysis of Circulating Triglycerides
3.7 Characteristics of Lipolytic Activity of Lipoprotein Lipase
4 Lipoprotein Lipase in Lung
4.1 Tissue Distribution and Regulation of Activity
4.2 Lung Lipoprotein Lipase in Disease
4.3 Origin
4.4 Functions
Figure 1. Figure 1.

Principal lipid components of plasma. Amphipathic lipids: unesterified cholesterol and phosphatidylcholine. Nonpolar lipids: triglyceride and cholesteryl ester. Free fatty acids are present in plasma as a complex with albumin.

Figure 2. Figure 2.

Metabolism of triglyceride‐rich lipoproteins. TG, triglyceride; CE, cholesteryl ester; LPL, lipoprotein lipase; FFA, free fatty acids; VLDL, very‐low‐density lipoprotein; IDL, intermediate‐density lipoprotein; LDL, low‐density lipoprotein; HDL, high‐density lipoprotein; A, B, C, and E, apoproteins.

Figure 3. Figure 3.

Low‐density lipoprotein (LDL) pathway. Sequential steps in catabolism of LDL. HMG CoA reductase, 3 hydroxy‐3‐methylglutaryl‐CoA reductase; ACAT, acyl‐CoA:cholesterol O‐acyltransferase.

From Brown et al. 59
Figure 4. Figure 4.

Scheme for hydrolysis of triglyceride (TG) in chylomicrons and very‐low‐density lipoproteins (VLDL) by endothelial lipoprotein lipase. Triglyceride‐rich lipoproteins are represented as large particles with a neutral lipid core and a surface film composed of lecithin (phosphatidylcholine), cholesterol, and apoproteins (apoA, apoB, etc.). VLDL, smaller than chylomicrons, contain different amounts of apoproteins. Lipoprotein lipase bound to endothelial surface through heparan sulfate hydrolyzes lipoprotein triglyceride to monoglyceride (MG) and free fatty acids (FFA); FFA are taken up by tissue or released into circulation where they bind to albumin (ALB). Shrinking particle core by lipolysis leaves excess surface constituents (broken line), which break off as disks similar to “nascent” high‐density lipoprotein (HDL). These newly formed particles acquire cholesteryl ester (CE) via lecithin‐cholesterol acyltransferase (LCAT) reaction, becoming spherical HDL particles.

Figure 5. Figure 5.

Attachment of circulating chylomicrons to capillary endothelium of various tissues. A: longitudinal section of capillary in lactating rat mammary gland taken 10 min after intravenous injection of chylomicrons (Ch). Many chylomicrons of various sizes are in capillary lumen (Lu). Cytoplasmic processes (P) extend from surface of endothelium (E) into capillary lumen. Chylomicrons in lumen are in contact with endothelial luminal surface (large arrows) and enmeshed by cytoplasmic processes (small arrows). S, secretory cell; N, nucleus; B, basement membrane; ECS, extracellular space; L, lipid droplet; ER, endoplasmic reticulum. × 10,000.

Micrograph courtesy of E. J. Blanchette‐Mackie B: longitudinal section of capillary in interscapular brown adipose tissue of 8‐day‐old rat 3 min after intravenous injection of chylomicrons. Many chylomicrons are in capillary lumen in contact with the luminal surface of the endothelial cell and enmeshed by cytoplasmic processes of endothelium. Endothelial cell has basal processes (BP) that extend into extracellular space to adipocytes (A). RBC, erythrocytes; M, mitochondria. × 10,000. (Micrograph courtesy of E. J. Blanchette‐Mackie.) C: cardiac muscle capillary. Section through profiles of two capillaries (C) containing chylomicrons from heart of a 24‐h‐fasted adult rat. Chylomicrons injected intravenously 2 min prior to fixation. Many cytoplasmic projections extend into capillary lumen making contact with chylomicron surfaces. Endothelial cell cytoplasm (E) contains numerous vesicles often open to either luminal or abluminal cell surface. L, myocyte lipid droplet; My, myocyte. × 17,000. (Micrograph courtesy of M. G. Wetzel.) D: endothelial cell from main‐stem pulmonary artery of dog. Endothelial projections on luminal surface may be involved in entrapment of chylomicrons and lipid droplets. × 34,000. [From Smith and Ryan 371.] E,F: detail of chylomicron‐capillary endothelium interaction. E: detail of capillary endothelium in interscapular brown adipose tissue of an 8‐day‐old rat taken 3 min after intravenous injection of chylomicrons. A chylomicron is in contact with endothelial cell surface at a point where cell is attenuated (arrow). Width of this small‐diameter capillary is ∼1 μm. × 90,000. (Micrograph courtesy of E. J. Blanchette‐Mackie.) F: detail of capillary in lactating rat mammary gland 10 min after intravenous injection of chylomicrons. Endothelium shows vesicles (v) and a long cytoplasmic process that projects into capillary lumen enmeshing a chylomicron. G, glycogen; Co, collagen. × 80,000. Micrograph courtesy of E. J. Blanchette‐Mackie
Figure 6. Figure 6.

Hydrolysis of glycerides by isolated perfused rat lung. Effect of loss of endothelial enzyme on rate of hydrolysis. Control, normal male Sprague‐Dawley rats. Heparin, animals received 100 units/kg heparin 1 h before perfusion with tri‐, di‐, or monoglyceride. FFA, free fatty acid.



Figure 1.

Principal lipid components of plasma. Amphipathic lipids: unesterified cholesterol and phosphatidylcholine. Nonpolar lipids: triglyceride and cholesteryl ester. Free fatty acids are present in plasma as a complex with albumin.



Figure 2.

Metabolism of triglyceride‐rich lipoproteins. TG, triglyceride; CE, cholesteryl ester; LPL, lipoprotein lipase; FFA, free fatty acids; VLDL, very‐low‐density lipoprotein; IDL, intermediate‐density lipoprotein; LDL, low‐density lipoprotein; HDL, high‐density lipoprotein; A, B, C, and E, apoproteins.



Figure 3.

Low‐density lipoprotein (LDL) pathway. Sequential steps in catabolism of LDL. HMG CoA reductase, 3 hydroxy‐3‐methylglutaryl‐CoA reductase; ACAT, acyl‐CoA:cholesterol O‐acyltransferase.

From Brown et al. 59


Figure 4.

Scheme for hydrolysis of triglyceride (TG) in chylomicrons and very‐low‐density lipoproteins (VLDL) by endothelial lipoprotein lipase. Triglyceride‐rich lipoproteins are represented as large particles with a neutral lipid core and a surface film composed of lecithin (phosphatidylcholine), cholesterol, and apoproteins (apoA, apoB, etc.). VLDL, smaller than chylomicrons, contain different amounts of apoproteins. Lipoprotein lipase bound to endothelial surface through heparan sulfate hydrolyzes lipoprotein triglyceride to monoglyceride (MG) and free fatty acids (FFA); FFA are taken up by tissue or released into circulation where they bind to albumin (ALB). Shrinking particle core by lipolysis leaves excess surface constituents (broken line), which break off as disks similar to “nascent” high‐density lipoprotein (HDL). These newly formed particles acquire cholesteryl ester (CE) via lecithin‐cholesterol acyltransferase (LCAT) reaction, becoming spherical HDL particles.



Figure 5.

Attachment of circulating chylomicrons to capillary endothelium of various tissues. A: longitudinal section of capillary in lactating rat mammary gland taken 10 min after intravenous injection of chylomicrons (Ch). Many chylomicrons of various sizes are in capillary lumen (Lu). Cytoplasmic processes (P) extend from surface of endothelium (E) into capillary lumen. Chylomicrons in lumen are in contact with endothelial luminal surface (large arrows) and enmeshed by cytoplasmic processes (small arrows). S, secretory cell; N, nucleus; B, basement membrane; ECS, extracellular space; L, lipid droplet; ER, endoplasmic reticulum. × 10,000.

Micrograph courtesy of E. J. Blanchette‐Mackie B: longitudinal section of capillary in interscapular brown adipose tissue of 8‐day‐old rat 3 min after intravenous injection of chylomicrons. Many chylomicrons are in capillary lumen in contact with the luminal surface of the endothelial cell and enmeshed by cytoplasmic processes of endothelium. Endothelial cell has basal processes (BP) that extend into extracellular space to adipocytes (A). RBC, erythrocytes; M, mitochondria. × 10,000. (Micrograph courtesy of E. J. Blanchette‐Mackie.) C: cardiac muscle capillary. Section through profiles of two capillaries (C) containing chylomicrons from heart of a 24‐h‐fasted adult rat. Chylomicrons injected intravenously 2 min prior to fixation. Many cytoplasmic projections extend into capillary lumen making contact with chylomicron surfaces. Endothelial cell cytoplasm (E) contains numerous vesicles often open to either luminal or abluminal cell surface. L, myocyte lipid droplet; My, myocyte. × 17,000. (Micrograph courtesy of M. G. Wetzel.) D: endothelial cell from main‐stem pulmonary artery of dog. Endothelial projections on luminal surface may be involved in entrapment of chylomicrons and lipid droplets. × 34,000. [From Smith and Ryan 371.] E,F: detail of chylomicron‐capillary endothelium interaction. E: detail of capillary endothelium in interscapular brown adipose tissue of an 8‐day‐old rat taken 3 min after intravenous injection of chylomicrons. A chylomicron is in contact with endothelial cell surface at a point where cell is attenuated (arrow). Width of this small‐diameter capillary is ∼1 μm. × 90,000. (Micrograph courtesy of E. J. Blanchette‐Mackie.) F: detail of capillary in lactating rat mammary gland 10 min after intravenous injection of chylomicrons. Endothelium shows vesicles (v) and a long cytoplasmic process that projects into capillary lumen enmeshing a chylomicron. G, glycogen; Co, collagen. × 80,000. Micrograph courtesy of E. J. Blanchette‐Mackie


Figure 6.

Hydrolysis of glycerides by isolated perfused rat lung. Effect of loss of endothelial enzyme on rate of hydrolysis. Control, normal male Sprague‐Dawley rats. Heparin, animals received 100 units/kg heparin 1 h before perfusion with tri‐, di‐, or monoglyceride. FFA, free fatty acid.

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Margit Hamosh, Paul Hamosh. Lipoproteins and Lipoprotein Lipase. Compr Physiol 2011, Supplement 10: Handbook of Physiology, The Respiratory System, Circulation and Nonrespiratory Functions: 387-418. First published in print 1985. doi: 10.1002/cphy.cp030112