Lipoprotein lipase activation

Partial summary of lipoprotein metabolism in humans. I to VII are sites of action of hypolipidemic drugs. I, stimulation of bile acid and/or cholesterol fecal excretion II, stimulation of lipoprotein lipase activity III, inhibition of VLDL production and secretion IV, inhibition of cholesterol biosynthesis V, stimulation of cholesterol secretion into bile fluid VI, stimulation of cholesterol conversion to bile acids VII, increased plasma clearance of LDL due either to increased LDL receptor activity or altered lipoprotein composition. CHOL, cholesterol IDL, intermediate-density lipoprotein. 

CN181 Plot, C., ]. Hocquette, P. Herpin, ]. H. Veerkamp, and D. Bauchart. Dietary coconut oil affects more lipoprotein lipase activity than the mitochondria oxidative capacities in muscles of preruminant calves. J Nutr Biochem 2000 11(4) 231-238. 

Progesterone has little effect on protein metabolism. It stimulates lipoprotein lipase activity and seems to favor fat deposition. The effects on carbohydrate metabolism are more marked. Progesterone increases basal insulin levels and the insulin response to glucose. There is... 

In the capillaries of these tissues, the extracellular enzyme lipoprotein lipase, activated by apoC-II, hydrolyzes triacylglycerols to fatty acids and glycerol (step... 

Extracellular lipoprotein lipase, activated by apo C-ll, degrades TG in VLDL... 

Decreased uptake of fatty acids In fasting, lipoprotein lipase activity of adipose tissue is low. Consequently, circulating triacyl-glycerol of lipoproteins is not available for triacylglycerol synthesis in adipose tissue. 

Two assays have been developed for measuring the relative concentration of lipoprotein lipase activator in milk. Anderson (1979) developed an immunoassay and Super et al (1976) used [23H]glycerol triolein and measured the liberated [23H]glycerol. 

Anderson, M. 1979. Enzyme immunoassay for measuring lipoprotein lipase activator in milk. J. Dairy Sci. 62, 1380-1383. 

Egelrud, T. and Olivecrona, T. 1973. Purified bovine milk (lipoprotein) lipase Activity against lipid substrates in the absence of exogenous serum factors. Biochem. Bio-phys. Acta 306, 115-127. 

Milk is clarified by high-speed centrifugation to remove extraneous matter held in suspension. Clarification occurs prior to heat treatment of the milk to prevent dissolution of the extraneous matter. Although clarification removes somatic cells, the elevated levels of lipoprotein lipase activators and plasmin that may be associated with increased numbers of white blood cells in the milk are not eliminated. Therefore, increased lipolysis of milk fat by lipoprotein lipase and proteolysis of casein by plasmin may not be deterred. 

Topiramate, felbamate, and zonisamide are associated with weight loss. In animals topiramate reduced food intake, but also reduced energy disposition in the absence of reduced intake. In addition, topiramate increased lipoprotein lipase activity in adipose tissue, possibly reflecting enhanced regulatory thermogenesis. In humans and animals topiramate reduces leptin concentrations. With felbamate weight loss is almost always associated with... 

In six patients with renal transplants treated with sirolimus, mean total plasma cholesterol, triglyceride, and apolipoprotein concentrations increased (1067). The authors suggested that sirolimus increases lipase activity in adipose tissue and reduces lipoprotein lipase activity, resulting in increased hepatic synthesis of triglycerides, increased secretion of VLDL, and increased hypertriglyceridemia. 

Brewster DW, Matsumura F. 1988. Reduction of adipose tissue lipoprotein lipase activity as a result of in vivo administration of 2,3,7,8-tetrachlorodibenzo-p-dioxin to the guinea pig. Biochem Pharmacol 37 2247-2253. 

Apolipoprotein C-II can also be isolated from VLDL or HDL (H20, L5, N3). It contains 78 residues (J3) and has been shown by Chou-Fasman analysis to bind phospholipids (M26, M40), with three predicted helical sequences (M26). ApoC-II has attracted a great deal of attention because it activates one of the most important enzymes in plasma lipid metabolism, lipoprotein lipase, responsible for the hydrolysis of triglyceride in chylomicrons and VLDL. Sparrow and Gotto have summarized a number of studies on structure-function relationships (S52). These, taken together, indicate that there are separate functional domains in apoC-II, in that lipoprotein lipase activation is mediated by residues 55-78 and phospholipid binding by... 

A disorder of lipid metabolism, in which absence of lipoprotein lipase activity due to an absolute apoC-II deficiency results in marked hypertriglyceridemia (Type I phenotype), has been reviewed elsewhere (N8). There are some unexplained differences in the clinical picture and plasma lipoprotein pattern between apoC-II deficiency and primary lipoprotein lipase deficiency. In apoC-II deficiency, symptoms appear to be milder (but recurrent abdominal pain, caused apparently by acute pancreatitis, is a frequently reported symptom). Patients do not show xanthomas or hepatomegaly, and few have splenomegaly (all features of lipoprotein lipase deficiency). Diagnosis is by electrophoresis of the C apolipoproteins, and a plasma triglyceride concentration usually 1000-3000 mg/dl (N8). There may be an increase in plasma VLDL concentration, whereas in classical lipoprotein lipase deficiency plasma VLDL concentration is nearly normal (N8). 

Another apolipoprotein, Pa-glycoprotein-1, or apoH, is a glycoprotein of Mr 54,000 found in all major lipoprotein density fractions, especially VLDL where it forms about 4% of the protein mass. Serum concentration is about 15-30 mg/100 ml. Two-thirds to three-quarters is found in the d > 1.21 g/ml fraction after ultracentrifugation (P19, P20). ApoH is taken up readily by a triglyceride-phospholipid emulsion (Intralipid) (P20) and it activates lipoprotein lipase (Nl). Lipoprotein lipase activation by either apoH or apoC-II is inhibited by apoC-III (Nl). 

Chylomicrons are triglyceride rich and contain apolipoprotein B-48 and the A types. The latter are synthesized in the intestinal tract cells. Additional apoproteins are transferred to the chylomicrons from HDL in circulation the apoE and apoC types. Their site of synthesis is the liver. The chylomicrons are subject to degradation by lipoprotein lipase in the peripheral tissue, especially adipose tissue. Lipoprotein lipase activity is increased by increased blood insulin levels. This enzyme is extracellular, attached to the capillary endothelial cells, and activated by ApoC-II, which is present in the chylomicrons. Lipoprotein lipase causes the hydrolysis of triglycerides, thus decreasing chylomicron size... 

Hamosh, M., Clary, T.R., Chernick, W.W., Scow, R.O. 1970. Lipoprotein lipase activity of adipose and mammary tissue and plasma triglyceride in pregnant and lactating rats. Biochim. Biophys. Acta 210, 473 182. 

A possible increase in the permeability of the MFGM during maturation due to storage-related hydrolysis of membrane components by lipoprotein lipase activity (Sugimoto et al., 1983 Deeth, 1997). 

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