PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2065043-5 1991 Although the composition of CNO/Chol VLDL differed from that of OO/Chol VLDL, the rates of triglyceride hydrolysis of CNO/Chol VLDL and OO/Chol VLDL by postheparin lipoprotein lipase in vitro were the same, suggesting that VLDLs from the two diet groups were equally good substrates for lipoprotein lipase. Triglycerides 91-103 lipoprotein lipase Oryctolagus cuniculus 164-182 15639492-3 2005 RESULTS: Increased expression of LPL significantly ameliorated hypertriglyceridemia and hypercholesterolemia in Tg WHHL rabbits [64% reduction in total cholesterol (TC) and 91% reduction in triglycerides (TG) vs. non-Tg]. Triglycerides 190-203 lipoprotein lipase Oryctolagus cuniculus 33-36 15639492-3 2005 RESULTS: Increased expression of LPL significantly ameliorated hypertriglyceridemia and hypercholesterolemia in Tg WHHL rabbits [64% reduction in total cholesterol (TC) and 91% reduction in triglycerides (TG) vs. non-Tg]. Triglycerides 205-207 lipoprotein lipase Oryctolagus cuniculus 33-36 15221136-8 2004 RESULTS: Increased LPL activity in transgenic rabbits resulted in a significant reduction of plasma triglycerides and non-esterified fatty acids, but not in basal levels of glucose and insulin. Triglycerides 100-113 lipoprotein lipase Oryctolagus cuniculus 19-22 12745668-1 2003 The synthetic compound NO-1886 is a lipoprotein lipase activator that lowers plasma triglycerides and elevates high-density lipoprotein cholesterol (HDL-C). Triglycerides 84-97 lipoprotein lipase Oryctolagus cuniculus 36-54 12236049-1 2002 The synthetic compound NO-1886 ([4-(4-bromo-2-cyano-phenylcarbamoyl)-benzyl]-phosphonic acid diethyl ester, CAS 133208-93-2) is a lipoprotein lipase activator which decreases plasma triglycerides and elevates high-density lipoprotein cholesterol (HDL-C) levels. Triglycerides 182-195 lipoprotein lipase Oryctolagus cuniculus 130-148 8206972-9 1994 Although triglyceride appears to be the preferred substrate for LPL, after greater than 25% of the triglyceride was hydrolyzed, significant amounts of retinyl ester were hydrolyzed by LPL. Triglycerides 9-21 lipoprotein lipase Oryctolagus cuniculus 64-67 11477088-4 2001 Increased LPL activity in transgenic rabbits was associated with as much as an 80% decrease in plasma triglycerides and a 59% decrease in high density lipoprotein-cholesterol. Triglycerides 102-115 lipoprotein lipase Oryctolagus cuniculus 10-13 11477088-8 2001 These results demonstrate that systemically increased LPL activity functions in the metabolism of all classes of lipoproteins, thereby playing a crucial role in plasma triglyceride hydrolysis and lipoprotein conversion, and that overexpression of LPL protects against diet-induced hypercholesterolemia and atherosclerosis. Triglycerides 168-180 lipoprotein lipase Oryctolagus cuniculus 54-57 11477088-8 2001 These results demonstrate that systemically increased LPL activity functions in the metabolism of all classes of lipoproteins, thereby playing a crucial role in plasma triglyceride hydrolysis and lipoprotein conversion, and that overexpression of LPL protects against diet-induced hypercholesterolemia and atherosclerosis. Triglycerides 168-180 lipoprotein lipase Oryctolagus cuniculus 247-250 9409232-5 1997 LPL activity was correlated with HDL cholesterol (r = .764, n = 18) and triglyceride (r = -.627, n = 18). Triglycerides 72-84 lipoprotein lipase Oryctolagus cuniculus 0-3 2065043-5 1991 Although the composition of CNO/Chol VLDL differed from that of OO/Chol VLDL, the rates of triglyceride hydrolysis of CNO/Chol VLDL and OO/Chol VLDL by postheparin lipoprotein lipase in vitro were the same, suggesting that VLDLs from the two diet groups were equally good substrates for lipoprotein lipase. Triglycerides 91-103 lipoprotein lipase Oryctolagus cuniculus 287-305 2065043-7 1991 The fractional clearance rate for triglyceride in OO/Chol rabbits was twice that of CNO/Chol rabbits, which parallels the previously observed differences in postheparin lipoprotein lipase activity. Triglycerides 34-46 lipoprotein lipase Oryctolagus cuniculus 169-187 6812640-6 1982 The amounts of these apolipoproteins in triacylglycerol-rich lipoprotein particles may determine the lipolytic activity of lipoprotein lipase and hepatic triacylglycerol lipase in triacylglycerol hydrolysis. Triglycerides 40-55 lipoprotein lipase Oryctolagus cuniculus 123-141 2930766-6 1989 Both hepatic lipase and lipoprotein lipase hydrolysed lipoprotein triacylglycerol and to a much lesser extent, also phospholipid. Triglycerides 66-81 lipoprotein lipase Oryctolagus cuniculus 24-42 2930766-9 1989 By contrast, lipoprotein lipase acted primarily on VLDL triacylglycerol. Triglycerides 56-71 lipoprotein lipase Oryctolagus cuniculus 13-31 4041478-10 1985 Lipoprotein lipase seemed to enhance the transfer of cholesteryl ester from HDL to VLDL when these lipoproteins were normal, but an important decline was obtained when triacylglycerol-rich VLDL were lipolyzed. Triglycerides 168-183 lipoprotein lipase Oryctolagus cuniculus 0-18 6740999-2 1984 The data obtained suggest that albumin is involved in regulation of lipoprotein lipolysis due to activation of LPL, caused by asseption of unesterified fatty acids, which are liberated after hydrolysis of triglycerides. Triglycerides 205-218 lipoprotein lipase Oryctolagus cuniculus 111-114 7030827-7 1981 Insulin injection to the hypertriglyceridemic rabbits induced a significant recovery of the decreased plasma LPL activity with a concomitant decrease of plasma triglyceride levels, while abeyance of insulin injection resulted in a decrease of LPL activity again. Triglycerides 30-42 lipoprotein lipase Oryctolagus cuniculus 109-112 184224-0 1976 Effect of an anti-lipoprotein lipase serum on plasma triglyceride removal. Triglycerides 53-65 lipoprotein lipase Oryctolagus cuniculus 18-36 599452-9 1977 It is concluded that (i) the rabbit placenta shows considerable lipase activity and the lipase has the same characteristics as clearing-factor (lipoprotein) lipase, (ii) triglyceride infused into the mother is taken up by the placenta and hydrolysed, and (iii) the fatty acids so released pass through the placenta and are taken up by the foetus. Triglycerides 170-182 lipoprotein lipase Oryctolagus cuniculus 127-163 184224-1 1976 Anti-lipoprotein lipase sera injected intravenously in roosters blocked quantitatively the catabolism of very low density lipoprotein (VLDL) triglyceride. Triglycerides 141-153 lipoprotein lipase Oryctolagus cuniculus 5-23 184224-3 1976 Following anti-LPL serum injection there was a linear increase in plasma triglyceride concentration. Triglycerides 73-85 lipoprotein lipase Oryctolagus cuniculus 15-18 184224-4 1976 The rate of entry of triglyceride in plasma was estimated from the rate of triglyceride accumulation in the plasma of animals injected with anti-LPL serum, or from the disappearance curve of biologically labelled VLDL. Triglycerides 21-33 lipoprotein lipase Oryctolagus cuniculus 145-148 184224-6 1976 Inhibition of VLDL triglyceride catabolism of anti-LPL serum provided a way to characterize newly secreted VLDL that exhibited a broad spectrum of particle sizes with a median of 625 A degrees. Triglycerides 19-31 lipoprotein lipase Oryctolagus cuniculus 51-54 184224-9 1976 The complete inhibition of triglyceride removal by an antiserum prepared against adipose tissue LPL demonstrates that the NaCl-inhibited, serum-activated lipase prepared by affinity chromatography on heparin-Sepharose and concanavalin A-Sepharose columns is the enzyme responsible in vivo for the catabolism of VLDL triglyceride. Triglycerides 27-39 lipoprotein lipase Oryctolagus cuniculus 96-99 184224-9 1976 The complete inhibition of triglyceride removal by an antiserum prepared against adipose tissue LPL demonstrates that the NaCl-inhibited, serum-activated lipase prepared by affinity chromatography on heparin-Sepharose and concanavalin A-Sepharose columns is the enzyme responsible in vivo for the catabolism of VLDL triglyceride. Triglycerides 316-328 lipoprotein lipase Oryctolagus cuniculus 96-99