Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.1.34 (lipoprotein lipase)
7,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The catabolism of human and rat 125I-labelled very low density lipoproteins (VLDL) was compared by perfusing the lipoproteins through beating rat hearts. Triacylglycerol was removed from the VLDL to a greater extent than the protein moiety, leaving remnants containing relatively more apo-B and less apo-C. The change in apo-C content of the remnants correlated with the loss of triacylglycerol. The extent of removal of triacylglycerol from the rat and human VLDL was similar and in most cases appeared to saturate the heart lipoprotein lipase. The remnants were slightly smaller in size than the VLDL, and included particles which appeared to be partially emptied. In addition to remnants of d less than 1.019 g/ml, iodinated lipoproteins derived from rat and human VLDL were recovered at d 1.019-1.063 and 1.063-1.21 g/ml. The former contained largely cholesterol and cholesteryl esters, while phospholipids were the dominant lipid in the latter. An average of 40% of the 125I-labelled apoprotein lost from the VLDL was associated with the perfused hearts. Very little d 1.019-1.063 g/ml lipoprotein was produced from low (physiological) concentrations of rat VLDL, most of the lipoprotein being removed by the heart. However, lipoproteins of density 1.019-1.063 g/ml were formed from human VLDL at all concentrations in the perfusate, as well as from higher concentrations of the rat VLDL. Agarose gel filtration of lipoproteins following heart perfusion with human VLDL revealed large aggregates containing particles which resemble low density lipoproteins (LDL) in electron microscopic appearance and apoprotein composition, since they contain largely apo-B. These data suggest that at normal concentrations rat VLDL are almost completely catabolised and taken up by the heart without the formation of LDL, while LDL is produced from human VLDL at all concentrations.
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PMID:The catabolism of human and rat very low density lipoproteins by perfused rat hearts. 20 23

A review of radioimmunoassays for measuring human apolipoprotein B (apo B), the A apolipoproteins of high density lipoprotein (apo A-I and apo A-II) and apolipoprotein C-II (apo C-II) in human plasma and in isolated lipoproteins is presented. The sensitivity, specificity and validity of each of these assays is discussed. In normolipidemic subjects the reported serum apo B concentrations ranged between 0.83 +/- 0.16 and 0.92 +/- 0.21 g per l (m +/- SD). Serum apo B concentrations were highest in Type II subjects (Type IIa homozygotes 3.83 +/- 0.43 g per l; Type IIa heterozygotes 2.37 +/- 0.47 g per l) and were less elevated in patients with Type IV and Type V disorders (1.32 +/- 0.21 g per l and 1.26 +/- 0.30 g per l, respectively). Preliminary data on the relationship between plasma apo B and cholesterol, the distribution of apo B amongst the lipoprotein classes and a comparison of the lipoprotein lipid-apo B ratios in the various hyperlipidemic disorders are summarized. In contrast to apo A-II, the immunoreactivity of apo A-I was not fully exposed in whole sera and in isolated lipoproteins. The different methods used to measure the apo A-I immunoreactivity are discussed. In normolipidemic subjects the serum apo A-I concentration in males and females was 1.13 +/- 0.061 and 1.24 +/- 0.068 g per l (m +/- SD), respectively, while the corresponding serum apo A-II values were 0.35 +/- 0.038 g per l and 0.41 +/- 0.046 g per l. In subjects with Tangier's disease, the serum apo A-I and apo A-II concentrations were less than 1 percent and 5 to 7 percent of that found in controls. The serum apo A-I level was also reduced in two subjects with abetalipoproteinemia (0.38 g per l and 0.30 g per l) and Tye II hyperlipoproteinemia (range 0.54 to 0.86 g per l). In normotriglyceridemic subjects and those with Type IIa hyperlipoproteinemia, the total plasma apo C-II concentrations were 0.0497 +/- 0.0040 g per l and 0.0562 +/- 0.0054 g per l (m +/- SE). Plasma apo C-II levels in Type IIb, Type IV and Type V lipoproteinemic subjects were 0.0899 +/- 0.0046, 0.0854 +/- 0.0069 and 0.1328 +/- 0.0021 g per l, respectively and were significantly higher than in the normotriglyceridemic subjects. An analysis of the relationship between the apo C-II content and the lipoprotein lipase activator properties of VLDL isolated from normo- and hypertriglyceridemic plasma samples is presented.
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PMID:Recent progress in the development of radioimmunoassays for human serum lipoproteins. 20 63

To identify cells developing into adipocytes by accumulation of triglyceride, rat epididymal fat pad cells from small rats were exposed to (3)H-labeled chylomicron fatty acids in vivo and then liberated with collagenase. Tissue remnants were removed by filtration and mature fat cells by flotation. Aggregating cells were then removed by filtration through a 25- micro m nylon screen. Further purification of cells labeled in vivo was obtained by removing floating cells from those adhering to the bottom of a culture dish. The adhering cells multiplied to a confluent monolayer when cultured in Medium 199 containing serum, glucose, insulin, and a triglyceride emulsion. The cells then gradually enlarged due to granulation of the cytoplasm by a lipid-staining material. After about 2 weeks these granules had coalesced forming mature adipocytes of typical signet-ring appearance. Free adipocytes could then be recovered from the cultures by collagenase treatment. After about 2 weeks of culture these cells had the same size (about 30 micro m) as adipocytes recovered in the original collagenase preparation of the rat epididymal fat pad. They contained triglyceride lipase activity and incorporated glucose into triglycerides to the same extent as cells developed in vivo but had higher lipoprotein lipase activity. In vitro, heparin in a low concentration, prostaglandin E(1), isobutylmethylxanthine, and cholera toxin markedly promoted the development of these cells into adipocytes. This could be shown to occur almost completely indicating that this fraction of cells was homogeneous and consisted of cells with the capacity to form adipocytes. The duplication time was about 2 days and did not change with subculturing. Preadipocytes could be obtained by density gradient centrifugation, isolating triglyceride-containing cells either directly from the pad or after 3 days in culture. All of these cells developed into adipocytes as described above but did not multiply as readily. It was concluded that cells from the epididymal fat pad from small rats can be isolated in a homogenous fraction that develops in culture into cells of identical morphology and function as adipocytes formed in vivo. The differentiation of these cells into adipocytes may be manipulated in vitro.
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PMID:Isolation and characterization of cells from rat adipose tissue developing into adipocytes. 20 38

In two patients with primary Type V hyperlipoproteinemia with typical clinical features including recurrent bouts of abdominal pain a myocardial infarction was diagnosed. In both cases coronary angiography revealed a severe three vessel disease. The case reports demonstrate that the incidence of ischemic heart disease in patients with Type V hyperlipoproteinemia is higher than reported in the literature. In each case of severe abdominal pain, even in younger Type V patients, a myocardial infarction has to be excluded, In both patients a selective depression in the activity of lipoprotein lipase was found. The possible pathogenetic implication of this finding will be discussed.
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PMID:[Coronary heart disease in patients with primary type V hyperlipoproteinemia (author's transl)]. 20 63

Hypertriglyceridemia, a risk factor for premature atherosclerosis, may result from decreased use of plasma triglycerides by tissues. The removal of triglycerides is mediated by the enzyme lipoprotein lipase (LPL). Heparin releases LPL from tissues and post-heparin plasma lipolytic activity (PHLA) has been extensively used to elucidate the mechanism of hypertriglyceridemia in various diseases. There is evidence to show that postheparin plasma contains enzymes other than LPL. Hence data on total PHLA are difficult to interpret. Availability of assays for the LPL component of PHLA has clarified equivocal findings in certain hypertriglyceridemic states. However, the LPL component is also heterogeneous. The LPL "isoenzymes" from various extrahepatic tissues behave differently under various metabolic conditions. Therefore, to understand properly the LPL system it is necessary to study the specific tissue LPL. Furthermore, the serum activator for LPL is now characterized. Its importance is evidenced by the recent discovery of a hypertriglyceridemic patient deficient in this apoprotein.
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PMID:The lipoprotein lipase system: new understandings. 20 4

Hepatic lipase activity and lipoprotein lipase activity were studied in postheparin plasma from 14 patients with various liver disorders. Plasma lecithin: cholesterol acyltransferase (LCAT) activity and lipoprotein composition and structure were also estimated. Five patients had lower hepatic lipase activity than the lowest control value, and in three of these no hepatic lipase activity was detected. Lipoprotein lipase was low in 5 patients, but in only one of them was hepatic lipase activity also low. Hepatic lipase was not significantly correlated to the concentration of plasma triglycerides, either in controls or in patients, whereas lipoprotein lipase was negatively correlated with plasma triglycerides both in controls and patients. Lipoprotein lipase and LCAT activity, but not hepatic lipase, was negatively correlated to the triglyceride content of the low density lipoproteins (density 1.019-1.063 g/ml) from the patients. No specific lipid or lipoprotein pattern was found in plasma from the patients with a low or without any hepatic lipase activity. The results suggest an important role of lipoprotein lipase and LCAT, for the increased content of triglycerides in the low density lipoproteins in patients with liver disease. The role of hepatic lipase remains unclear.
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PMID:Triglyceride lipase activity in postheparin plasma and plasma lipoproteins in liver disease. 20 7

The removal rate of apoprotein-B (apo B) in very low density lipoprotein (VLDL) was decreased in individuals with broad beta disease when compared with endogenous hypertriglyceridemia. Following the injection of 125I-VLDL isolated from individuals with endogenous hypertriglyceridemia, both VLDL apo B fractional catabolic rate (0.058 +/- 0.029 hr-1) and VLDL apo-B turnover rate (0.300 +/- 0.070 mg/kg/hr) were lower in broad beta disease than in endogenous hypertriglyceridemia (fractional catabolic rate 0.112 +/- 0.046, p less than .05; turnover rate 0.640 +/- 0.199, p less than .005) despite equivalent plasma concentrations of VLDL-apo-B. Furthermore, conversion of VLDL apo-B to LDL was impaired in broad beta disease relative to endogenous hypertriglyceridemia. Differences in the kinetics of lipoprotein lipase-related triglyceride removal during a maximal heparin infusion were also demonstrated between these two disorders. These differences suggest an abnormality in the interaction of lipoprotein lipase with the lipoproteins of unusual composition in broad beta disease. This is further supported by the normalization of lipoprotein composition in broad beta disease by estrogen therapy, with a simultaneous change in the kinetics of lipoprotein lipase-related triglyceride removal towards those seen in endogenous hypertriglyceridemia.
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PMID:Impaired very low density lipoprotein and triglyceride removal in broad beta disease: comparison with endogenous hypertriglyceridemia. 21 Mar 51

A system for classification of genetic and acquired forms of hyperlipidemia in humans based on lipoprotein physiology is described. Most hyperlipidemia can be accounted for by defects in one of four sites of physiologic regulation: (1) triglyceride-rich lipoprotein production, (2) lipoprotein lipase-mediated triglyceride catabolism, (3) remnant lipoprotein catabolism, and (4) extrahepatic cholesterol-rich lipoprotein catabolism.
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PMID:Pathophysiology of lipoprotein transport. 21 Mar 52

In vitro experiments showed that blood sera of the patients with atherosclerosis contained rather often the fraction of very low density lipoproteins (VLDL) with sf 100-400 S, which were cleaved by the lipoprotein lipase at the decreased rate as compared with that of normal people. The decrease in cleavage of the VLDL fraction was usually observed in patients with the increased concentration of the lipoprotein fraction in blood sera. These data suggest that separate constituents occurring in the VLDL fraction (sf 100-400 S) may be nonuniformly increased in hyperlipoproteinemia.
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PMID:[Lipoprotein lipase fractionation of very low density serum lipoproteins from healthy subjects and persons afflicted with atherosclerosis]. 21 May 86

The influence of purified human apolipoprotein C-II on phospholipase A1 and triglyceridase activities of lipoprotein lipase were compared. Lipoprotein lipase was obtained from rat hearts by perfusion with a medium containing heparin and purified on a heparin Sepharose 4-B column. Using phosphatidyl-ethanolamine-coated triglyceride particles as substrate it was found that the phospholipase A1 and triglyceridase activities of lipoprotein lipase similarly depend on the presence of apolipoprotein C-II. Apolipoprotein C-III cannot replace apolipoprotein C-II. However, addition of apolipoprotein C-III in the presence of C-II affects both lipase activities. While strong inhibition of triglyceridase activity was observed under these conditions, phospholipase A1 activity was slightly stimulated. On the basis of these findings a model was constructed for the role of apolipoprotein C-II in lipoprotein lipase action.
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PMID:Triglyceridase and phospholipase A1 activities of rat-heart lipoprotein lipase. Influence of apolipoproteins C-II and C-III. 21 Aug 32


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