Results 161 to 170 of about 80,622 (214)
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The Indian Journal of Pediatrics, 2020
To analyse the clinical and molecular spectrum of Lipoprotein Lipase (LPL) deficiency and to highlight the effect of a cost-effective indigenous diet for management of this disorder.This is a single-centre retrospective study. Fifteen patients from 14 kindreds with severe hypertriglyceridemia (more than 1000 mg/dl) were evaluated for a period of 12.5 y
Shwetha Kuthiroly +6 more
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To analyse the clinical and molecular spectrum of Lipoprotein Lipase (LPL) deficiency and to highlight the effect of a cost-effective indigenous diet for management of this disorder.This is a single-centre retrospective study. Fifteen patients from 14 kindreds with severe hypertriglyceridemia (more than 1000 mg/dl) were evaluated for a period of 12.5 y
Shwetha Kuthiroly +6 more
openaire +4 more sources
Lipoprotein lipase and atherosclerosis [PDF]
Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 2015 Lipoprotein lipase has long been known to hydrolyse triglycerides from triglycerides-rich lipoproteins. More recently, it has been shown to promote the binding of lipoproteins to various lipoprotein receptors. Evidence is also presented regarding the possible atherogenic role of lipoprotein lipase.
Hiroshi Mabuchi, Junji Kobayashi
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Lipoprotein Lipase and Atherosclerosis
Current Vascular Pharmacology, 2003Lipoprotein lipase (LPL) is a rate-limiting enzyme that hydrolyzes circulating triglyceride-rich lipoprotein such as very low density lipoproteins and chylomicrons. A decrease in LPL activity is associated with an increase in plasma triglycerides (TG) and decrease in high density lipoprotein (HDL) cholesterol.
Y. Stein, Olga Stein
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Lipoprotein lipase and hepatic lipase
Current Opinion in Lipidology, 1990Lipoprotein metabolism involves two major steps (Eisenberg 1990). First, triglyceride (TG) rich lipoproteins bind transiently to lipoprotein lipase (LPL) at the vascular endothelium (Fig. 1). The enzyme rapidly hydrolyzes triglycerides, which accomplishes two things (Eckel 1989): it enables the tissues to utilize fatty acids from the lipoproteins, and ...
Gunilla Olivecrona, Thomas Olivecrona
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Lipases and Lipoproteins [PDF]
, 1976 The degradation of triglyceride-rich plasma lipoproteins and the uptakeof their lipid constituents by tissues is dependent on enzymaticactivities which reside on or near the luminal surface of the capillary endothelium. Intravenous heparin injection releases a group of lipid hydrolyzing activities that are not normally present in plasma.
M L Baginsky +4 more
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The effects of tolbutamide on lipoproteins, lipoprotein lipase and hormone-sensitive lipase
Diabetes Research and Clinical Practice, 1999Type 2 diabetic patients are at increased risk to develop atherosclerotic vascular disease. These patients are often treated with sulphonylurea derivatives, and it has been suggested that this treatment might contribute to the increased atherosclerotic process.
Peter Nilsson-Ehle +2 more
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Regulation of lipoprotein lipase by Angptl4
Trends in Endocrinology & Metabolism, 2014Triglyceride (TG)-rich chylomicrons and very low density lipoproteins (VLDL) distribute fatty acids (FA) to various tissues by interacting with the enzyme lipoprotein lipase (LPL). The protein angiopoietin-like 4 (Angptl4) is under sensitive transcriptional control by FA and the FA-activated peroxisome proliferator activated receptors (PPARs), and its ...
Dijk, W., Kersten, A.H.
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β-lipoprotein, lipoprotein lipase and atromid
Journal of Atherosclerosis Research, 1963Summary The lipoprotein lipase activity eluted in connection with chromatographically separated β-lipoprotein was considerably lower in 6 cases of essential hyperlipaemia than the average for 7 healthy controls. Atromid administration seemed to increase the lipoprotein lipase activity per mg β-lipoprotein protein in 4 of 5 cases.
P. Bedding, B. Hood, B. Carlander
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The effect of lipoprotein lipase and hepatic lipase on the electrophoretic mobility of lipoprotein-X
Clinica Chimica Acta, 1978Lipoprotein-X containing plasma from a patient with familial lecithin:cholesterol acyltransferase (LCAT) deficiency, was used as substrate and incubated with postheparin plasma or partly purified lipases. LP-X could not be demonstrated by agar gel electrophoresis after incubation with postheparin plasma from a healthy subject, from a patient with ...
Randi Holme +3 more
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