Lipoprotein lipase (LPL) plays a central role in lipoprotein metabolism by catalyzing the hydrolysis of triglycerides (TG) in chylomicrons and VLDL particles (1). Hepatic lipase (HL) is synthesized by hepatocytes and linked to heparin sulfate proteoglycans on the surface of the sinusoidal capillaries of the liver, which hydrolyzes TG and phospholipids in the remains of chylomicron, the intermediate density lipoproteins (IDL) and HDL (1).
Patients with LPL deficiency exhibit marked hypertriglyceridemia with accumulation of chylomicrons (1–3). Patients with HL deficiency have hypercholesterolemia and hypertriglyceridemia and an accumulation of β-VLDL, chylomicron remains, IDL and LDL and HDL rich in TG (4–9).
The diagnosis of LPL and HL deficiency is based on the lack of their respective enzymatic activities in the postheparin plasma (PHP) of affected individuals (1). The conventionally available method for measuring LPL and HL activity has been the use of 3H or 14C labeled trioleoylglycerol as a substrate in the presence of 1 M NaCl or the anti-LPL monoclonal antibody, 5D2 (10, 11); the remaining activity is considered an HL activity under these conditions.
Research Article: Journal of Health & Medical Informatics
Research Article: Journal of Health & Medical Informatics
Research Article: Journal of Health & Medical Informatics
Research Article: Journal of Health & Medical Informatics
Review Article: Journal of Health & Medical Informatics
Review Article: Journal of Health & Medical Informatics
Research Article: Journal of Health & Medical Informatics
Research Article: Journal of Health & Medical Informatics
Editorial: Journal of Health & Medical Informatics
Editorial: Journal of Health & Medical Informatics
Editorial: Journal of Health & Medical Informatics
Editorial: Journal of Health & Medical Informatics
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