The mechanism of assimilation of constituents of chylomicrons, very low density lipoproteins and remnants-a new theory

JM Felts, H Itakura, RT Crane - Biochemical and Biophysical Research …, 1975 - Elsevier
JM Felts, H Itakura, RT Crane
Biochemical and Biophysical Research Communications, 1975Elsevier
Purified remnant lipoproteins produced from chylomicrons in vivo or in vitro by the action of
lipoprotein lipase (LPL) contain firmly bound LPL. The perfused rat liver removes the
particulate bound LPL and triglyceride-labeled remnants at exactly the same rate, while
purified chylomicrons are not removed. Once remnants are removed by the liver, they are
not rereleased into the perfusate. These observations have led to the theory that the LPL
attached to the remnant is the signal that allows the liver to “recognize” remnants from …
Purified remnant lipoproteins produced from chylomicrons in vivo or in vitro by the action of lipoprotein lipase (LPL) contain firmly bound LPL. The perfused rat liver removes the particulate bound LPL and triglyceride-labeled remnants at exactly the same rate, while purified chylomicrons are not removed. Once remnants are removed by the liver, they are not rereleased into the perfusate. These observations have led to the theory that the LPL attached to the remnant is the signal that allows the liver to “recognize” remnants from chylomicrons. This is followed by fusion of the particle with the cell surface and may be associated with the splitting off a low density lipoprotein particle. The remaining lipids of the remnant are further metabolized by the liver triglyceridase and the cholesterol esterase.
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