Journal of Lipid Research, Vol 38, 77-85, Copyright © 1997 by Lipid Research, Inc.

ARTICLES

Dissociation of LPL and LDL: effects of lipoproteins and anti-apoB antibodies

SY Choi, L Pang, PA Kern, HJ Kayden, LK Curtiss, TM Vanni-Reyes and IJ Goldberg
Department of Medicine, Columbia University College of Physicians & Surgeons, New York, NY, USA.

We have shown previously that the activity of lipoprotein lipase (LPL), the major enzyme responsible for hydrolysis of triglyceride contained in circulating lipoproteins, is associated with lipoproteins in postheparin plasma. In other studies, microtiter plate assays showed that LPL interaction with low density lipoprotein (LDL) and very low density lipoprotein (VLDL) was decreased by antibodies to apolipoprotein (apo)B. To test whether antibodies to apoB affected LPL- LDL association in solution, two types of assays were performed, gel filtration and coprecipitation. First we showed that LPL activity and immunoreactive mass co-eluted during gel filtration of normal postheparin plasma, approximately with the peak of low density lipoproteins. Then LPL was used for gel filtration studies in the presence and absence of LDL and anti-apoB monoclonal antibodies. LPL association with LDL was diminished by antibodies to the amino-terminal region of apoB; antibodies to the carboxyl-terminal LDL receptor binding region of apoB were less effective. LDL binding to LPL containing heparin-agarose was also disrupted by the amino-terminal antibodies to apoB. To determine the LPL-lipoprotein association in situations in which the distribution of plasma lipoproteins was altered, we studied plasma from two types of subjects with dyslipidemias. The addition of 125I-labeled LPL to type 1 postheparin plasma produced two peaks of radioactivity, one peak eluted in the void volume of the column (with the chylomicrons) and a second peak eluted just prior to the normal elution of low density lipoproteins. In postheparin plasma from an abetalipoproteinemic subject, LPL eluted with HDL. We conclude that LPL associates primarily with apoB- containing lipoproteins. The reason for this appears to be that LPL interacts with the apoB.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				B. Loeffler, J. Heeren, M. Blaeser, H. Radner, D. Kayser, B. Aydin, and M. Merkel Lipoprotein lipase-facilitated uptake of LDL is mediated by the LDL receptor J. Lipid Res., February 1, 2007; 48(2): 288 - 298. [Abstract] [Full Text] [PDF]

				M. O. Pentikainen, R. Oksjoki, K. Oorni, and P. T. Kovanen Lipoprotein Lipase in the Arterial Wall: Linking LDL to the Arterial Extracellular Matrix and Much More Arterioscler. Thromb. Vasc. Biol., February 1, 2002; 22(2): 211 - 217. [Abstract] [Full Text] [PDF]

				S.-Q. Xiang, K. Cianflone, D. Kalant, and A. D. Sniderman Differential binding of triglyceride-rich lipoproteins to lipoprotein lipase J. Lipid Res., September 1, 1999; 40(9): 1655 - 1663. [Abstract] [Full Text]

				S. Y. Choi, I. J. Goldberg, L. K. Curtiss, and A. D. Cooper Interaction between ApoB and Hepatic Lipase Mediates the Uptake of ApoB-containing Lipoproteins J. Biol. Chem., August 7, 1998; 273(32): 20456 - 20462. [Abstract] [Full Text] [PDF]

				M. M. Hussain, J. C. Obunike, A. Shaheen, M. J. Hussain, G. S. Shelness, and I. J. Goldberg High Affinity Binding between Lipoprotein Lipase and Lipoproteins Involves Multiple Ionic and Hydrophobic Interactions, Does Not Require Enzyme Activity, and Is Modulated by Glycosaminoglycans J. Biol. Chem., September 15, 2000; 275(38): 29324 - 29330. [Abstract] [Full Text] [PDF]

				J. Boren, A. Lookene, E. Makoveichuk, S. Xiang, M. Gustafsson, H. Liu, P. Talmud, and G. Olivecrona Binding of Low Density Lipoproteins to Lipoprotein Lipase Is Dependent on Lipids but Not on Apolipoprotein B J. Biol. Chem., July 13, 2001; 276(29): 26916 - 26922. [Abstract] [Full Text] [PDF]