J. Lipid Res.
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Journal of Lipid Research, Vol 31, 507-513, Copyright © 1990 by Lipid Research, Inc.

ARTICLES

Apolipoprotein VLDL-II inhibits lipolysis of triglyceride-rich lipoproteins in the laying hen

WJ Schneider, R Carroll, DL Severson and J Nimpf
Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.

In the laying hen, very low density lipoprotein (VLDL) particles contain large amounts of apolipoprotein (apo)-VLDL-II in addition to apoB. These triglyceride-rich lipoproteins are transported from the liver primarily to growing oocytes. Since no appreciable hydrolysis of triglyceride occurs during this transport, we have investigated the possibility that apoVLDL-II functions as an inhibitor of lipoprotein lipase (LPL). The presence of LPL in chicken follicular granulosa cells was demonstrated by immunoblotting, and LPL activity with the usual in vitro characteristics could be measured in cultured granulosa cell extracts. ApoVLDL-II inhibited LPL activity in these extracts as well as in the post-heparin medium of rat cardiac myocytes. Half-maximal inhibition in both systems occurred at 40 micrograms/ml, a concentration that is one-tenth of the circulating apoVLDL-II in the laying hen. Much less inhibition was observed with reduced and alkylated apoVLDL-II and with apoA-I. We conclude that the presence of apoVLDL-II on laying hen VLDL ensures efficient delivery of triglyceride to the oocyte for subsequent use as energy source by the embryo.
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