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New wrinkles in lipoprotein lipase biology

Davies, Brandon S.J.; Beigneux, Anne P.; Fong, Loren G.; Young, Stephen G.

doi: 10.1097/MOL.0b013e32834d0b33
NUTRITION AND METABOLISM: Edited by Paul Nestel and Ronald P. Mensink

Purpose of review We summarize recent progress on GPIHBP1, a molecule that transports lipoprotein lipase (LPL) to the capillary lumen, and discuss several newly studied molecules that appear important for the regulation of LPL activity.

Recent findings LPL, the enzyme responsible for the lipolytic processing of triglyceride-rich lipoproteins, interacts with multiple proteins and is regulated at multiple levels. Several regulators of LPL activity have been known for years and have been investigated thoroughly, but several have been identified only recently, including an endothelial cell protein that transports LPL to the capillary lumen, a microRNA that reduces LPL transcript levels, a sorting protein that targets LPL for uptake and degradation, and a transcription factor that increases the expression of apolipoproteins that regulate LPL activity.

Summary Proper regulation of LPL is important for controlling the delivery of lipid nutrients to tissues. Recent studies have identified GPIHBP1 as the molecule that transports LPL to the capillary lumen, and have also identified other molecules that are potentially important for regulating LPL activity. These new discoveries open new doors for understanding basic mechanisms of lipolysis and hyperlipidemia.

aDepartment of Medicine

bDepartment of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, California, USA

Correspondence to Brandon S.J. Davies, UCLA, Division of Cardiology, Department of Medicine, A2-237 CHS Building, 10833 LeConte Ave., Los Angeles, CA 90095, USA. Tel: +1 310 825 9422; e-mail:

Copyright © 2012 Wolters Kluwer Health, Inc. All rights reserved.