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The Ins and Outs of Adipose Tissue

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Cellular Lipid Metabolism

Abstract

The aim of this chapter is to discuss what mechanisms are available to rapidly modulate fatty acid uptake/mobilization in adipose tissue. The major pathway for net uptake is lipoprotein lipase (LPL)-mediated hydrolysis of lipoprotein lipids. There are several mechanisms for control and they all serve to suppress LPL activity on a time-scale of hours in the setting of essentially unchanged LPL mRNA and mass. A protein complex that specifically binds to LPL mRNA can block synthesis of new enzyme. The Ca2+ milieu, and perhaps other conditions in the ER, can partition more of the enzyme towards intracellular degradation and less for export. After secretion from the adipocytes, active LPL can be converted into inactive monomers through interaction with angiopoietin-like proteins. At the vascular endothelium, product control may balance LPL action. If fatty acids accumulate at sites of lipolysis they eliminate the effect of apolipoprotein CII, which is a necessary activator for LPL. Intracellular lipolysis is initiated by adipose tissue triglyceride lipase (ATGL) which hydrolyzes triglycerides to diglycerides. These can either be re-esterified by a diacylglycerol acyl transferase (DGAT) enzyme or further hydrolyzed by hormone-sensitive lipase (HSL). The system is controlled by phosphorylation mediated by protein kinase A, and perhaps other protein kinases, as well as protein phosphatases. The prime target is perilipin, a lipid droplet protein which in its unphosphorylated form suppresses the activity of both ATGL and HSL. The two lipase systems are modulated by different mechanisms and on different time-scales. Both systems seem to operate at levels that generate an excess of fatty acids. The overriding control of how much gets deposited in the tissue as triglyceride and how much spills over into blood as albumin-bound fatty acids (NEFA) is exerted by the rate of glyceride synthesis. Recent studies show that glycerol-3-phosphate for this is generated mainly through glyceroneogenesis from citric acid cycle intermediates.

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Abbreviations

Angptl:

angiopoietin-like protein

Apo:

apolipoprotein

AKAP:

A kinase-binding protein

AQP:

aquaporin

ATGL:

Adipose triglyceride lipase

CETP:

cholesteryl ester transfer protein

CGI-58:

comparative gene identification 58

cld:

combined lipase deficiency

CoA:

coenzyme A

DGAT:

diacylglycerol acyl transferase

DG:

diglyceride

EM:

electron microscopy

ER:

endoplasmatic reticulum

FATP:

fatty acid transport protein

GPI:

glycerolphosphatidylinositol

GPIHBP:

glycerolphosphatidylinositol-linked high-density binding protein

HDL:

high-density lipoprotein

HSL:

hormone-sensitive lipase

HSPG:

heparan sulfate proteoglycan

LDL:

low-density lipoprotein

Lmf:

lipase maturation factor

LPL:

lipoprotein lipase

LPS:

lipopolysaccharide

LRP:

low-density lipoprotein receptor-related protein

MAGH:

monoacylglycerol hydrolase

MG:

monoglyceride

MGAT:

monoacylglycerol acyl transferase

NEFA:

non-esterified fatty acids (also called albumin-bound free fatty acids)

PTH:

parathyroid hormone

PKA:

protein kinase A

RAP:

receptor-associated protein

SR-B1:

scavenger receptor type B1

SREBP:

steroid regulatory element binding protein

TG:

triglyceride

UTR:

untranslated region

VLDL:

very low-density lipoprotein

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    Olivecrona, T., Olivecrona, G. (2009). The Ins and Outs of Adipose Tissue. In: Ehnholm, C. (eds) Cellular Lipid Metabolism. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-00300-4_13

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