MINIREVIEW
Mechanisms of obesity and related pathologies: Role of
apolipoprotein E in the development of obesity
Kyriakos E. Kypreos
1
, Iordanes Karagiannides
2
, Elisavet H. Fotiadou
1
, Eleni A. Karavia
1
,
Maria S. Brinkmeier
1
, Smaragda M. Giakoumi
1
and Eirini M. Tsompanidi
1
1 Department of Medicine, Pharmacology Unit, University of Patras Medical School, Rio, Greece
2 Department of Medicine, David Geffen School of Medicine, UCLA, Los Angeles, CA, USA
Introduction
Apolipoprotein E (ApoE) is a major protein of the
lipid and lipoprotein transport system mainly
involved in the metabolism of dietary lipids and the
removal of atherogenic lipoproteins, such as chylomi-
cron remnants and very low density lipoproteins
(VLDL), from the circulation [1,2]. In humans,
ApoE is a polymorphic 34.5 kDa glycoprotein
synthesized primarily by the liver, although it is also
synthesized by other tissues, such as brain and
adipose tissue. Human ApoE has three natural

August 2009, accepted 11 August 2009)
doi:10.1111/j.1742-4658.2009.07301.x
Apolipoprotein E is a polymorphic glycoprotein in humans with a molecu-
lar mass of 34.5 kDa. It is a component of chylomicron remnants, very
low density lipoprotein, low density lipoprotein and high density lipopro-
tein, and is primarily responsible for maintaining plasma lipid homeostasis.
In addition to these well-documented functions, recent studies in experi-
mental mouse models, as well as population studies, show that apolipo-
protein E also plays an important role in the development of obesity and
insulin resistance. It is widely accepted that disruption in homeostasis
between food intake and energy expenditure, and the subsequent deposition
of excess fatty acids into fat cells in the form of triglycerides, leads to the
development of obesity. Despite the pivotal role of obesity and dyslipide-
mia in the development of the metabolic syndrome and heart disease, the
functional interactions between adipose tissue and components of the lipo-
protein transport system have not yet been investigated thoroughly. In this
minireview, we focus on the current literature pertinent to the involvement
of apolipoprotein E in the development of pathologies associated with the
metabolic syndrome.
Abbreviations
ABCA1, ATP-binding cassette A1; ApoE, apolipoprotein E; ApoE
) ⁄ )
, ApoE-deficient; HDL, high density lipoprotein; LCAT, lecithin:cholesterol
acyl transferase; LDLr, low density lipoprotein receptor; LDLr
) ⁄ )
, LDLr-deficient; LpL, lipoprotein lipase; LRP1, LDLr related protein 1; VLDL,
very low density lipoprotein; VLDLr, very low density lipoprotein receptor.
5720 FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS
lipids are packaged into chylomicrons, which, subse-
quent to partial lipolysis by lipoprotein lipase (LpL),

Epidemiological and population studies have
established a direct correlation between obesity and
the development of cardiovascular disease [36,37].
Despite the pivotal role of obesity and dyslipidemia in
the development of the metabolic syndrome and heart
disease, the functional interactions between adipose tis-
sue and the lipid and lipoprotein transport system have
only recently started to be investigated.
ApoE in adipocyte differentiation and
lipid loading
In vitro experiments using cultures of primary prea-
dipocytes, adipocytes, adipose tissue explants or
Peripheral tissues
or liver
ABCA1
N
C
Plasma
apoE
Minimally
lipidated
apoE
Discoidal
apoE-HDL
LCAT
Spherical
apoE-HDL
Chylomicrons
ApoE-containing
chylomicron

enzyme LCAT. Minimally lipidated ApoE in plasma interacts with ABCA1 (step 1) that is present in the liver or other peripheral tissues. This
interaction promotes the lipidation of ApoE (step 2), which is then converted into a discoidal HDL-like particle through a sequence of steps
that are not yet well understood (step 3). Then, ApoE containing discoidal HDL-like particles are converted into spherical HDL by the action
of the plasma enzyme LCAT (step 4).
K. E. Kypreos et al. ApoE and obesity
FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS 5721
3T3-L1 cells provide some information on the role of
ApoE in preadipocyte differentiation and on ApoE
expression from mature adipocytes.
A study by Chiba et al. [38] provided the first direct
evidence that lipid-bound ApoE promotes preadipo-
cyte differentiation in a dose-dependent manner. Using
bone marrow stromal cells from ApoE-deficient
(ApoE
) ⁄ )
) mice and 3T3-L1 cells, these investigators
showed that ApoE-deficient VLDL failed to induce
adipogenesis, whereas normal VLDL promoted differ-
entiation of these cells into fat cells. Incubation of
ApoE-deficient VLDL with recombinant human ApoE
partially restored its ability to stimulate adipogenesis,
whereas the selective removal of ApoE from VLDL by
trypsin abolished the adipogenic activity of human
VLDL. When tetrahydrolipstatin, a potent lipoprotein
lipase inhibitor, was used in these experiments, it did
not alter the ability of ApoE-containing VLDL to pro-
mote adipogenesis, suggesting that hydrolysis of
VLDL triglycerides does not play a major role in the
adipogenic effects of ApoE-containing VLDL. Simi-
larly, individual lipid components of the VLDL or free

cells increases linearly with time in differentiation,
whereas the inhibition of lipid accumulation in differ-
entiated cells by biotin deprivation decreased ApoE
expression.
Interestingly, another set of experiments conducted
by Huang et al. [41] suggested that ApoE expression in
adipocytes was affected by the feeding state of the
mice that the tissue was derived from. ApoE expres-
sion was induced by fasting, whereas diet-induced
obesity or hyperphagia was associated with the
reduced expression of ApoE in the adipose tissue.
Because other studies showed that ApoE-expression in
the adipose tissue promoted lipid accumulation and
adipocyte differentiation [39], one interpretation of the
results obtained by Huang et al. [41] is that intrinsic
defense mechanisms in adipose tissue limit adipogene-
sis by reducing the expression of ApoE in the fed state.
Certainly, additional studies are required to determine
the role of adipocyte-synthesized ApoE, and to distin-
guish between the functions of peripherally expressed
ApoE versus adipocyte expressed ApoE.
Studies in experimental mouse models
Despite the differences in anatomy, pathology, physiol-
ogy and metabolism between mice and humans, studies
in mice during the last few decades have provided
important leads with respect to the pathogenesis and
genetics of human metabolic diseases, including obes-
ity. A number of studies in experimental mouse models
have provided a definitive link between ApoE and
obesity.

ApoE and obesity K. E. Kypreos et al.
5722 FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS
was accompanied by impaired plasma triglyceride
clearance and lipid uptake by adipose tissue. Direct
calorimetry studies did not reveal any significant differ-
ences in energy expenditure and respiratory quotient
between ApoE
) ⁄ )
and wild-type C57BL ⁄ 6 mice fed a
high-fat, high-sucrose diet for 24 weeks, suggesting
that, in the absence of ApoE, decreased plasma lipid
delivery to insulin sensitive tissues improves insulin
sensitivity and prevents the development of diet
induced obesity.
Using an approach similar to Chiba et al. [38], Gao
et al. [43] established that ApoE deficiency in Ay
⁄ +
mice prevented the development of obesity, with
decreased fat accumulation in the liver and adipose tis-
sues. Ay (also known as lethal yellow) is a mutation at
the mouse agouti locus in chromosome 2 that results
in a number of dominant pleiotropic effects, including
a yellow coat color, obesity, an insulin-resistant type II
diabetic condition, and an increased propensity to
develop a variety of spontaneous and induced tumors
[44]. The Ay mutation is the result of a 170 bp deletion
that removes all but the promoter and noncoding first
exon of the Raly gene, which lies in the same transcrip-
tional orientation as agouti and maps 280 kb proximal
to the 3¢ end of the agouti gene [44]. Gao et al. [43]

) ⁄ )
· Ay
⁄ +
mice, ApoE
protein expression in the plasma of these mice wors-
ened the glucose tolerance and insulin sensitivity of the
ApoE
) ⁄ )
· Ay
⁄ +
mice, and triggered obesity, indicat-
ing that circulating ApoE is involved in increased
adiposity and obesity-related metabolic disorders. Of
note, the uptake of ApoE-lacking VLDL into the liver
and adipocytes was markedly inhibited, although
adipocytes in ApoE
) ⁄ )
· Ay
⁄ +
mice exhibited normal
differentiation.
In a recent study from our laboratory [45], we
established that ApoE3
knock-in
mice fed the standard
Western-type diet for 24 weeks were more sensitive
to diet-induced obesity and related metabolic dys-
functions than wild-type C57BL ⁄ 6 mice, whereas
ApoE
) ⁄ )

, C57BL ⁄ 6 and ApoE
) ⁄ )
mice was
similar among groups, suggesting that different
responses to a Western type diet could not be attrib-
uted to differences in appetite. It is quite interesting
that, in all our experiments, plasma cholesterol levels
correlated inversely with body weight gain and body
fat accumulation. In the ApoE
) ⁄ )
mice, failure to
clear chylomicron remnants because of a deficiency
in ApoE resulted in a steady increase in plasma cho-
lesterol levels and rendered these mice resistant to
diet-induced obesity. By contrast, in the ApoE3
knock-
in
mice, the efficient catabolism of chylomicron rem-
nants resulted in only slightly elevated plasma choles-
terol levels, but promoted obesity, insulin resistance
and glucose intolerance. Similar to the ApoE3
knock-in
mice, C57BL ⁄ 6 mice, which express the mouse ApoE,
developed only mild hypercholesterolemia, but
became obese and insulin resistant after consuming a
Western-type diet for 24 weeks. Direct measurements
of dietary lipid delivery to hepatic and adipose tissue
raised the possibility that chylomicron and VLDL
remnants containing the human ApoE3 isoform are
taken up more avidly by adipose tissue than the lipo-

induced obesity and related metabolic dysfunctions.
Thus, in the absence of LDLr, other ApoE-recognizing
‘scavenger’ receptors, such as LDLr-related protein
(LRP1) and very low density lipoprotein receptor
(VLDLr) may promote, to some extent, delivery of
ApoE-containing chylomicron remnants to adipose tis-
sue. However, in the case of the ApoE
) ⁄ )
mice that
lack the endogenous ApoE, all these ApoE-mediated
receptor processes may be blocked, and ApoE
) ⁄ )
mice
become more resistant to body fat gaining compared
to LDLr
) ⁄ )
mice. Indeed, Hofmann et al. [50] showed
that adipocyte-specific inactivation of the multifunc-
tional receptor LRP1 in mice resulted in delayed post-
prandial lipid clearance, reduced body weight, smaller
fat stores, lipid-depleted brown adipocytes, improved
glucose tolerance and elevated energy expenditure as a
result of enhanced muscle thermogenesis. Furthermore,
inactivation of adipocyte LRP1 resulted in resistance
to dietary fat-induced obesity and glucose intolerance.
In another study by Gourdiaan et al. [51] VLDLr-defi-
cient mice were found to be resistant to diet-induced
obesity when fed a high-fat, high-calorie diet. Thus, it
is possible that, in the absence of LDLr, remnant-
bound ApoE interacts with VLDLr or LRP1 present

knock-in
mice at the end of
the 8-week period. However, although ApoE4
knock-in
mice gained 30% less weight during the period on high-
fat diet compared to ApoE3 mice, they showed
impaired insulin-stimulated glucose uptake. Further-
more, epididymal adipocytes derived from ApoE4
knock-
in
mice were larger in size than those derived from
ApoE3
knock-in
mice. When ApoE3 and ApoE4 were
expressed by adenovirus-mediated gene transfer in cul-
tures of ApoE-deficient adipocytes, only ApoE3 expres-
sion was able to significantly induce adiponectin
mRNA expression, and mobilize the glucose transporter
GLUT4, suggesting that ApoE3 but not ApoE4 expres-
sion interferes with insulin sensing pathways. On the
basis of these findings, it was concluded that, even
though ApoE3 expression leads to higher adipose tissue
mass in mice compared to ApoE4, qualitative differ-
ences in the epididymal adipose tissue between the
ApoE3
knock-in
and ApoE4
knock-in
mice contribute to
the accelerated impairment of glucose tolerance in the

reduces food intake in rats. Specifically, the intrecere-
broventricular injection of ApoE in rats decreased
their food intake, whereas intrecerebroventricular infu-
sion of ApoE anti-serum stimulated feeding. However,
in previous studies [38,43,45,55] that compared ApoE-
deficient with ApoE-expressing mice, there were no
significant changes in daily food intake between these
mouse groups. One possibility is that the peripheral
effects of ApoE predisposing to obesity in those
studies offset the brain-specific effects that reduced
food-intake in the study by Shen et al. [56].
ApoE and obesity K. E. Kypreos et al.
5724 FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS
ApoE expression and obesity in
epidemiological studies
To date, there is no established link between ApoE-
deficiency and obesity in humans. Specifically, there
are no epidemiological studies comparing the sensi-
tivity towards obesity of ApoE-expressing versus
ApoE-deficient human subjects because ApoE-defi-
ciency is an extremely rare condition in humans.
However, mutations in ApoE that affect its func-
tions, including the natural ApoE polymorphism
(ApoE4, ApoE3 and ApoE4), appear to modulate
the ability of the protein to predispose to obesity.
Few studies have attempted to link different human
ApoE-isoforms to obesity and related metabolic
dysfunctions, although they have produced somewhat
conflicting results. Data from the Atherosclerosis
Risk in Communities (ARIC) study, which included

· Ay
⁄ +
versus Ay
⁄ +
ApoE-deficiency renders genetically predisposed Ay
⁄ +
mice resistant to
obesity mainly by limiting uptake of VLDL by adipose tissue
Karagiannides et al. [45] ApoE3
knock-in
versus
C57Bl ⁄ 6 versus LDLr
) ⁄ )
versus ApoE
) ⁄ )
ApoE promotes diet-induced obesity and insulin resistance, at
least in part, through its interactions with the LDLr, after 24 weeks of
being fed a Western-type diet. Human ApoE3 is more potent than
mouse ApoE in promoting diet-induced obesity
Hofmann et al. [50] Adipose tissue-specific LRP1
) ⁄ )
versus wild-type mice
Adipose tissue-specific deletion of LRP1 renders mice resistant to
diet-induced obesity by limiting postprandial lipid clearance
Gourdiaan et al. [51] VLDLr
) ⁄ )
versus wild-type mice Deletion of VLDLr renders mice resistant to diet-induced obesity
possibly by limiting LpL-mediated lipolysis of postprandial triglycerides
Arbones-Mainar et al. [55] ApoE3
knock-in

3
Fat cells
4
ApoE
Lipid-rich
meal
Intestine
Fig. 2. Model for the role of ApoE in the development of diet-induced obesity in mice. Dietary lipids are packaged into chylomicrons in the
intestine and then secreted into the circulation (step 1) where they are partially lipolysed by plasma lipoprotein lipase and acquire ApoE (step
2). ApoE-containing chylomicron remnants then interact with receptors, such as LDLr, LRP1 and VLDLr, present on the surface of a number
of cells, including hepatocytes and adipocytes (step 3). This interaction promotes the delivery of dietary lipids to adipose tissue and leads to
diet-induced obesity and related metabolic dysfunctions (step 4). In the absence of the expression of ApoE or ApoE-recognizing receptors,
the delivery of dietary lipids to the adipose tissue is blocked (steps 3 and 4), resulting in resistance to diet-induced obesity.
K. E. Kypreos et al. ApoE and obesity
FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS 5725
In addition to its direct relation to body mass index
and obesity, the ApoE4 phenotype also appears to be
the link between obesity and abnormalities related to
glucose metabolism and diabetes. In obese men, the
expression of the ApoE4 isoform was correlated with
higher plasma insulin and glucose levels than in obese
men expressing the other ApoE phenotypes [60,61].
However, no such association between ApoE pheno-
type and insulin or glucose levels was observed in non-
obese men [60], whereas the association between
ApoE4 phenotype and insulin and glucose levels
became stronger with increasing body mass index
[60,61]. These findings again raise the interesting possi-
bility that, although hyperplastic types of obesity may
be more extreme in individuals expressing other ApoE-

TB, Zanni EE & Kardassis D (2004) Probing the
pathways of chylomicron and HDL metabolism using
adenovirus-mediated gene transfer. Curr Opin Lipidol
15, 151–166.
2 Zannis VI, Kypreos KE, Chroni A, Kardassis D &
Zanni EE (2004) Lipoproteins and atherogenesis. In
Molecular Mechanisms of Atherosclerosis (Loscalzo J,
ed.), pp. 111–174. Taylor & Francis, New York, NY.
3 Zannis VI & Breslow JL (1981) Human very low density
lipoprotein apolipoprotein E isoprotein polymorphism is
explained by genetic variation and posttranslational
modification. Biochemistry 20, 1033–1041.
4 Davignon J, Gregg RE & Sing CF (1988) Apolipopro-
tein E polymorphism and atherosclerosis. Arteriosclero-
sis 8, 1–21.
5 Boerwinkle E & Utermann G (1988) Simultaneous
effects of the apolipoprotein E polymorphism on
apolipoprotein E, apolipoprotein B, and cholesterol
metabolism. Am J Hum Genet 42, 104–112.
6 Kypreos KE, Teusink B, Van Dijk KW, Havekes LM
& Zannis VI (2001) Analysis of the structure and func-
tion relationship of the human apolipoprotein E
in vivo, using adenovirus-mediated gene transfer.
FASEB J 15, 1598–1600.
7 Yamamoto T, Choi HW & Ryan RO (2008) Apolipo-
protein E isoform-specific binding to the low-density
lipoprotein receptor. Anal Biochem 372, 222–226.
8 Kypreos KE & Zannis VI (2006) LDL receptor defi-
ciency or apoE mutations prevent remnant clearance
and induce hypertriglyceridemia in mice. J Lipid Res 47,

(2000) Low levels of extrahepatic nonmacrophage ApoE
inhibit atherosclerosis without correcting hypercholes-
terolemia in ApoE-deficient mice. Arterioscler Thromb
Vasc Biol 20, 1939–1945.
16 Shimano H, Ohsuga J, Shimada M, Namba Y, Gotoda
T, Harada K, Katsuki M, Yazaki Y & Yamada N
(1995) Inhibition of diet-induced atheroma formation in
transgenic mice expressing apolipoprotein E in the arte-
rial wall. J Clin Invest 95, 469–476.
17 Tsukamoto K, Tangirala R, Chun SH, Pure E & Rader
DJ (1999) Rapid regression of atherosclerosis induced
by liver-directed gene transfer of ApoE in ApoE-defi-
cient mice. Arterioscler Thromb Vasc Biol 19, 2162–
2170.
18 Tsukamoto K, Tangirala RK, Chun S, Usher D, Pure
E & Rader DJ (2000) Hepatic expression of apolipopro-
tein E inhibits progression of atherosclerosis without
reducing cholesterol levels in LDL receptor-deficient
mice. Mol Ther 1, 189–194.
19 Desurmont C, Caillaud JM, Emmanuel F, Benoit P,
Fruchart JC, Castro G, Branellec D, Heard JM &
Duverger N (2000) Complete atherosclerosis regression
after human ApoE gene transfer in ApoE-defi-
cient ⁄ nude mice. Arterioscler Thromb Vasc Biol 20,
435–442.
20 Raffai RL, Loeb SM & Weisgraber KH (2005) Apoli-
poprotein E promotes the regression of atherosclerosis
independently of lowering plasma cholesterol levels.
Arterioscler Thromb Vasc Biol 25, 436–441.
21 Spiegelman BM & Flier JS (2001) Obesity and the

Cell 93, 229–240.
31 Lehmann JM, Moore LB, Smith-Oliver TA, Wilkison
WO, Willson TM & Kliewer SA (1995) An antidiabetic
thiazolidinedione is a high affinity ligand for peroxi-
some proliferator-activated receptor gamma (PPAR
gamma). J Biol Chem 270, 12953–12956.
32 Hube F, Birgel M, Lee YM & Hauner H (1999) Expres-
sion pattern of tumour necrosis factor receptors in sub-
cutaneous and omental human adipose tissue: role of
obesity and non-insulin-dependent diabetes mellitus.
Eur J Clin Invest 29
, 672–678.
33 Arias J, Vara E, Gomez M, Garcia C, Moreno A &
Balibrea JL (1992) Effect of cytokines on ‘de novo’ lipid
synthesis and hormone secretion by isolated human
islets. Transplant Proc 24, 2909–2912.
34 Hotamisligil GS & Spiegelman BM (1994) Tumor
necrosis factor alpha: a key component of the obesity-
diabetes link. Diabetes 43, 1271–1278.
35 Hotamisligil GS, Murray DL, Choy LN & Spiegelman
BM (1994) Tumor necrosis factor alpha inhibits signal-
ing from the insulin receptor. Proc Natl Acad Sci USA
91, 4854–4858.
36 Grundy SM (2007) Metabolic syndrome: a multiplex
cardiovascular risk factor. J Clin Endocrinol Metab 92,
399–404.
37 Lazar MA (2005) How obesity causes diabetes: not a
tall tale. Science 307, 373–375.
38 Chiba T, Nakazawa T, Yui K, Kaneko E & Shimokado
K (2003) VLDL induces adipocyte differentiation in

of the mouse lethal yellow (Ay) mutation. Proc Natl
Acad Sci USA 91, 2562–2566.
45 Karagiannides I, Abdou R, Tzortzopoulou A, Voshol
PJ & Kypreos KE (2008) Apolipoprotein E predisposes
to obesity and related metabolic dysfunctions in mice.
FEBS J 275, 4796–4809.
46 Boden G (1997) Role of fatty acids in the pathogenesis
of insulin resistance and NIDDM. Diabetes 46, 3–10.
47 Roden M, Price TB, Perseghin G, Petersen KF, Roth-
man DL, Cline GW & Shulman GI (1996) Mechanism
of free fatty acid-induced insulin resistance in humans.
J Clin Invest 97, 2859–2865.
48 Lohmann C, Schafer N, von Lukowicz T, Sokrates Stein
MA, Boren J, Rutti S, Wahli W, Donath MY, Luscher
TF & Matter CM (2009) Atherosclerotic mice exhibit
systemic inflammation in periadventitial and visceral
adipose tissue, liver, and pancreatic islets. Atherosclerosis
doi:10.1016/j.atherosclerosis.2009.05.004.
49 Tangirala RK, Pratico D, FitzGerald GA, Chun S,
Tsukamoto K, Maugeais C, Usher DC, Pure E &
Rader DJ (2001) Reduction of isoprostanes and
regression of advanced atherosclerosis by
apolipoprotein E. J Biol Chem 276, 261–266.
50 Hofmann SM, Zhou L, Perez-Tilve D, Greer T, Grant
E, Wancata L, Thomas A, Pfluger PT, Basford JE,
Gilham D et al. (2007) Adipocyte LDL receptor-related
protein-1 expression modulates postprandial lipid trans-
port and glucose homeostasis in mice. J Clin Invest 117,
3271–3282.
51 Goudriaan JR, Tacken PJ, Dahlmans VE, Gijbels MJ,

57 Volcik KA, Barkley RA, Hutchinson RG, Mosley TH,
Heiss G, Sharrett AR, Ballantyne CM & Boerwinkle E
(2006) Apolipoprotein E polymorphisms predict low
density lipoprotein cholesterol levels and carotid artery
wall thickness but not incident coronary heart disease
in 12,491 ARIC study participants. Am J Epidemiol
164, 342–348.
58 Oh JY & Barrett-Connor E (2001) Apolipoprotein E
polymorphism and lipid levels differ by gender and
family history of diabetes: the Rancho Bernardo Study.
Clin Genet 60, 132–137.
59 Sima A, Iordan A & Stancu C (2007) Apolipoprotein E
polymorphism – a risk factor for metabolic syndrome.
Clin Chem Lab Med 45, 1149–1153.
60 Elosua R, Demissie S, Cupples LA, Meigs JB, Wilson
PW, Schaefer EJ, Corella D & Ordovas JM (2003) Obes-
ity modulates the association among APOE genotype,
insulin, and glucose in men. Obes Res 11, 1502–1508.
61 Marques-Vidal P, Bongard V, Ruidavets JB, Fauvel J,
Hanaire-Broutin H, Perret B & Ferrieres J (2003) Obesity
and alcohol modulate the effect of apolipoprotein E poly-
morphism on lipids and insulin. Obes Res 11, 1200–1206.
ApoE and obesity K. E. Kypreos et al.
5728 FEBS Journal 276 (2009) 5720–5728 ª 2009 The Authors Journal compilation ª 2009 FEBS