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J. Biol. Chem., Vol. 277, Issue 10, 8267-8272, March 8, 2002
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From the Perilipin (Peri) A is a phosphoprotein
located at the surface of intracellular lipid droplets in adipocytes.
Activation of cyclic AMP-dependent protein kinase (PKA)
results in the phosphorylation of Peri A and hormone-sensitive lipase
(HSL), the predominant lipase in adipocytes, with concurrent
stimulation of adipocyte lipolysis. To investigate the relative
contributions of Peri A and HSL in basal and PKA-mediated lipolysis, we
utilized NIH 3T3 fibroblasts lacking Peri A and HSL but stably
overexpressing acyl-CoA synthetase 1 (ACS1) and fatty acid transport
protein 1 (FATP1). When incubated with exogenous fatty acids,
ACS1/FATP1 cells accumulated 5 times more triacylglycerol (TG) as
compared with NIH 3T3 fibroblasts. Adenoviral-mediated expression of
Peri A in ACS1/FATP1 cells enhanced TG accumulation and inhibited
lipolysis, whereas expression of HSL fused to green fluorescent protein
(GFPHSL) reduced TG accumulation and enhanced lipolysis. Forskolin
treatment induced Peri A hyperphosphorylation and abrogated the
inhibitory effect of Peri A on lipolysis. Expression of a mutated Peri
A
Modulation of Hormone-sensitive Lipase and Protein Kinase
A-mediated Lipolysis by Perilipin A in an Adenoviral Reconstituted
System*
,,,,,
,,, and§§¶¶
Jean Meyer United States Department
of Agriculture Human Nutrition Research Center on Aging at Tufts
University, Boston, Massachusetts 02111, § Department of
Physiology, Tufts University School of Medicine, Boston, Massachusetts
02111, ¶ Departments of Medicine, Molecular Biology, and
Pharmacology, Washington University, St. Louis, Missouri 63110, Nessel Gene Therapy Center and Department of Medicine and
Molecular Biology, Massachusetts General Hospital, Boston,
Massachusetts 02114, ** Division of Endocrinology, Department
of Medicine, Stanford University, Stanford, California,
VA Palo Alto Health Care System, Palo Alto,
California 94305, and §§ Division of
Endocrinology, Metabolism, and Molecular Medicine, New England Medical
Center, Boston, Massachusetts 02111
3 (Ser to Ala substitutions at PKA consensus sites Ser-81, Ser-222,
and Ser-276) reduced Peri A hyperphosphorylation and blocked
constitutive and forskolin-stimulated lipolysis. Thus, perilipin
expression and phosphorylation state are critical regulators of
lipid storage and hydrolysis in ACS1/FATP1 cells.
*
Portions of this work were presented at the 60th
(2000) and 61st (2001) meetings of the American Diabetes
Association. This work was supported in part by the United States
Department of Agriculture, under agreement No. 581950-9-001 and DK
50647 (to A. S. G.) and DK 46942 (to F. B. K.), the Research
Service of the Department of Veterans Administration (to F. B. K.)
and research awards from the American Diabetes Association (to
A. S. G.). This work was supported in part by the Molecular Biology
Core of the Gastroenterology Research on Absorptive and Secretory
Processes, Grant P30 DK 34928.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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S. Miura, J.-W. Gan, J. Brzostowski, M. J. Parisi, C. J. Schultz, C. Londos, B. Oliver, and A. R. Kimmel Functional Conservation for Lipid Storage Droplet Association among Perilipin, ADRP, and TIP47 (PAT)-related Proteins in Mammals, Drosophila, and Dictyostelium J. Biol. Chem., August 23, 2002; 277(35): 32253 - 32257. [Abstract] [Full Text] [PDF]
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