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Human Molecular Genetics Advance Access originally published online on January 13, 2006
Human Molecular Genetics 2006 15(4):653-663; doi:10.1093/hmg/ddi480
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Nuclear lamin A inhibits adipocyte differentiation: implications for Dunnigan-type familial partial lipodystrophy

Revekka L. Boguslavsky1, Colin L. Stewart2 and Howard J. Worman1,*

1Departments of Medicine and Anatomy and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA and 2Cancer and Developmental Biology Laboratory, National Cancer Institute, Frederick, MD 21702, USA

* To whom correspondence should be addressed at: Department of Medicine, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, 10th Floor, Room 509, New York, NY 10032, USA. Email: hjw14{at}columbia.edu

Received December 1, 2005; Accepted January 6, 2006

Mutations in the LMNA gene encoding A-type lamins cause several diseases, including Emery–Dreifuss muscular dystrophy and Dunnigan-type familial partial lipodystrophy (FPLD). We analyzed differentiation of 3T3-L1 preadipocytes to adipocytes in cells overexpressing wild-type lamin A as well as lamin A with amino acid substitutions at position 482 that cause FPLD. We also examined adipogenic conversion of mouse embryonic fibroblasts lacking A-type lamins. Overexpression of both wild-type and mutant lamin A inhibited lipid accumulation, triglyceride synthesis and expression of adipogenic markers. This was associated with inhibition of expression of peroxisome-proliferator-activated receptor gamma 2 (PPAR{gamma}2) and Glut4. In contrast, embryonic fibroblasts lacking A-type lamins accumulated more intracellular lipid and exhibited elevated de novo triglyceride synthesis compared with wild-type fibroblasts. They also had increased basal phosphorylation of AKT1, a mediator of insulin signaling. We conclude that A-type lamins act as inhibitors of adipocyte differentiation, possibly by affecting PPAR{gamma}2 and insulin signaling.


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