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Originally published In Press as doi:10.1074/jbc.M000564200 on March 15, 2000
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J Biol Chem, Vol. 275, Issue 19, 14394-14400, May 12, 2000

Transgenic Mice Expressing a Truncated Form of the High Mobility Group I-C Protein Develop Adiposity and an Abnormally High Prevalence of Lipomas*

Paola ArlottaDagger §, Albert K.-F. TaiDagger , Guidalberto Manfioletti||, Charles Clifford**, Gilbert JayDagger Dagger , and Santa Jeremy OnoDagger §§

From the Dagger  Schepens Eye Research Institute, Division of Rheumatology, Immunology & Allergy, Department of Medicine, Brigham & Women's Hospital, and Committee on Immunology, Harvard Medical School, Boston, Massachusetts 02114, the  Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Universita di Trieste, via L. Giorgieri 1, Trieste, Italy, the ** Department of Pathology, Charles River Laboratories, Wilmington, Massachusetts 01887, and the Dagger Dagger  OriGene Technologies, Inc., Rockville, Maryland 20850

Chromosomal translocations in human lipomas frequently create fusion transcripts encoding high mobility group (HMG) I-C DNA-binding domains and C-terminal sequences from different presumed transcription factors, suggesting a potential role for HMG I-C in the development of lipomas. To evaluate the role of the HMG I-C component, the three DNA-binding domains of HMG I-C have now been expressed in transgenic mice. Despite the ubiquitous expression of the truncated HMG I-C protein, the transgenic mice develop a selective abundance of fat tissue early in life, show marked adipose tissue inflammation, and have an abnormally high incidence of lipomas. These findings demonstrate that the DNA-binding domains of HMG I-C, in the absence of a C-terminal fusion partner, are sufficient to perturb adipogenesis and predispose to lipomas. We provide data supporting the central utility of this animal model as a tool to understand the molecular mechanisms underlying the development of one of the most common kind of human benign tumors.

* This work was supported by National Institutes of Health Grant R01 GM49661 and by a grant from the Lucille P. Markey Foundation (to S. J. O.).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.

This work is dedicated to Jack L. Strominger and Tom Maniatis.

§ Recipient of an international fellowship from TELETHON-ITALIA.

|| Supported by funds from Associazione Italiana per la Ricerca sul Cancro (Milano, Italy) and Universita' degli Studi di Trieste and by MURST (Rome, Italy) Grant 9806279300.

§§ To whom correspondence should be addressed: Schepens Eye Research Inst., Harvard Medical School, 20 Staniford St., Boston, MA 02114. Tel.: 617-912-2521; Fax: 617-912-0127; E-mail: sjono@vision.eri.harvard.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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