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Originally published In Press as doi:10.1194/jlr.M700396-JLR200 on October 5, 2007

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Journal of Lipid Research, Vol. 49, 206-216, January 2008
Copyright © 2008 by American Society for Biochemistry and Molecular Biology

Mammary glands of adipophilin-null mice produce an amino-terminally truncated form of adipophilin that mediates milk lipid droplet formation and secretion

Tanya D. Russell1,*,{dagger}, Carol A. Palmer1,§, David J. Orlicky**, Elise S. Bales{dagger}, Benny Hung-Junn Chang{dagger}{dagger}, Lawrence Chan{dagger}{dagger} and James L. McManaman2,*,{dagger},§

* Graduate Program in Molecular Biology, Division of Basic Reproductive Science, University of Colorado at Denver and Health Sciences Center, Aurora, CO
{dagger} Graduate Program in Molecular Biology, Department Obstetrics and Gynecology, University of Colorado at Denver and Health Sciences Center, Aurora, CO
§ Graduate Program in Molecular Biology, Department of Physiology and Biophysics, University of Colorado at Denver and Health Sciences Center, Aurora, CO
** Graduate Program in Molecular Biology, Department of Pathology, University of Colorado at Denver and Health Sciences Center, Aurora, CO
{dagger}{dagger} Department of Molecular and Cellular Biology and Division of Diabetes, Endocrinology, and Metabolism, Department of Medicine, Baylor College of Medicine, Houston, TX

Published, JLR Papers in Press, October 5, 2007.

1 T. D. Russell and C. A. Palmer contributed equally to this study.

2 To whom correspondence should be addressed. e-mail: jim.mcmanaman{at}uchsc.edu

Adipophilin (ADPH), a member of the perilipin family of lipid droplet-associated proteins, is hypothesized to mediate milk lipid formation and secretion. Unexpectedly, the fat content of milk from ADPH-null mice was only modestly lower than that of wild-type controls, and neither TIP47 nor perilipin appeared to fully compensate for ADPH loss. This prompted us to investigate the possibility that the mutated ADPH gene was not a genuine null mutation. ADPH transcripts were detected in ADPH-null mammary tissue by quantitative real-time PCR, and C-terminal-specific, but not N-terminal-specific, ADPH antibodies detected a single lower molecular weight product and immunostained cytoplasmic lipid droplets (CLDs) and secreted milk fat globules in ADPH-null mammary tissue. Furthermore, stable cell lines expressing cDNA constructs corresponding to the ADPH-null mutation produced a product comparable in size to the one detected in ADPH-null mammary glands and localized to CLDs. Based on these data, we conclude that ADPH-null mice express an N-terminally truncated form of ADPH that retains the ability to promote the formation and secretion of milk lipids.

Supplementary key words PAT domain • functional differentiation • TIP47 compensation


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