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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
,
* Graduate Program in Molecular Biology, Division of Basic Reproductive Science, University of Colorado at Denver and Health Sciences Center, Aurora, CO
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
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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