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Originally published as MBC in Press, 10.1091/mbc.E02-08-0459 on December 7, 2002
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Vol. 14, Issue 3, 903-915, March 2003

The Two Variants of Oxysterol Binding Protein-related Protein-1 Display Different Tissue Expression Patterns, Have Different Intracellular Localization, and Are Functionally Distinct

Marie Johansson,* Virginie Bocher,dagger Markku Lehto,* Giulia Chinetti,dagger Esa Kuismanen,Dagger Christian Ehnholm,* Bart Staels,dagger and Vesa M. Olkkonen*§

 *Department of Molecular Medicine, National Public Health Institute, Biomedicum, FIN-00251 Helsinki, Finland;  dagger Institut Pasteur de Lille and Faculté de Pharmacie, Université de Lille II-U545 Institut National de la Santé et de la Recherche Médicale, 59019 Lille, France; and  Dagger Department of Biosciences, Division of Biochemistry, Viikki Biocenter, University of Helsinki, FIN-00014 Helsinki, Finland

Oxysterol binding protein (OSBP) homologs comprise a family of 12 proteins in humans (Jaworski et al., 2001; Lehto et al., 2001). Two variants of OSBP-related protein (ORP) 1 have been identified: a short one that consists of the carboxy-terminal ligand binding domain only (ORP1S, 437 aa) and a longer N-terminally extended form (ORP1L, 950 aa) encompassing three ankyrin repeats and a pleckstrin homology domain (PHD). We now report that the two mRNAs show marked differences in tissue expression. ORP1S predominates in skeletal muscle and heart, whereas ORP1L is the most abundant form in brain and lung. On differentiation of primary human monocytes into macrophages, both ORP1S and ORP1L mRNAs were induced, the up-regulation of ORP1L being >100-fold. The intracellular localization of the two ORP1 variants was found to be different. Whereas ORP1S is largely cytosolic, the ORP1L variant localizes to late endosomes. A significant amount of ORP1S but only little ORP1L was found in the nucleus. The ORP1L ankyrin repeat region (aa 1-237) was found to localize to late endosomes such as the full-length protein. This localization was even more pronounced for a fragment that additionally includes the PHD (aa 1-408). The amino-terminal region of ORP1L consisting of the ankyrin repeat and PHDs is therefore likely to be responsible for the targeting of ORP1L to late endosomes. Interestingly, overexpression of ORP1L was found to enhance the LXRalpha -mediated transactivation of a reporter gene, whereas ORP1S failed to influence this process. The results suggest that the two forms of ORP1 are functionally distinct and that ORP1L is involved in control of cellular lipid metabolism.

§ Corresponding author. E-mail address: vesa.olkkonen{at}ktl.fi.

Molecular Biology of the Cell
Vol. 14, 903-915, March 2003
Copyright © 2003 by The American Society for Cell Biology


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