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1 Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA
2 Huntsman Cancer Institute and Department of Biology, University of Utah, Salt Lake City, UT, USA
* To whom correspondence should be addressed. E-mail: aps2n{at}virginia.edu.
An 80 kDa protein, prominently expressed in smooth muscle, was microsequenced and identified as LPP, the product of the Lipoma-Preferred Partner gene (21). Using a specific anti-LPP antibody we showed, in Western blots and with immunofluorescence microscopy, the selective expression of LPP in vascular and visceral smooth muscles (approximately 0.5-1 ng/µg total protein). In other mature (non-cultured) tissues, including heart and skeletal muscle, the protein is present only in trace amounts and closely correlated with the levels of the smooth muscle marker, 
-actin. In freshly isolated guinea-pig bladder smooth muscle cells, immunofluorescence images showed LPP as linear arrays of punctate, longitudinally oriented staining superimposed with vinculin staining on the plasma membrane surface. A corresponding pattern of periodic labeling at the membrane in transverse sections of bladder smooth muscle suggested an association of LPP with peripheral dense bodies. In cultured rat aortic smooth muscle cells, LPP colocalized with vinculin at focal adhesions, but not with p120 catenin or -actinin. Overexpression of the protein increased EGF-stimulated migration of vascular smooth muscle cells in Transwell assays, suggesting the participation of LPP in cell motility. The Rho-kinase inhibitor, Y-27632, dissociated focal adhesions and LPP staining from the cell periphery, and enhanced the nuclear accumulation of LPP induced by leptomycin B, indicating that LPP has a potential for relocating to the nucleus through a shuttling mechanism that is sensitive to inhibition of Rho-kinase.
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