LPP, a LIM protein highly expressed in smooth muscle.
An 80-kDa protein, prominently expressed in smooth muscle, was microsequenced and identified as LPP, the product of the lipoma-preferred partner gene (Petit MMR, Mols R, Schoenmakers EFPM, Mandahl N, and Van de Ven WJM. Genomics 36: 118-129, 1996). 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/microg total protein). In other mature (noncultured) tissues, including heart and skeletal muscle, the protein is present only in trace amounts and is closely correlated with the levels of the smooth muscle marker alpha-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 alpha-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 at 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.
Gorenne
Isabelle
I
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.
Nakamoto
Robert K
RK
Phelps
Clayton P
CP
Beckerle
Mary C
MC
Somlyo
Avril V
AV
Somlyo
Andrew P
AP
D021581:Active Transport, Cell Nucleus / Q000187:drug effects / Q000502:physiology; D000818:Animals; D000903:Antibiotics, Antineoplastic / Q000494:pharmacology; D001013:Aorta, Thoracic / Q000166:cytology; D002465:Cell Movement / Q000502:physiology; D002467:Cell Nucleus / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D005231:Fatty Acids, Unsaturated / Q000494:pharmacology; D005455:Fluorescent Antibody Technique; D015870:Gene Expression; D006168:Guinea Pigs; D047908:Intracellular Signaling Peptides and Proteins; D060588:LIM Domain Proteins; D008297:Male; D008970:Molecular Weight; D009131:Muscle, Smooth, Vascular / Q000166:cytology / Q000502:physiology*; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism; D011817:Rabbits; D001743:Urinary Bladder / Q000166:cytology / Q000502:physiology*; D054460:rho-Associated Kinases
D000903:Antibiotics, Antineoplastic; D003598:Cytoskeletal Proteins; D005231:Fatty Acids, Unsaturated; D047908:Intracellular Signaling Peptides and Proteins; D060588:LIM Domain Proteins; C103594:LPP protein, human; D017346:Protein Serine-Threonine Kinases; D054460:rho-Associated Kinases; C038753:leptomycin B