Linked Life Data

12760907

Source:http://linkedlifedata.com/resource/pubmed/id/12760907

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-8-5
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0363-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C674-85
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12760907-Active Transport, Cell Nucleus, pubmed-meshheading:12760907-Animals, pubmed-meshheading:12760907-Antibiotics, Antineoplastic, pubmed-meshheading:12760907-Aorta, Thoracic, pubmed-meshheading:12760907-Cell Movement, pubmed-meshheading:12760907-Cell Nucleus, pubmed-meshheading:12760907-Cytoskeletal Proteins, pubmed-meshheading:12760907-Fatty Acids, Unsaturated, pubmed-meshheading:12760907-Fluorescent Antibody Technique, pubmed-meshheading:12760907-Gene Expression, pubmed-meshheading:12760907-Guinea Pigs, pubmed-meshheading:12760907-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:12760907-LIM Domain Proteins, pubmed-meshheading:12760907-Male, pubmed-meshheading:12760907-Molecular Weight, pubmed-meshheading:12760907-Muscle, Smooth, Vascular, pubmed-meshheading:12760907-Protein-Serine-Threonine Kinases, pubmed-meshheading:12760907-Rabbits, pubmed-meshheading:12760907-Urinary Bladder, pubmed-meshheading:12760907-rho-Associated Kinases
pubmed:year
2003
pubmed:articleTitle
LPP, a LIM protein highly expressed in smooth muscle.
pubmed:affiliation
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.