Linked Life Data

17385722

Source:http://linkedlifedata.com/resource/pubmed/id/17385722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-4-2
pubmed:abstractText
Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) expressed in endothelial cells (ECs) plays an important role in angiogenesis due to its involvement in migration, proliferation and network formation. Here we examined the biological function of PILSAP with respect to EC morphogenesis and the related intracellular signaling for this process. When mouse endothelial MSS31 cells were cultured, a dominant negative PILSAP mutant converted cell shape to disk-like morphology, blocked stress fiber formation, and augmented membrane ruffling in random directions. These phenotypic changes led us to test whether PILSAP affected activities of Rho family small G-proteins. Abrogation of PILSAP enzymatic activity or its expression attenuated RhoA but not Rac1 activation during cell adhesion. This attenuation of RhoA activation was also evident when G-protein coupled receptors such as proteinase-activated receptor or lysophosphatidic acid receptor were activated in ECs. These results indicate that PILSAP affects RhoA activation and that influences the proper function of ECs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9541
pubmed:author
pubmed:issnType
Print
pubmed:volume
211
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
708-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) affects RhoA activation in endothelial cells.
pubmed:affiliation
Department of Vascular Biology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't