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Puromycin insensitive leucyl‐specific aminopeptidase (PILSAP) affects RhoA activation in endothelial cells
Author(s) -
Suzuki Takahiro,
Abe Mayumi,
Miyashita Hiroki,
Kobayashi Toshimitsu,
Sato Yasufumi
Publication year - 2007
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.20980
Subject(s) - rhoa , lysophosphatidic acid , microbiology and biotechnology , stress fiber , puromycin , angiogenesis , receptor , biology , morphogenesis , membrane ruffling , rac1 , g protein coupled receptor , intracellular , signal transduction , chemistry , cell , biochemistry , focal adhesion , cytoskeleton , cancer research , protein biosynthesis , gene
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. J. Cell. Physiol. 211: 708–715, 2007. © 2007 Wiley‐Liss, Inc.