Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins

Tetsuya Akada, Tohru Yamazaki, Hiroki Miyashita, Osamu Niizeki, Mayumi Abe, Akira Sato, Susumu Satomi, Yasufumi Sato

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8 Citations (Scopus)


We previously reported that mouse orthologue of puromycin insensitive leucyl-specific aminopeptidase (mPILSAP) played an important role in angiogenesis by regulating the proliferation and migration of endothelial cells (ECs) (Miyashita et al., 2002. Blood 99:3241-3249). Here, we examined the mechanism as to how mPILSAP regulates the migration of ECs. Cell adhesion through integrins plays a crucial role in cell migration, and ECs use at least type-1 collagen receptor integrin α2β1, fibronectin receptor α5β1, and vitronectin receptors αvβ3 and αvβ5. mPILSAP antisense oligodeoxynucleotide (AS-ODN) or leucinethiol (LT), a leucyl-aminopeptidase inhibitor, did not affect the attachment but did significantly inhibit the spreading of cells of the murine endothelial cell line MSS31 when they were plated on vitronectin-, fibronectin-, or type-1 collagen, although they did not affect the expression of integrin α2, α5, αv, β1, β3, and β5 subunits on the cell surface. AS-ODN and LT also inhibited the tyrosine phosphorylation of FAK when cells were plated on vitronectin, fibronectin, or type-1 collagen. This inhibition of cell spreading and of tyrosine phosphorylation of FAK could be negated by Mg2+. These results suggest that mPILSAP is involved in the activation of endothelial integrins.

Original languageEnglish
Pages (from-to)253-262
Number of pages10
JournalJournal of Cellular Physiology
Issue number2
Publication statusPublished - 2002 Nov

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology


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