Tie2 is tied at the cell-cell contacts and to extracellular matrix by Angiopoietin-1

Shigetomo Fukuhara, Keisuke Sako, Kazuomi Noda, Kaori Nagao, Koichi Miura, Naoki Mochizuki

Research output: Contribution to journalReview articlepeer-review

58 Citations (Scopus)


Angiopoietin-1 (Ang1) binds to and activates Tie2 receptor tyrosine kinase. Ang1-Tie2 signal has been proposed to exhibit two opposite roles in the controlling blood vessels. One is vascular stabilization and the other is vascular angiogenesis. There has been no answer to the question as to how Tie2 induces two opposite responses to the same ligand. Our group and Dr. Alitalo's group have demonstrated that trans-associated Tie2 at cell-cell contacts and extracellular matrix (ECM)-anchored Tie2 play distinct roles in the endothelial cells. The complex formation depends on the presence or absence of cell-cell adhesion. Here, we review how Ang1-Tie2 signal regulates vascular maintenance and angiogenesis. We further point to the unanswered questions that must be clarified to extend our knowledge of vascular biology and to progress basic knowledge to the treatment of the diseases in which Ang1-Tie2-mediated signal is central.

Original languageEnglish
Pages (from-to)133-139
Number of pages7
JournalExperimental and Molecular Medicine
Issue number3
Publication statusPublished - Mar 31 2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry


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