Aminopeptidase N/CD13 is an endothelial cell surface ectoenzyme involved in one of the initial steps of angiogenesis. However, little is known how APN induces angiogenesis in endothelial cells. Using human cDNA library-encoding phage display biopanning method, we here identified a galactoside-specific lectin family protein, galectin-3, as an interacting protein of APN. Galectin-3 specifically binds to APN both in vitro and in human umbilical vein endothelial cells (HUVECs) in a carbohydrate recognition-dependent manner. Immunohistochemical analysis demonstrates that both APN and galectin-3 are exclusively coexpressed during the angiogenic stage of mouse forebrain development. Finally, exogenous addition of galectin-3 into HUVECs induced angiogenesis in an APN-dependent manner, implying that APN is a crucial mediator of galectin-3-induced angiogenesis in endothelial cells.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 2007 Nov 16|
Bibliographical noteFunding Information:
We are grateful to Drs. J.M. Kim and W.J. Lee for their help with phage library construction. This study was partially supported by grants from the Chemical Genomics program, the National Research Laboratory from the Korean Ministry of Science and Technology, and the Brain Korea 21 Project, Republic of Korea.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology