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The Membrane Protein CD9/DRAP 27 Potentiates the Juxtacrine Growth Factor Activity of the Membrane-Anchored Heparin-Binding EGF-Like Growth Factor

✍ Scribed by Shigeki Higashiyama, Ryo Iwamoto, Katsutoshi Goishi, Gerhard Raab, Naoyuki Taniguchi, Michael Klagsbrun and Eisuke Mekada


Book ID
124818080
Publisher
Rockefeller University Press.
Year
1995
Tongue
English
Weight
749 KB
Volume
128
Category
Article
ISSN
0021-9525

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CD9 is a protein with 4 transmembrane domains, and functions as a cell surface antigen. We have previously reported that CD9 functions as an up-regulator of membrane-anchored heparin-binding EGF-like growth factor (proHB-EGF) activity, which is a potent mitogen as well as a soluble HB-EGF. Anti-CD9

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## Abstract Heparin‐binding EGF‐like growth factor (HB‐EGF) is initially synthesized as a type I transmembrane protein (proHB‐EGF). The proHB‐EGF is shed by specific metalloproteases, releasing the N‐terminal fragment into the extracellular space as a soluble growth factor (HB‐EGF) and the C‐termin