scholarly journals Amino-terminal Processing of Cell Surface Heparin-binding Epidermal Growth Factor-like Growth Factor Up-regulates Its Juxtacrine but Not Its Paracrine Growth Factor Activity

1996 ◽  
Vol 271 (48) ◽  
pp. 30858-30863 ◽  
Author(s):  
Takatoshi Nakagawa ◽  
Shigeki Higashiyama ◽  
Toshihide Mitamura ◽  
Eisuke Mekada ◽  
Naoyuki Taniguchi
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Heparin Binding ◽  
Factor Activity ◽  
Amino Terminal ◽  
Epidermal Growth ◽  
Paracrine Growth Factor

scholarly journals The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF)

2002 ◽  
Vol 367 (1) ◽  
pp. 229-238 ◽  
Author(s):  
Véronique HOSPITAL ◽  
Eiichiro NISHI ◽  
Michael KLAGSBRUN ◽  
Paul COHEN ◽  
Nabil G. SEIDAH ◽  
...  
Keyword(s):  
Amino Acid ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Active Site ◽  
Regulatory Element ◽  
Enzymic Activity ◽  
Heparin Binding ◽  
Epidermal Growth

Nardilysin (N-arginine dibasic convertase, or NRDc) is a cytosolic and cell-surface metalloendopeptidase that, in vitro, cleaves substrates upstream of Arg or Lys in basic pairs. NRDc differs from most of the other members of the M16 family of metalloendopeptidases by a 90 amino acid acidic domain (DAC) inserted close to its active site. At the cell surface, NRDc binds heparin-binding epidermal growth factor-like growth factor (HB-EGF) and enhances HB-EGF-induced cell migration. An active-site mutant of NRDc fulfills this function as well as wild-type NRDc, indicating that the enzyme activity is not required for this process. We now demonstrate that NRDc starts at Met49. Furthermore, we show that HB-EGF not only binds to NRDc but also potently inhibits its enzymic activity. NRDc—HB-EGF interaction involves the 21 amino acid heparin-binding domain (P21) of the growth factor, the DAC of NRDc and most probably its active site. Only disulphide-bonded P21 dimers are inhibitory. We also show that Ca2+, via the DAC, regulates both NRDc activity and HB-EGF binding. We conclude that the DAC is thus a key regulatory element for the two distinct functions that NRDc fulfills, i.e. as an HB-EGF modulator and a peptidase.

scholarly journals Heparin-binding epidermal growth factor-like growth factor is an autocrine growth factor for human keratinocytes.

1994 ◽  
Vol 269 (31) ◽  
pp. 20060-20066 ◽  
Author(s):  
K. Hashimoto ◽  
S. Higashiyama ◽  
H. Asada ◽  
E. Hashimura ◽  
T. Kobayashi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Human Keratinocytes ◽  
Heparin Binding ◽  
Autocrine Growth ◽  
Autocrine Growth Factor ◽  
Epidermal Growth

Epidermal Growth Factor Tethered through Coiled-Coil Interactions Induces Cell Surface Receptor Phosphorylation

2009 ◽  
Vol 20 (8) ◽  
pp. 1569-1577 ◽  
Author(s):  
Cyril Boucher ◽  
Benoît Liberelle ◽  
Mario Jolicoeur ◽  
Yves Durocher ◽  
Gregory De Crescenzo
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Coiled Coil ◽  
Cell Surface Receptor ◽  
Receptor Phosphorylation ◽  
Surface Receptor ◽  
Epidermal Growth

scholarly journals Differential Pathways of Angiotensin II-Induced Extracellularly Regulated Kinase 1/2 Phosphorylation in Specific Cell Types: Role of Heparin-Binding Epidermal Growth Factor

2004 ◽  
Vol 18 (8) ◽  
pp. 2035-2048 ◽  
Author(s):  
Bukhtiar H. Shah ◽  
Akin Yesilkaya ◽  
J. Alberto Olivares-Reyes ◽  
Hung-Dar Chen ◽  
László Hunyady ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Types ◽  
Specific Cell ◽  
Heparin Binding ◽  
Epidermal Growth
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