Faculty Opinions recommendation of [CONFERENCE POSTER]: The protein kinase DYRK1A increases alpha-secretase activity in neuronal cells and accelerates cleavage of amyloid precursor protein.

Author(s):  
W Sue Griffin
2003 ◽  
Vol 278 (29) ◽  
pp. 26687-26694 ◽  
Author(s):  
Stephen H. Pasternak ◽  
Richard D. Bagshaw ◽  
Marianne Guiral ◽  
Sunqu Zhang ◽  
Cameron A. Ackerley ◽  
...  

1999 ◽  
Vol 343 (2) ◽  
pp. 371-375 ◽  
Author(s):  
Hisashi KOIKE ◽  
Shigeo TOMIOKA ◽  
Hiroyuki SORIMACHI ◽  
Takaomi C. SAIDO ◽  
Kei MARUYAMA ◽  
...  

MDC9, also known as meltrin γ, is a membrane-anchored metalloprotease. MDC9 contains several distinct protein domains: a signal sequence followed by a prodomain and a domain showing sequence similarity to snake venom metalloproteases, a disintegrin-like domain, a cysteine-rich region, an epidermal-growth-factor-like repeat, a transmembrane domain and a cytoplasmic domain. Here we demonstrate that MDC9 expressed in COS cells is cleaved between the prodomain and the metalloprotease domain. Further, when MDC9 was co-expressed in COS cells with amyloid precursor protein (APP695) and treated with phorbol ester, APP695 was digested exclusively at the α-secretory site in MDC9-expressing cells. When an artificial α-secretory site mutant was also co-expressed with MDC9 and treated with phorbol ester, APP secreted by α-secretase was not increased in conditional medium. Inhibition of MDC9 by a hydroxamate-based metalloprotease inhibitor, SI-27, enhanced β-secretase cleavage. These results suggest that MDC9 has an α-secretase-like activity and is activated by phorbol ester.


1993 ◽  
Vol 695 (1) ◽  
pp. 128-131 ◽  
Author(s):  
BARBARA E. SLACK ◽  
ROGER M. NITSCH ◽  
ETTA LIVNEH ◽  
GEORGE M. KUNZ ◽  
HAGIT ELDAR ◽  
...  

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