Abstract：
:Amyloid beta protein (beta/A4) is deposited in senile plaques of patients with Alzheimer's disease. This protein is derived from a larger membrane-associated protein, termed amyloid precursor protein (APP). The constitutive processing of APP occurs at the central portion of beta/A4, resulting in the release of large N-terminal peptides. We have purified these peptides from the culture medium of cDNA-transfected COS-1 cells. Some of the isoforms contain the Kunitz-type protease inhibitor (KPI) domain and strongly inhibit trypsin, chymotrypsin and plasmin, but do not inhibit kallikrein, prolyl endopeptidase or granzyme A. The peptides also do not inhibit cysteine proteases such as cathepsin B or calpain. Soluble APPs lacking the KPI domain fail to inhibit any of these proteases. The results indicate that the KPI domain in soluble APPs has protease inhibitory activity against certain serine proteases.
journal_name
Biochimiejournal_title
Biochimieauthors
Shimokawa M,Nakamura K,Maruyama K,Tagawa K,Miyatake T,Sugita H,Ishiura S,Suzuki Kdoi
10.1016/0300-9084(93)90048-wsubject
Has Abstractpub_date
1993-01-01 00:00:00pages
911-5issue
10eissn
0300-9084issn
1638-6183pii
0300-9084(93)90048-Wjournal_volume
75pub_type
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