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- W2009676102 abstract "Based upon recent evidence that the secreted form of APP can cause the release of cytokines and elicit other biological activities, we sought to identify whether a receptor could be identified on the surface of cells. The secreted amyloid precursor protein containing the Kunitz domain (scAPP 751 ) is identical to protease nexin II, a protease inhibitor which has been shown to form complexes with labeled EGF binding protein that subsequently binds to cells. Results of [ 125 I]scAPP 751 -trypsin complex incubated with intact fibroblast cells show that the complex appears to bind in a saturable time-dependent and reversible manner. The kinetic constants from the binding studies demonstrate a k 1 = 2.5 × 10 7 M −1 s −1 and k 2 =4.7 × 10 −4 s −1 and thus a K D (=k 2 /k 1 ) = 20 pM. Furthermore, the complex formation of [ 125 I]scAPP 751 with a protease appears to be a requirement for optimal binding. The binding affinity of secreted APP demonstrated in this study is consistent with its potency in eliminating a range of biological efforts that have been documented." @default.
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- W2009676102 date "1994-05-01" @default.
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- W2009676102 title "Identification of Secreted β-Amyloid Precursor Protein Binding Sites on Intact Human Fibroblasts" @default.
- W2009676102 doi "https://doi.org/10.1006/bbrc.1994.1646" @default.
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