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Evidence that the Precursor Protein of Non-Ap Component of Alzheimer's Disease Amyloid (NACP) Has an Extended Structure Primarily Composed of Random-coil

 Jongsun Kim 
 MOLECULES AND CELLS, Vol.7(1) : 78-83, 1997 
Journal Title
Issue Date
Alzheimer Disease/etiology* ; Alzheimer Disease/physiopathology ; Amyloid/chemistry* ; Amyloid/isolation & purification ; Amyloid/physiology ; Chromatography, High Pressure Liquid ; Circular Dichroism ; Cross-Linking Reagents ; Endopeptidases ; Humans ; In Vitro Techniques ; Molecular Structure ; Molecular Weight ; Nerve Tissue Proteins* ; Protein Precursors/chemistry* ; Protein Precursors/isolation & purification ; Protein Precursors/physiology ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Synucleins
The precursor protein of the non-Aβ component of Alzheimer's disease amyloid (NACP) is a presynaptic protein of the central nervous system. The physiological function of NACP is not known, but the localization of NACP at presynaptic nerve terminals suggests that it may be involved in the neuronal function. To better understand the physiological function of NACP and its role in the pathogenesis of Alzheimer s disease (AD), the biochemical and biophysical properties of NACP were investigated. The NACP behaves abnormally on FPLC gel-filtration chromatography with the apparent molecular mass of 70 kDa, and the results from chemical cross-linking, limited proteolysis and CD experiments suggest that significant parts of NACP may be unfolded. The abnormal hydrodynamic behavior and extreme protease sensitivity of NACP could result from the extended structure which may be related to the physiological function and pathological role of this protein in the development of AD.
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1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
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