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An abnormality of plasma amyloid protein precursor in Alzheimer's disease


Bush, AI and Whyte, S and Thomas, LD and Williamson, TG and Van Tiggelen, CV and Currie, J and Small, DH and Moir, RD and Li, QX and Rumble, B and Monning, U and Beyreuther, K and Masters, CL, An abnormality of plasma amyloid protein precursor in Alzheimer's disease, Annals of Neurology, 32, (1) pp. 57-65. ISSN 0364-5134 (1992) [Refereed Article]

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DOI: doi:10.1002/ana.410320110


βA4 amyloid deposition in the brain, which is characteristic of Alzheimer's disease(AD), may result from either overexpression of the amyloid protein precursor (APP) or failure of APP to be correctly processed. A blood marker reflecting this abnormal metabolism would be of diagnostic value and would provide a means of monitoring the efficacy of therapeutic interventions. We analyzed immunoblots of plasma APP enriched by heparin‐Sepharose chromatography from patients with moderate to severe AD dementia (n = 34) and control subjects (n = 77) and found an approximately 50% increase in the proportion of 130‐kd APP species in patients with AD (p < 0.001), no difference in the 110‐kd form, a 15 to 30% decrease in the 65‐kd form (p < 0.001), and a 20 to 35% decrease in the proportion of 42‐kd APP (p < 0.001). These species of APP were soluble, lacked the carboxyl terminus, and the 110‐and 42‐kd species were shown to be consistent with degradation products derived from the 130‐kd species. A comparison of levels of 130‐kd plasma APP from moderately to severely demented patients with AD and control subjects distinguished the two groups with a specificity of 87.0% and a sensitivity of 79.4%. Copyright © 1992 The American Neurological Association

Item Details

Item Type:Refereed Article
Research Division:Biomedical and Clinical Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:75467
Year Published:1992
Web of Science® Times Cited:61
Deposited By:Research Division
Deposited On:2012-01-31
Last Modified:2012-03-15

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