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Table 1 Glycosylation of sAPPα and sAPPβ in brain extracts from NDC and AD subjects

From: Amyloid precursor protein glycosylation is altered in the brain of patients with Alzheimer’s disease

 

%APP unbound to the lectin

sAPPα

sAPPβ

Sample

APP specie

Con A

PHA

Con A

PHA

NDC

APP695

12.2 ± 1.7 [7.3–20.6]

6.6 ± 0.8 [4.3–9.4]

2.9 ± 0.8 [0.3–7.1]

2.6 ± 0.8 [0.2–6.8]

APP-KPI

13.7 ± 2.1 [9.2–24.6]

5.7 ± 0.8 [2.8–8.1]

40.4 ± 4.6 [20.2–58.3]

37.0 ± 3.2 [22.6–51.0]

AD

APP695

7.0 ± 1.5 [2.4–12.9]

4.0 ± 0.6 [1.8–6.8]

1.2 ± 0.5 [0.1–3.7]

1.9 ± 0.3 [1.0–3.1]

APP-KPI

7.7 ± 1.3 [4.0–12.4]

3.8 ± 0.6 [2.3–5.4]

57.1 ± 8.5 [37.6–89.0]

56.7 ± 9.7 [27.4–95.3]

  1. The brain extracts from 7 non-demented controls (NDC) and 7 AD patients were incubated with immobilized Con A and PHA lectins. The supernatant recovered that contained the unbound protein was assayed in western blots probed with pan-specific antibodies for sAPPα and sAPPβ (see Fig. 3). The data represent the percentages (mean ± SEM) and the intervals of the unbound immunoreactivity for sAPPα and sAPPβ. These values were used to compare the differences in lectin binding between the species and groups (see Figs. 5, 6, and 7)
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Alzheimer's Research & Therapy

ISSN: 1758-9193