Skip to main content

Table 2 Glycosylation of sAPPα and sAPPβ in culture media from CHO-PS70 cell treated with Aβ42

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

  %APP unbound to the lectin
sAPPα sAPPβ
CHO-PS70 cell media Con A PHA Con A PHA
Control 41.9 ± 4.8 [26.9–61.8] 62.2 ± 3.2 [51.8–74.2] 57.3 ± 5.8 [40.0–77.1] 75.0 ± 3.5 [62.6–87.5]
Aβ42 24.7 ± 2.6* [12.9–30.0] 52.5 ± 2.4* [44.2–53.3] 28.9 ± 3.2* [39.0–16.9] 56.6 ± 3.0* [46.1–68.6]
  1. The culture media from CHO-PS70 cells (over-expressing APP 751) treated with Aβ42 or scrambled peptide (control) were incubated with immobilized Con A and PHA lectins. The supernatant recovered containing the unbound protein was evaluated by western blots using with pan-specific antibodies for sAPPα and sAPPβ, similarly that in Table 1. Accordingly, the unbound sAPPα and sAPPβ were used to compare differences in lectin binding between groups and between sAPP species. The data represent the percentages (mean ± SEM) and the intervals of the unbound immunoreactivity for sAPPα and sAPPβ, estimated in 8 independent determinations from 2 different experiments
  2. *Significantly different (p < 0.05) from the control group
  3. Significantly different (p < 0.05) from the sAPPα species