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. Author manuscript; available in PMC: 2010 Nov 10.
Published in final edited form as: Biochem Biophys Res Commun. 2010 Jul 24;399(4):487–491. doi: 10.1016/j.bbrc.2010.07.081

Fig. 2.

Fig. 2

AICAR modulates APP β-cleavage through reducing APP lipid raft distribution. The effect of AICAR (0.5 and/or 1 mM/36 h) on cellular levels of APP, BACE1 and C99 (C-terminal fragment of APP generated by β-secretase; β-CTF) (A-i), activities of α- and β-secretases in post-nuclear fractions (A-ii), APP distribution in membrane micro-domains (B-i) were analyzed in primary cultured rat cortical neurons. The distribution of APP in the lipid raft fractions was determined by comparing protein levels of APP and non-lipid raft markers (CD71 and clathrin), marker for glycosylphosphatidylinositol-anchored protein containing lipid rafts (PrP) or caveolae marker (flotillin-1) (B-i). The protein levels of APP in fractions # 2 and 3 (control and 0.5 mM AICAR) were quantified and represented on bar graph (B-ii). The lack of differences in protein quantities in each fraction between control (CON) and AICAR treated groups (B-iii) indicate that the observed alterations in APP levels are not due to the differences of protein amounts. The effects of AICAR on α-and β-secretase activities and BACE1 protein levels in lipid raft fractions (fraction # 2) were also measured (C). The vertical bar on each group indicates the standard error of mean (*P < 0.05 compared to control group in each fraction).