No abstract

PAGE 27890:FIGURE 6. DKK-1 blocks baicalin-induced osteoblastic differentiation. An error was found in Fig. 6A (upper panel) after publication. The gel images of (i) PGSK-3␤ by LiCl treatment (with and without DKK-1) and (ii) GSK-3␤ by LiCl treatment (with and without DKK-1) were misplaced due to an error in handling the image processing. The results from four independent experiments, from set 1 to 4, are now shown here for clarification and revision. Here, the drugs including baicalin (50 M), Wnt3a (200 ng/ml), or LiCl (10 mM) were applied onto cultured osteoblasts for 10 min, with or without the pretreatment of DKK-1 (0.2 mg/ml) for 1 h, as indicated. The total GSK-3␤, or its phosphorylated form (P-GSK-3␤), was revealed (both at ϳ46 kDa) by specific antibodies in Western blot (upper panel). The quantification of the blots was performed by a densitometer (lower panel), which was quantified based on the four independent results from set 1 to 4, as shown here. The overall result of Fig. 6A, which was illustrated on p. 27888 (line 11), remained unchanged. Values are expressed as the fold of increase to basal reading (control cultured treated with 0.02% dimethyl sulfoxide) and are means ϩ S.E.

In the mammalian brain, acetylcholinesterase (AChE) is anchored in cell membranes by a transmembrane protein PRiMA (proline-rich membrane anchor). We present evidence that at least part of the PRiMA-linked AChE is integrated in membrane microdomains called rafts. A significant proportion of PRiMA-linked AChE tetramers from rat brain was recovered in raft fractions; this proportion was markedly higher at low rather than at high concentrations of cold Triton X-100. The detergent-resistant fraction increased during brain development. In NG108-15 neuroblastoma cells transfected with cDNAs encoding AChE T and PRiMA, PRiMA-linked G 4 AChE was found in membrane rafts and showed the same sensitivity to cold Triton X-100 extraction as in the brain.