complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA7))

Components

• a(MESH:Bungarotoxins)
• p(HGNC:CHRNA7)

One study showed high-affinity binding of Abeta at picomolar levels to human alpha7 nAChRs heterologously expressed in cell lines, based both on the ability of Abeta to displace labeled alpha-bungarotoxin and the ability of alpha-bungarotoxin to displace fluorescently labeled Abeta (Wang et al., 2000b). PubMed:19293145

One study showed high-affinity binding of Abeta at picomolar levels to human alpha7 nAChRs heterologously expressed in cell lines, based both on the ability of Abeta to displace labeled alpha-bungarotoxin and the ability of alpha-bungarotoxin to displace fluorescently labeled Abeta (Wang et al., 2000b). PubMed:19293145

In contrast, Small et al. (2007) found no displacement of alpha-BTX from SH-SY5Y cells (a cell line very closely related to that used by Wang et al.) by either amyloid or methyllycaconitine. Wang et al. (2000b) also showed similar staining of human AD cortical neurons by alpha7 and Abeta antibodies in double immunofluorescence, suggesting that in human cortical neurons, alpha7 and Abeta are closely associated, although such an approach does not prove direct binding. However another study (Small et al., 2007) showed no displacement of labeled alpha-bungarotoxin from cell lines expressing rat alpha7 nAChRs. PubMed:19293145

In contrast, Small et al. (2007) found no displacement of alpha-BTX from SH-SY5Y cells (a cell line very closely related to that used by Wang et al.) by either amyloid or methyllycaconitine. Wang et al. (2000b) also showed similar staining of human AD cortical neurons by alpha7 and Abeta antibodies in double immunofluorescence, suggesting that in human cortical neurons, alpha7 and Abeta are closely associated, although such an approach does not prove direct binding. However another study (Small et al., 2007) showed no displacement of labeled alpha-bungarotoxin from cell lines expressing rat alpha7 nAChRs. PubMed:19293145