Fig. 1

Different ADAM10 species are present in human CSF. a Schematic representation of ADAM10 and its domain organization, which consists of a pro-domain (Pro), a zinc-binding metalloprotease (Protease) domain, a disintegrin domain (Dis), which binds to integrin cell adhesion molecules, a cysteine-rich domain (Cys), a variable stalk region, a transmembrane (TM) domain, and a cytosolic domain (Cyto). Not drawn in scale; adapted from [29]. The potential species resulting from proteolytic removal of the prodomain that are further released from the membrane are indicated (immature form, proADAM10; mature full-length form, ADAM10f; truncated soluble form, sADAM10). The approximate localizations matching identified ADAM10 peptides in human CSF by nano-LC-MS analysis are indicated (see Additional file 1: TableS1 for additional details). b Western blot of human CSF samples from controls (non-AD) subjects, resolved with the indicated anti-ADAM10 antibodies. Arrow head indicates a non-specific band (see C). c Control CSF samples were immunoprecipitated with the ADAM10 N-terminal antibody, and precipitated proteins (IP) were immunoblotted with either ADAM10 (ectodomain) or albumin antibodies. The same CSF samples were incubated, in parallel, with a non-specific rabbit IgG and analyzed as negative controls (IP control, IPc). For the blot resolved for albumin, the unbound fraction (Unb) is also shown to demonstrated that ADAM10 antibodies is not able to pull-down albumin