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Levels of ADAM10 are reduced in Alzheimer's disease CSF

Artikel i vetenskaplig tidskrift
Författare A. Sogorb-Esteve
M. S. Garcia-Ayllon
Johan Gobom
J. Alom
Henrik Zetterberg
Kaj Blennow
J. Saez-Valero
Publicerad i Journal of Neuroinflammation
Volym 15
ISSN 1742-2094
Publiceringsår 2018
Publicerad vid Institutionen för neurovetenskap och fysiologi, sektionen för psykiatri och neurokemi
Språk en
Länkar dx.doi.org/10.1186/s12974-018-1255-...
Ämnesord amyloid precursor protein, mild cognitive impairment, alpha-secretase, adam10, human cerebrospinal-fluid, tace activity, bace1 activity, disintegrin, metalloprotease, identification, dimerization, Immunology, Neurosciences & Neurology
Ämneskategorier Neurokemi, Immunologi inom det medicinska området

Sammanfattning

Background: The disintegrin metalloproteinase 10 (ADAM10) is the main alpha-secretase acting in the non-amyloidogenic processing of the amyloid precursor protein. This study assesses whether ADAM10 is present in cerebrospinal fluid (CSF), and whether it has potential as a biomarker for Alzheimer's disease (AD). Methods: ADAM10 was characterized in human CSF samples by immunoprecipitation and western blotting using antibodies specific for different domains of the protein and by ultracentrifugation in sucrose density gradients. Samples from AD patients (n = 20) and age-matched non-AD controls (n = 20) were characterized for classical CSF biomarkers, A beta 42, T-tau, or P-tau by ELISA, and assayed for soluble ADAM10 levels by western blotting. Results: We found that ADAM10 is present in human CSF as several distinct species: an immature form retaining the prodomain (proADAM10; similar to 80 kDa), a mature unprocessed full-length form (ADAM10f; similar to 55 kDa), and a truncated large soluble form released from the membrane (sADAM10; similar to 50 kDa). Fractionation by ultracentrifugation on sucrose density gradients showed that the ADAM10f and sADAM10 species form large complexes. Immunoblotting revealed a significant decrease in ADAM10f and sADAM10 in AD CSF compared to control CSF, while proADAM10 levels remained unaltered. Conclusions: Several forms of ADAM10 are present in CSF, mainly assembled as high-molecular weight complexes. The determination of the levels of mature forms of CSF-ADAM10 may be useful as a biomarker for AD.

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