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Amyloid β concentrations and stable isotope labeling kinetics of human plasma specific to central nervous system amyloidosis
Author(s) -
Ovod Vitaliy,
Ramsey Kara N.,
Mawuenyega Kwasi G.,
Bollinger Jim G.,
Hicks Terry,
Schneider Theresa,
Sullivan Melissa,
Paumier Katrina,
Holtzman David M.,
Morris John C.,
Benzinger Tammie,
Fagan Anne M.,
Patterson Bruce W.,
Bateman Randall J.
Publication year - 2017
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2017.06.2266
Subject(s) - amyloidosis , cerebrospinal fluid , kinetics , amyloid (mycology) , central nervous system , chemistry , blood plasma , pathology , endocrinology , biochemistry , medicine , physics , quantum mechanics , inorganic chemistry
Cerebrospinal fluid analysis and other measurements of amyloidosis, such as amyloid‐binding positron emission tomography studies, are limited by cost and availability. There is a need for a more practical amyloid β (Aβ) biomarker for central nervous system amyloid deposition. Methods We adapted our previously reported stable isotope labeling kinetics protocol to analyze the turnover kinetics and concentrations of Aβ38, Aβ40, and Aβ42 in human plasma. Results Aβ isoforms have a half‐life of approximately 3 hours in plasma. Aβ38 demonstrated faster turnover kinetics compared with Aβ40 and Aβ42. Faster fractional turnover of Aβ42 relative to Aβ40 and lower Aβ42 and Aβ42/Aβ40 concentrations in amyloid‐positive participants were observed. Discussion Blood plasma Aβ42 shows similar amyloid‐associated alterations as we have previously reported in cerebrospinal fluid, suggesting a blood‐brain transportation mechanism of Aβ. The stability and sensitivity of plasma Aβ measurements suggest this may be a useful screening test for central nervous system amyloidosis.