Journal
MOLECULAR BIOLOGY
Volume 48, Issue 4, Pages 607-614Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0026893314040098
Keywords
phosphorylation; amyloid-beta; mass spectrometry; quantitative evaluation
Categories
Funding
- Russian Foundation for Basic Research [13-08-01445-a, 14-08-01236-a, 14-08-31652-mol_a, 14-08-31360mol_a, 13-04-40110-N-KOMFI]
- Ministry of Education and Sciences of the Russian Federation [14.132.21.1780, 14.132.21.1779, 8149, 16.512.11.2081]
- Presidium of the Russian Academy of Sciences (Program Molecular and Cellular Biology)
- Presidium of the Russian Academy of Sciences (Program Fundamental Science for Medicine)
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Recently, amyloid-beta (A beta) phosphorylation at position 8 has been shown to be associated with pathogenesis of Alzheimer's disease. Since the modification occurs in the key fragment of the metal-binding domain of A beta and should seriously affect the interaction of pS8-A beta with zinc ions, this isoform may be a potential precursor of pathogenic oligomer forms of A beta. Hence the level of pS8-A beta in human biological fluids (blood, urine, cerebrospinal fluid) may reflect various stages of pathogenesis of the Alzheimer's disease. The aim of the work was to develop a prototype of an analytical method for quantitative determination of the level of pS8-A beta isoform in binary mixtures with native A beta in order to further use it to estimate the levels of phosphorylated amyloid-beta in blood plasma samples of patients diagnosed with Alzheimer's disease.
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