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P2–138: Chemokine serum levels in mild cognitive impairment as Alzheimer's disease early biomarkers
Author(s) -
Galimberti Daniela,
Fenoglio Chiara,
Lovati Carlo,
Venturelli Eliana,
Guidi Ilaria,
Corrà Barbara,
Scalabrini Diego,
Clerici Francesca,
Mariani Claudio,
Bresolin Nereo,
Scarpini Elio
Publication year - 2006
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.2006.05.976
Subject(s) - pathogenesis , medicine , chemokine , immunology , alzheimer's disease , peripheral blood mononuclear cell , cerebrospinal fluid , disease , inflammation , biology , biochemistry , in vitro
fluids spans twelve orders of magnitude, with about 90% of the total protein content being represented by only six proteins, that is serum albumin (HSA), IgG, IgA, haptoglobin, antitrypsin and transferrin. Thus, we tested several chromatographic techniques to deplete abundant proteins in human serum and cerebrospinal fluid samples. Whereas HSA can be removed by a blue column or the POROS Affinity Depletion Cartridge (Applied Biosystems, Langen, Germany), it was much more effective to remove several dominant proteins with commercially available affinity columns based on antibodies. The multiple affinity removal system (MARS, Agilent Technologies GmbH, Waldbronn, Germany) quantitatively removed the six most abundant proteins, as mentioned above, and the IgY-12 Proteome Partitioning Spin Column (Beckmann-Coulter GmbH, Unterschlei heim, Germany) removed even twelve abundant proteins. The IgY-12 column depleted besides the six most dominant proteins also IgM, fibrinogen, apolipoprotein (A-I and A-II), -1 acid glycoprotein and -2 macroglobulin from human body fluids. The depleted samples were analyzed by 2-DE followed by western blotting. Specific low-abundant proteins were tested as potential biomarkers with monoclonal antibodies (mAbs) in western-blot analysis to retrieve disease-related spots in the 2D-pattern.