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P3‐289: Microelectrode arrays and Alzheimer's disease: A novel in vitro investigative paradigm
Author(s) -
Varghese Kucku,
Molnar Peter,
Das Mainak,
Kindy Mark S.,
Wheeler Bruce C.,
Hickman James J.
Publication year - 2009
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.2009.04.960
Subject(s) - hippocampal formation , toxicity , programmed cell death , multielectrode array , electrophysiology , patch clamp , extracellular , in vitro , synapse , chemistry , neuroscience , biophysics , pharmacology , microelectrode , biology , biochemistry , apoptosis , electrode , organic chemistry
Ab-40 and Ab-42 monomers. The dissociation constant of anti-amyloid antibodies in the D-IgG fraction was determined by Surface Plasmon Resonance (SPR). As a probe of polyvalency, direct binding and Ab competition ELISAs were performed using thyroglobulin as the competing antigen. Results: Dimeric IgG comprised 8-17% of the total IgG in various IVIG preparations. The Ab-binding specific activity of D-IgG was greater than that of M-IgG by a factor of 10.5. The dissociation constant for D-IgG on the Ab monomer SPR sensor was 1.4 micromolar. Thyroglobulin reduced binding to Ab ELISA monomer plates by 70% suggesting that IVIG contains anti-monomer antibodies that cross-react with non-Ab antigens. Conclusions: The dimer fraction of IVIG possesses significant Ab binding capacity. However, anti-monomer antibodies in the dimer fraction have relatively low affinity for Ab and may be cross-reactive with non-amyloid antigens. Future studies will address the extent to which Ab binding by antibodies in the monomeric and dimeric fractions contributes to IVIG’s therapeutic effects in AD patients.