P4–076: Immobilization of β–amyloid peptide on a chip and characterization of its interaction with proteins via atomic force microscopy and mass spectrometry | Zendy

Boussert Stéphanie | Zendy

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P4–076: Immobilization of β–amyloid peptide on a chip and characterization of its interaction with proteins via atomic force microscopy and mass spectrometry

Author(s) -

Boussert Stéphanie

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.2006.05.1814

Subject(s) - peptide , chemistry , self assembled monolayer , monolayer , mass spectrometry , amyloid (mycology) , atomic force microscopy , amyloid precursor protein , biophysics , characterization (materials science) , colloidal gold , nanotechnology , chromatography , biochemistry , nanoparticle , materials science , alzheimer's disease , inorganic chemistry , biology , medicine , disease , pathology

by fibrillar A . To explore this possibility, primary rat astrocytes were used to test IDE levels after exposure to soluble or fibrillar A . After treatment with 5 M fibrillar A , IDE protein and transcripts increased 2-fold as detected by WB, immunofluorescence and RT-PCR compared to soluble A or control cultures. Conclusions: Our results suggest that the defective clearance of A due to IDE lower expression or activity is not an accelerating factor in Tg2576 mice amyloid deposition. Moreover, IDE overexpression associated to late-stages of the neuropathologic process in this animal model may be part of an inflammatory response, suggesting a new role for IDE in the brain that deserves future investigation.

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