Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1784, Issue 12, Pages 2052-2058Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2008.07.013
Keywords
Glyceraldehyde-3-phosphate dehydrogenase; Amyloid-beta; Oxidation; Alzheimer's disease
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Funding
- RFBR [OS-04-00231-a, 08-0800540-a]
- President of Russian Federation [MC-467.2008.4]
- NATO [(PDD(CP)-(CBP.NR.RIG 982779))]
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Interactions between different forms of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and amyloid-beta peptide (1-42) were investigated by direct (surface plasmon resonance) and indirect (kinetics of spontaneous and GroEL/S-assisted reactivation of denatured GAPDH) methods. It was demonstrated that non-native forms of GAPDH obtained by different ways (cold denaturation, oxidation of the enzyme, and its unfolding in guanidine hydrochloride) efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42). The results suggest that non-native GAPDH species can be involved in the formation of amyloid structures during Alzheimer's disease, binding to soluble amyloid-beta peptide (1-42). (c) 2008 Elsevier B.V. All rights reserved.
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