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).

Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures / Irina, Naletova; Elena, Schmalhausen; Aleksey, Kharitonov; Aleksey, Katrukha; Saso, Luciano; Antonio, Caprioli; Vladimir, Muronetz. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - STAMPA. - 1784:12(2008), pp. 2052-2058. [10.1016/j.bbapap.2008.07.013]

Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures

SASO, Luciano;
2008

Abstract

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).
2008
005% non-ionic detergent r{cyrillic}-20; alzheimer's disease; amyloid-beta; amyloid-beta peptide (1-42); aβ; bacterial chaperonin complex; gapdh; glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (ec 1.2.1.12); groel/s; guanidine hydrochloride; guhcl; hbs-ep; 10 mm hepes; r{cyrillic}n{cyrillic} 7.4; 150 mm nacl; 3 mm edta; oxidation
01 Pubblicazione su rivista::01a Articolo in rivista
Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures / Irina, Naletova; Elena, Schmalhausen; Aleksey, Kharitonov; Aleksey, Katrukha; Saso, Luciano; Antonio, Caprioli; Vladimir, Muronetz. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - STAMPA. - 1784:12(2008), pp. 2052-2058. [10.1016/j.bbapap.2008.07.013]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/47804
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