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

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• 作者：Irina Naletova ; Elena Schmalhausen ; Aleksey Kharitonov ; Aleksey Katrukha ; Luciano Saso ; Antonio Caprioli ; Vladimir Muronetz
• 关键词：Glyceraldehyde-3-phosphate dehydrogenase ; Amyloid-beta ; Oxidation ; Alzheimer's disease
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2008
• 出版时间：December 2008
• 年：2008
• 卷：1784
• 期：12
• 页码：2052-2058
• 全文大小：475 K

文摘

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).