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lüll The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspective de Tullio MB; Morelli L; Castano EMPrion 2008[Apr]; 2 (2): 51-6Insulin-degrading enzyme (IDE) is a conserved Zn(2+)metalloendopeptidase involved in insulin degradation and in the maintenance of brain steady-state levels of amyloid beta peptide (Abeta) of Alzheimer's disease (AD). Our recent demonstration that IDE and Abeta are capable of forming a stoichiometric and extremely stable complex raises several intriguing possibilities regarding the role of this unique protein-peptide interaction in physiological and pathological conditions. These include a protective cellular function of IDE as a "dead-end chaperone" alternative to its proteolytic activity and the potential impact of the irreversible binding of Abeta to IDE upon its role as a varicella zoster virus receptor. In a pathological context, the implications for insulin signaling and its relationship to AD pathogenesis are discussed. Moreover, our findings warrant further research regarding a possible general and novel interaction between amyloidogenic peptides and other Zn(2+)metallopeptidases with an IDE-like fold and a substrate conformation-dependent recognition mechanism.|Alzheimer Disease/*metabolism/pathology[MESH]|Amyloid beta-Peptides/*metabolism[MESH]|Animals[MESH]|Brain/*metabolism/pathology[MESH]|Herpesvirus 3, Human/metabolism[MESH]|Humans[MESH]|Insulysin/*metabolism[MESH]|Molecular Chaperones/*metabolism[MESH]|Multiprotein Complexes/*metabolism[MESH]|Protein Binding[MESH]|Receptors, Virus/metabolism[MESH]|Zinc/metabolism[MESH] |