Amyloid fil rouge from invertebrate up to human ageing: A focus on Alzheimer disease

Amyloid fibrils and fibril-like structures are currently estimated to represent many different products of several genes in humans and play a key role in many types of proteinopathies, commonly associated with ageing process. They share the mutual feature of aggregation-prone proteins and the buildi...

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Veröffentlicht in:Mechanisms of ageing and development 2022-09, Vol.206, p.111705-111705, Article 111705
Hauptverfasser: de Eguileor, Magda, Grimaldi, Annalisa, Pulze, Laura, Acquati, Francesco, Morsiani, Cristina, Capri, Miriam
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Sprache:eng
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Zusammenfassung:Amyloid fibrils and fibril-like structures are currently estimated to represent many different products of several genes in humans and play a key role in many types of proteinopathies, commonly associated with ageing process. They share the mutual feature of aggregation-prone proteins and the building up of molecular-supramolecular structure, such as inter-neuronal plaques in the brain of Alzheimer’s Disease (AD) patients, characterized by an extraordinary strength. Noteworthy, this type of structure has been reported in different organisms, in particular in invertebrates. The aim of the current review is to focus on alpha and beta amyloids i.e., SAAs, SAP and APP, elucidating the structure and function of amyloid proteins in invertebrates (such as nematods, annelids, molluscs, insects, ascidians) and highlighting their striking pattern of functional conservation when compared to human amyloid-like fibrils, thus focusing on possible new studies and applications for innovative therapies, particularly for AD, the most common and worldwide type of dementia. •Amyloidogenesis is a process conserved from invertebrates up to humans.•Amyloidogenesis is a physiological process utilized to solve various necessity.•Amyloid fibrils have a key role in proteinopathies associated with ageing process.•Finding new therapies starting from studies on invertebrate amyloidogenesis.
ISSN:0047-6374
1872-6216
DOI:10.1016/j.mad.2022.111705