Hypoxia and Inflammation as a Consequence of β-Fibril Accumulation: A Perspective View for New Potential Therapeutic Targets

Table 1

Common molecular features of amyloidosis.

Molecular features	Description and mechanisms	References
Misfolded proteins	Misfolding of β-sheet-rich proteins, such as amyloid β-protein tau, tau, α-synuclein, and prion protein (PrP^sc)	[1, 24]
Polymers/protofibrils	Formation of intra/extracellular polymers with antiparallel β-sheet-rich proteins or protofibrils	[69]
β-Fibrils at optical microscopy (OM)	β-Fibrils show green birefringence at polarized OM after red Congo staining	[2]
β-Fibrils at TEM	β-Fibrils are linear, 8-12 nm in diameter, and interact with EM extracellular matrix molecules	[1, 2, 12]
β-Fibril physicochemistry	Linear, rigid, nonbranching, and protease-resistant polymers, probably interacting with extracellular matrix proteins	[12, 70]
β-Fibril protein composition	β-Fibril proteins are heterogeneous in their origin and composition, depending on the cell type involved	[12]
β-Fibril passing in the blood	β-Fibrils associate with SAP (serum amyloid protein)	[1, 2]
Large aggregates and deposits of β-fibrils	Formations of aggregates and deposits of rigid, stable, and protease-resistant β-fibrils, containing 15% of SAP, localized in the extracellular space, mostly around the vessel	[71]