Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation

• Published in: Biochemistry (Easton) Vol. 53; no. 51; pp. 8001 - 8004
• Main Authors: Dubey, Kriti, Anand, Bibin G, Temgire, Mayur K, Kar, Karunakar
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 30.12.2014
• Subjects: Amino Acid Sequence; Amyloid - biosynthesis; Amyloid - chemistry; Amyloid - ultrastructure; Amyloidosis - etiology; Amyloidosis - metabolism; Animals; Cattle; Circular Dichroism; Cytochromes c - chemistry; Cytochromes c - genetics; Cytochromes c - metabolism; Humans; Insulin - chemistry; Insulin - genetics; Insulin - metabolism; Kinetics; Microscopy, Electron, Transmission; Molecular Sequence Data; Muramidase - chemistry; Muramidase - genetics; Muramidase - metabolism; Protein Aggregates; Protein Aggregation, Pathological - metabolism; Sequence Homology, Amino Acid; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - genetics; Serum Albumin, Bovine - metabolism; Spectrometry, Fluorescence
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi501333q

The question of how an aggregating protein can influence aggregation of other proteins located in its vicinity is particularly significant because many proteins coexist in cells. We demonstrate in vitro coaggregation and cross-seeding of lysozyme, bovine serum albumin, insulin, and cytochrome c during their amyloid formation. The coaggregation process seems to be more dependent on the temperature-induced intermediate species of these proteins and less dependent on their sequence identities. Because amyloid-linked inclusions and plaques are recognized as multicomponent entities originating from aggregation of the associated protein, these findings may add new insights into the mechanistic understanding of amyloid-related pathologies.