Journal article

Physicochemical properties that control protein aggregation also determine whether a protein is retained or released from necrotic cells.

Andre L Samson, Bosco Ho, Amanda E Au, Simone M Schoenwaelder, Mark J Smyth, Stephen P Bottomley, Oded Kleifeld, Robert L Medcalf

Open Biology | Published : 2016

Abstract

Amyloidogenic protein aggregation impairs cell function and is a hallmark of many chronic degenerative disorders. Protein aggregation is also a major event during acute injury; however, unlike amyloidogenesis, the process of injury-induced protein aggregation remains largely undefined. To provide this insight, we profiled the insoluble proteome of several cell types after acute injury. These experiments show that the disulfide-driven process of nucleocytoplasmic coagulation (NCC) is the main form of injury-induced protein aggregation. NCC is mechanistically distinct from amyloidogenesis, but still broadly impairs cell function by promoting the aggregation of hundreds of abundant and essentia..

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University of Melbourne Researchers