Kiraly, Vanessa T. R.
Dores-Silva, Paulo R.
Serrao, Vitor H. B.
Cauvi, David M.
De Maio, Antonio
[2, 4, 5]
Borges, Julio C.
Total Authors: 6
 Univ Sao Paulo, Sao Carlos Inst Chem, Sao Carlos, SP - Brazil
 Univ Calif, Sch Med, Dept Surg, La Jolla, CA - USA
 Univ Toronto, Dept Lab Med & Pathobiol, Toronto, ON - Canada
 Univ Calif San Diego, Ctr Invest Hlth & Educ Dispar, La Jolla, CA 92093 - USA
 Univ Calif, Sch Med, Dept Neurosci, La Jolla, CA - USA
Total Affiliations: 5
International Journal of Biological Macromolecules;
MAR 1 2020.
Web of Science Citations:
The Hsp70 family of heat shock proteins plays a critical function in maintaining cellular homeostasis within various subcellular compartments. The human mitochondrial Hsp70 (HSPA9) has been associated with cellular death, senescence, cancer and neurodegenerative diseases, which is the rational for the name mortalin. It is well documented that mortalin, such as other Hsp70s, is prone to self-aggregation, which is related to mitochondria biogenesis failure. Here, we investigated the assembly, structure and function of thermic aggregates/oligomers of recombinant human mortalin and Hsp70-1A (HSPA1A). Summarily, both Hsp70 thermic aggregates have characteristics of supramolecular assemblies. They display characteristic organized structures and partial ATPase activity, despite their nanometric size. Indeed, we observed that the interaction of these aggregates/oligomers with liposomes is similar to monomeric Hsp70s and, finally, they were non-toxic over neuroblastoma cells. These findings revealed that high molecular mass oligomers of mortalin and Hsp70-1A preserved some of the fundamental functions of these proteins. (C) 2019 Elsevier B.V. All rights reserved. (AU)