ArticleInternational journal of biological macromolecules2020
Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies.
Article in International journal of biological macromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Heat shock proteins in hypothermia: a review.Frontiers in molecular biosciences · 2025Review
- The clinical significance of mitochondrial calcium uniporter in gastric cancer patients and its preliminary exploration of the impact on mitochondrial function and metabolism.Frontiers in oncology · 2024Article
- Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.Cell stress & chaperones · 2023Article
- Elevated circulating Hsp70 levels are correlative for malignancies in different mammalian species.Cell stress & chaperones · 2023Article
- Article
- Mitochondrial chaperones in human health and disease.Free radical biology & medicine · 2022Review
- The interaction of heat shock proteins with cellular membranes: a historical perspective.Cell stress & chaperones · 2021Review
- Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.Cell stress & chaperones · 2021Article
- Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain.Cell stress & chaperones · 2020Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.