Transfection of Heat Shock Protein 70 kDa (HSP70)

Abstract

Heat shock protein 70 kDa (HSP70) is a major protein family in the cell protections against stress-induced denaturation and aggregation and in the folding of nascent proteins. It is a highly conserved protein that can be found in most organisms and is strongly connected to several intracellular pathways such as protein folding and refolding, protein degradation and regulation, and protection against intense stress. Cellular delivery of HSP70 would be of high impact for clarification of its role in these cellular processes.PepFect14 is a cell-penetrating peptide known to be able to mediate the transfection of various oligonucleotides to multiple cell lines with a higher efficacy than most commercially available transfection agents and without inducing significant toxic effects.In this study we demonstrated that PepFect14 was able to form a complex with HSP70 and to deliver it inside cells in the same fashion with oligonucleotide delivery. The delivered HSP70 showed an effect in the cell regulation indicating that the protein was biologically available in the cytoplasm and the interactions with PepFect14 did not impeach its active sites once the plasma barrier crossed.This study reports the first successful delivery of HSP70 to our knowledge and the first protein transfection mediated by PepFect14. It opens new fields of research for both PepFect14 as a delivery agent and HSP70 as a therapeutic agent; with potential in peptide aggregation caused diseases such as Parkinson’s and Alzheimer’s diseases.

Hsp70 Gene Family in Sebastiscus marmoratus: The Genome-Wide Identification and Transcriptome Analysis under Thermal Stress

“…The number of damaged proteins increased under low-temperature stress (13 °C). The production of hsp70 gradually increased, presumably reflecting the need for more Hsp70 protein, which promoted the renaturation of abnormal proteins [ 1 ]. The hyou1 and hspa5 proteins have a signal peptide and a transmembrane domain and are found in the endoplasmic reticulum as secreted proteins.…”

“…As a highly conserved protein, heat shock protein 70 kDa (Hsp70) could protect features in response to intense cellular stress by assisting in their refolding and stabilization [ 1 , 2 ]. By correcting protein folding, Hsps could minimize the aggregation of unnatural proteins and denatured proteins, which have a significant influence on resistance to adverse environmental stresses as a group of molecular chaperones [ 3 , 4 , 5 , 6 ].…”