Structural and Biochemical Properties of Hsp40/Hsp70 Chaperone System

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates

“…It is evident that SBD binds to exposed segments of five to seven amino acids, mostly composed of hydrophobic residues and flanked by positively charged residues. 7,32 Promiscuity of the SBD domain substrate recruitment, enabled by the limited specificity of the binding site, allows for the interaction of a wide variety of polypeptides, which are not significantly homologous on the sequence level. 4 Thus, it is evident that the interactions are not fully dependent on the substrate's unique linear amino acid sequence.…”

“…4,5 Chaperones play a vital part in every step of cellular metabolism including protein synthesis, folding, translocation, and rearrangements such as assembly and disassembly into complex organizations, and ultimately in protein degradation and apoptosis. 4,5,7 Impact statement Protein homeostasis is the cellular protein quality control machinery that maintains structural integrity of the cellular proteome. Genetic level mutations, errors occur at the transcriptional and translational levels, and conditions that contribute to cellular stress cause protein misfolding which ultimately leads to toxic protein aggregates resulting in wide range of diseases including Parkinson's disease, Alzheimer's disease, Huntington's disease, Creutzfeldt-Jakob disease, and type 2 diabetes.…”

“…4,28 The network of co-chaperones that interact with Hsp70 can be divided into two main categories, termed J-domain protein co-chaperones (JDP) and nucleotide exchange factors (NEF), based on how they interact with Hsp70. 7 In this review, we will explore Hsp70 (HSPA) co-chaperones based on the co-chaperone function and the Hsp70 domains that mediate the Hsp70co-chaperone interactions.…”

The Concentration of Hsp70 in the Cytosol and Mitochondria of the Brain in Animals With Experimental Autoimmune Encephalo- Myelitis and After the Time Course of Intranasally Administered N-Phenylacetyl-L-Prolylglycine Ethyl Ester (Noopept)

“…In addition, one of the main functions of HSP 70 is the induction, as well as the extension of the lifespan of the stable form of HIF-1α, which launches subsequent adaptive responses in the cell. It has been established that HSP 70 "prolongs" the action of HIF-1α, and also independently maintains the expression of NAD-MDH-mx, thereby maintaining the activity of the compensatory mechanism of ATP productionthe malate-aspartate shuttle mechanism for a long time [4,5,6].The most widely accepted animal model of MS is experimental autoimmune encephalomyelitis (EAE) that has clinical manifestations and pathophysiological mechanisms similar to MS [7,8, 9,10].The purpose of the study was to investigate the specific activity of a nasal dosage form with ethyl ester of n-phenylacetyl-l-prolylglycine on the expression of HSP 70 in the rat brain.Materials and methods. The experiments were carried out on 100 white outbred rats weighing 190-220 g, collected from the breeding center of institute of pharmacology and toxicology of the academy of medical sciences of ukraine.…”

“…In addition, one of the main functions of HSP 70 is the induction, as well as the extension of the lifespan of the stable form of HIF-1α, which launches subsequent adaptive responses in the cell. It has been established that HSP 70 "prolongs" the action of HIF-1α, and also independently maintains the expression of NAD-MDH-mx, thereby maintaining the activity of the compensatory mechanism of ATP productionthe malate-aspartate shuttle mechanism for a long time [4,5,6].…”