Coaxum SD, Griffin TM, Martin JL, Mestril R. Influence of PKCoverexpression on HSP70 and cardioprotection. Am J Physiol Heart Circ Physiol 292: H2220–H2226, 2007. First published January 5, 2007; doi:10.1152/ajpheart.01080.2006.—Recent research has indicated that the protein kinase C (PKC) isoforms and the heat shock proteins (HSPs) are involved in cardioprotection. We have investigated the pos...

This study examined very brief focal ischemia that simulates transient ischemic attacks (TIAs) that occur in humans. Adult rats were subjected to sham operations or 5 min, 10 min, or 2 h of middle cerebral artery (MCA) ischemia using the suture (thread) model. Hsp70 protein was induced 24 h, 48 h and 72 h later in neurons throughout the entire MCA territory in many but not all animals. Followin...

Expression of heat shock proteins (hsps) results in the protection of cells from subsequent stresses. However, hsps are also toxic when present within cells for a prolonged time period. Thus, the expression of hsps should be tightly regulated. In the present study, the expression of Hsp70 after heat shock was compared between thermotolerant cells, which contain a large concentration of Hsp70, a...

Tumor immunotherapy has exploited the ability of heat shock proteins to chaperone precursors of antigenic peptides to antigen-presenting cells and to activate efficiently an immune response against tumor-associated antigens. The most common strategy is based on the purification of heat shock protein-peptide complexes from tumor cell lines or from tumor surgical samples for in vivo administratio...

Pancreatic carcinoma is a malignant disease that responds poorly to chemotherapy because of its resistance to apoptosis. Heat shock proteins (Hsp) are not only cytoprotective but also interfere with the apoptotic cascade. Here, we investigated the role of Hsp70 in regulating apoptosis in pancreatic cancer cells. Hsp70 expression was increased in pancreatic cancer cells compared with normal panc...

Hsp70 molecular chaperones function in protein folding in a manner dependent on regulation by co-chaperones. Hsp40s increase the low intrinsic ATPase activity of Hsp70, and nucleotide exchange factors (NEFs) remove ADP after ATP hydrolysis, enabling a new Hsp70 interaction cycle with non-native protein substrate. Here, we show that members of the Hsp70-related Hsp110 family cooperate with Hsp70...

Heat shock stress induces some heat shock proteins, including Hsp70, and activates sodium-dependent glucose transport in porcine renal LLC-PK(1) cells, but its mechanisms have not been described in detail. We investigated whether sodium-dependent glucose transporter (SGLT1) interacts with Hsp70 to increase SGLT1 activity. Heat shock stress increased SGLT1 activity without changing SGLT1 express...

Insufficient stress response and elevated oxidative can contribute to skeletal muscle atrophy during mechanical unloading (e.g., spaceflight bedrest). Perturbations in heat shock proteins HSP70), antioxidant enzymes, sarcolemmal neuronal nitric oxidase synthase (nNOS) have been linked unloading-induced atrophy. We recently discovered that the NADPH oxidase-2 complex (Nox2) is unloading, downstr...