The human HSP70 gene was modified in vitro using oligonucleotide-directed mutagenesis to add sequences encoding a peptide from the testis-specific form of human lactate dehydrogenase (LDH) to the carboxy terminus of HSP70. The peptide-tagged HSP70 can be distinguished from the endogenous HSP70 protein using an LDH peptide-specific antiserum in indirect immunofluorescence assays of cells transie...

We have studied the expression of the major heat shock protein HSP70 during maturation of avian erythroid cells. Primitive and definitive erythroid cells were isolated from staged day 3-8 chicken embryos, and the levels of HSP70 mRNA and protein synthesis were examined. The highest levels of HSP70 are detected in polychromatic cells of the day 3-4 primitive erythroid cell. After the initial bur...

Exposure of pulmonary artery endothelial cells (PAECs) to hyperoxia results in a compromise in endothelial monolayer integrity, an increase in caspase-3 activity, and nuclear translocation of apoptosis-inducing factor (AIF), a marker of caspase-independent apoptosis. In an endeavor to identify proteins involved in hyperoxic endothelial injury, we found that the protein expression of heat-shock ...

BACKGROUND Heat shock protein 70 (Hsp70) was identified as a cellular interaction partner of the influenza virus ribonucleoprotein (RNP) complex. The biological significance of the interaction between Hsp70 and RNP has not been fully investigated. PRINCIPAL FINDINGS Here we demonstrated that Hsp70 was involved in the regulation of influenza A viral transcription and replication. It was found ...

In contrast to normal cells, tumor cells of multiple entities overexpress the Heat shock protein 70 (Hsp70) not only in cytosol, but also present it on their plasma membrane a tumor-specific manner. Furthermore, Hsp70-positive actively release Hsp70 small extracellular vesicles with biophysical characteristics exosomes. Due conformational changes lipid environment, most commercially available a...

The major inducible 70-kDa heat shock protein (hsp70) protects against measles virus (MeV) neurovirulence in the mouse that is caused by a cell-associated noncytolytic neuronal infection. Protection is type I interferon (IFN) dependent, and we have established a novel axis of antiviral immunity in which hsp70 is released from virus-infected neurons to induce IFN-β in macrophages. The present wo...