Jul 10, 2012 · WT and KO fibroblasts were exposed to stressors that induce hsp70 including heat shock, cadmium, and azetidine-2-carboxylic acid (AZE), as well as 2-deoxyglucose (2-DG), a stressor that does not routinely induce hsp70.

Hsp70 (encoded by three very closely related paralogs: HSPA1A, HSPA1B, and HSPA1L) is a stress-induced protein. High levels can be produced by cells in response to hyperthermia, oxidative stress, and changes in pH. Binding immunoglobulin protein (BiP or Grp78) is a protein localized to the endoplasmic reticulum. It is involved in protein ...

Mar 19, 2015 · Affinity chromatography provides evidence that Az binds HSP70 but not other types of heat shock proteins including HSP40, HSP60, and HSP90. We also demonstrate that Az induces cancer cell death via caspase-dependent apoptosis by disrupting the interaction of HSP70 with APAF-1.

Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short ...

Heat shock protein 70 (Hsp70) is a molecular chaperone that is expressed in response to stress.

Mar 19, 2015 · Affinity chromatography provides evidence that Az binds HSP70 but not other types of heat shock proteins including HSP40, HSP60, and HSP90. We also demonstrate that Az induces cancer cell death via caspase-dependent apoptosis by disrupting the interaction of HSP70 with APAF-1.

Heat shock proteins (HSPs) are induced in response to many injuries including stroke, neurodegenerative disease, epilepsy, and trauma. The overexpression of one HSP in particular, Hsp70, serves a protective role in several different models of ...

Feb 6, 1998 · Hsp70 chaperones, with their co-chaperones, comprise a set of abundant cellular machines that assist a large variety of protein folding processes in almost all cellular compartments.

We describe the de novo design of Hsp70 binding proteins that either inhibit or stimulate Hsp70 ATPase activity. An ATPase stimulating design promoted the refolding of denatured luciferase in vitro, similar to native JDPs.

Mar 19, 2015 · Our results show that Az induces caspase-dependent apoptosis by blocking the interaction of HSP70 with APAF-1, while not affecting the interaction of HSP70 with ASK1, JNK, BAX, and AIF. Animal model study exhibits that Az suppresses tumor growth in a …