Members of the heat-shock protein (hsp) 70 family, distributed within various cellular compartments, have been implicated in facilitating protein maturation events. In particular, related hsp 70 family members appear to bind nascent polypeptides which are in the course of synthesis and/or translocation into organelles. We previously reported that in normal, unstressed cells, cytosolic hsp 70 (h...

Research into heat shock proteins (HSPs) for the clinical management of tumours has intensified as new evidence shows they can be used as biomarkers in carcinogenesis and are related to poor prognosis in some cancer types. Members of small HSP, HSP70 and HSP90 families have been studied extensively in breast cancer. This article reviews current understanding of the role of HSP and HSF-1 (Heat s...

While studying the quantitative relationship between hyperthermiainduced heat shock proteins (HSPs) and thermotolerance (TT), we ob served that heat induced a family of HSPs, particularly an HSP 70 family, that might be involved in the development of TT. When cells were heated for 10 min at 4S.S°C, they became thermotolerant to a second heat exposure at 45.5°C,with a thermotolerance ratio of ...

Leukemic cells appear to develop less thermotolerance and then to lose their thermotolerance more rapidly than do other tumor cell lines. The reason for this phenomenon is not known. After heat shock (or other environmental stresses), mammalian cells preferentially synthesize a set of proteins known as heat shock proteins (HSPs). HSP-28 and the various isoforms of HSP-70 have been suggested as ...

A conditioning treatment of 30 min at 42 degrees C or 43 degrees C, followed by a 4-h recovery period at 37 degrees C, induces thermotolerance state in the cytoskeleton of Reuber H35 hepatoma cells and N2A neuroblastoma cells. Evidence for the involvement of heat shock proteins in the development of thermotolerance in the cytoskeleton has been obtained from the following observations: only thos...

The 70 kDa heat shock family of molecular chaperones is essential to a variety of cellular processes, yet it is unclear how these proteins are regulated in vivo. We present evidence that the protein BAG-1 is a potential modulator of the molecular chaperones, Hsp70 and Hsc70. BAG-1 binds to the ATPase domain of Hsp70 and Hsc70, without requirement for their carboxy-terminal peptide-binding domai...

Knowledge of the physiological role of heat shock proteins is currently limited; however better understanding of their function and thereby the acquisition of the capacity to harness their power might lead to their use as therapeutic agents and revolutionize clinical practice in a number of areas. Future work is needed to translate the experimental data on the capacity of heat shock proteins to...

conclusions we have highlighted the role of rns3 plus rnt-gp96 mediated by α5integrin in producing il-12 and tnfα. it can be suggested that rnt-gp96 could enhance immunity characteristic of rns3 protein via production of pro-inflammatory cytokines. results our results showed that rnt-gp96 alone significantly increases the expression level of il-12, tnfα and α5integrin in thp-1 macrophages and d...

The spontaneous increase in the transcription of the heat shock protein (hsp 70) gene in peripheral blood mononuclear cells of patients with active systemic lupus erythematosus (SLE) is shown by nuclear run on transcription assay. The transcription of hsp 70 gene in the peripheral blood mononuclear cells of five patients with active SLE was more than 10 times greater than that in five normal he...