Heat shock proteins (Hsps) are among the most widely distributed and evolutionary conserved proteins. Hsps are essential regulators of diverse constitutive metabolic processes and are markedly upregulated during stress. A 62 kDa Hsp (Hsp60) of Histoplasma capsulatum (Hc) is an immunodominant antigen and the major surface ligand to CR3 receptors on macrophages. However little is known about the ...

Heat shock proteins (HSPs) are known to play ecological and evolutionary roles in this postgenomic era. Recent research suggests that HSPs are implicated in cardiovascular biology and disease development, proliferation and regulation of cancer cells, cell death via apoptosis, and several other key cellular functions. These activities have generated great interest amongst cell and molecular biol...

The heat-shock response of Streptococcus pyogenes following exposure to elevated growth temperatures, and the immunological reactivity of heat-shock proteins (HSPs) in streptococcal infections were studied. Two major proteins of 65 and 75 kDa were expressed when a S. pyogenes strain was shifted from 37 degrees C to heat-shock temperatures of 40, 42 and 45 degrees C. Such proteins are members of...

Adult T cell leukemia is a fatal malignant transformation caused by the human T-cell lymphoptropic virus type I (HTLV-I). HTLV-I is only associated with the development of this disease in a small percentage of infected individuals. Using two rabbit transformed T-cell lines; RH/K30 (asymptomatic) and RH/K34 (leukemogenic), we have investigated the expression of heat shock proteins (HSP) 90 and 7...

skeletal muscle may develop adaptive chaperone and enhancementdefense system through daily exercisestimulation. the present study investigated resistance and exhaustion training alters the expression of chaperoneproteins. these proteins function to maintain homeostasis, facilitate repair from injury and provide protection. exercise-induced production of hsps in skeletal muscle and peripheral le...

Heat shock proteins (HSPs) are present in most cells, serving as molecular chaperones, and they play a role in cell protection from damage in response to stress stimuli. However, accumulating data indicate the involvement of HSPs in the pathogenesis of diseases. The aim of this article is to update the progress concerning the role of HSPs in atherosclerosis. It has been demonstrated that HSPs a...

Wagner, M., I. Hermanns, F. Bittinger, and C. J. Kirkpatrick. Induction of stress proteins in human endothelial cells by heavy metal ions and heat shock. Am. J. Physiol. 277 (Lung Cell. Mol. Physiol. 21): L1026–L1033, 1999.—In the present study, we compared the induction of heat shock proteins (HSPs) by heat and heavy metal ions in three different endothelial cell types, namely, human umbilical...

Heat-shock proteins (Hsps) are molecular chaperones that are ubiquitously expressed but are also induced in cells exposed to stressful stimuli. Hsps have been implicated in the induction and propagation of several diseases. This paper focuses on regulatory factors that control the transcription of the genes encoding Hsps. We also highlight how distinct transcription factors are able to interact...

Tobacco (Nicotiana tabacum L. cv Wisconsin 38) cells grown in suspension culture at 26 degrees C produce heat shock proteins (HSPs) when exposed to elevated temperature of 34 to 42 degrees C. At 34 and 38 degrees C, synthesis of normal proteins is maintained while HSPs are expressed within 30 minutes after initiation of the shock. At 42 degrees C, HSPs are still expressed but normal proteins ar...

Molecular chaperones are ubiquitous and abundant within cellular environments, functioning as a defense mechanism against outer environment. The range of molecular chaperones varies from 10 to over 100 kDa. Depending on the size, the specific locations and physiological roles of molecular chaperones vary within the cell. Multifunctionality of heat shock proteins (HSPs) expressed via various cyt...