Heat shock protein

Heat shock protein 90 (Hsp90) is a 90 kilo Dalton, ubiquitously expressed molecular chaperone that is required for plays a critical role in various biological processes including cellular survival, regulation of cell cycle, steroid and other signaling pathways. Although Hsp90 was initially discovered as a protein whose expression increases upon heat stress, it is one of the most abundant chaperone in the cytoplasm of the eukaryotic cells encompassing 1-2% of the total cellular protein under normal

At the start of the paper (Lancaster et al., 2004) the abstract is written well by stating their hypothesis, whether heat shock protein 72 (Hsp72) can be released during times of physical stress. This section also contains data collected from the results to give the reader a clear insight in to what to expect to find. It is my opinion, the abstract is a positive due to it enticing you in and explaining what the study will be about. Following on from the abstract the introduction goes in to extensive

Heat shock proteins are chaperone proteins with many functions. Some known functions of heat shock proteins are of assisting the folding of nonnative proteins, stabilizing cellular proteins under stressful conditions such as heat, and aiding in the degradation of proteins. Hsp90 is a particular heat shock protein with a specific role. Hsp90 not only assists proteins undergoing stress but it also helps unstressed cells with intracellular transport and cell signaling. It is a required protein for the

Proteins play a part in every cellular activity and must fold into proper three dimensional configurations, or native state, to execute their intended functions. Proteomic stressors such as chemical exposure or elevated temperature can inhibit protein folding upsetting protein homeostasis and resulting in cell death and human disease (Broadley 2009). Excessive protein misfolding can lead to amyloid fibrillar aggregates which deposit around brain neurons contributing to the development or progression

erythrocytes (Homer et al., 2000). The 70 kDa heat-shock proteins (HSP-70s) are intracellular proteins found in all organisms. HSPs play important roles in cell proliferation and the control of cellular functions (Lindquist, 1986). Heat shock proteins (HSPs) are known as stress proteins because various forms of stress enhance their transcriptional activation and biosynthesis (Lindquist, 1986). As many bacteria and parasites produce HSP-70, the protein serves as an antigen for bacteria and parasitic

Electro-encephalography : Electro-Encephalography (EEG) is primarily an electrophysiological monitoring method, recording the electrical activity of the brain. It involves placing electrodes along the scalp, which measure voltage fluctuations resulting from the ionic flux across the brain neurons. These are recorded graphically and typically referred to as ‘brain waves’. Prior to the advent of Computed Tomography (CTScan) and Magnetic Resonance Imaging (MRI), EEG

GRP170 is large protein that belong to the HSP70 superfamily of molecular chaperones that are located in the lumen of the endoplasmic reticulum, these class of proteins assist with properly folding polypeptides into proteins, these chaperones are also utilized in the Unfolded Protein response in the endoplasmic reticulum. Caenorhabditis elegans contain two paralogues of the GRP170 gene, GRP170a and GRP170a. The expressions of these two loci of the gene occur at different instances and are induced

response to heat-shock, yeast extracts up-regulate the HSP 30 gene by producing more proteins the same way bacteria cells up-regulate gene expression. In an environmental stress, such as heat shock, proteins inside a cell will degenerate. Once the protein is exposed to heat shock, the weak interactions that hold the proteins’ tertiary structure will degrade. Therefore, the cell must use the chaperone proteins to re-fold the degraded proteins. In order to create more chaperone proteins, the HSP 30

The HSP is a group of highly conserved proteins that are induced in both prokaryotes and eukaryotes by elevated temperatures or a variety of cellular stresses (Ross et al., 2003). When heat shocked to animal, the cells reduce their overall rates of gene transcription, RNA processing and translation, alter the activity of expressed proteins and, for a short period of time, increase expression of HSP. HSP are traditionally classified by their molecular weight and the best understood are in the 110

2011). This occurs through the remodeling of translating mRNAs into non-translating mRNPs which accumulate in cytoplasmic RNA- protein granules, known as P-bodies (mainly contain mRNA decay machinery) and stress granules (mainly contain translation initiation factors). (Buchan, Yoon, & Parker, 2011). Several studies reveal that both granules share specific mRNA and many protein components. Stress granules and P-bodies are likely to interact and exchange mRNP between them. In yeast, stress granules are