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Heat shock proteins are also believed to play a role in the presentation of pieces of proteins (or peptides) on the cell surface to help the immune system recognize diseased cells. [22] The major HSPs involved in the HSR include HSP70, HSP90, and HSP60. [5] Chaperones include the HSP70s and HSP90s while HSP60s are considered to be chaperonins. [17]
Simplified control circuit of human thermoregulation. [8]The core temperature of a human is regulated and stabilized primarily by the hypothalamus, a region of the brain linking the endocrine system to the nervous system, [9] and more specifically by the anterior hypothalamic nucleus and the adjacent preoptic area regions of the hypothalamus.
The permissive temperature is the temperature at which a temperature-sensitive mutant gene product takes on a normal, functional phenotype. [2] When a temperature-sensitive mutant is grown in a permissive condition, the mutant gene product behaves normally (meaning that the phenotype is not observed), even if there is a mutant allele present.
Heat shock proteins (HSPs) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock , [ 1 ] but are now known to also be expressed during other stresses including exposure to cold, [ 2 ] UV light [ 3 ] and during wound healing or tissue remodeling. [ 4 ]
Temperature also modulates the activity of the Na + /K +-ATPase [citation needed]. The Na + /K +-ATPase is a P-type pump that extrudes 3Na + ions in exchange for 2K + ions for each hydrolytic cleavage of ATP. This results in a net movement of positive charge out of the cell, i.e. a hyperpolarizing current. The magnitude of this current is ...
The human body always works to remain in homeostasis. One form of homeostasis is thermoregulation. Body temperature varies in every individual, but the average internal temperature is 37.0 °C (98.6 °F). [1] Sufficient stress from extreme external temperature may cause injury or death if it exceeds the ability of the body to thermoregulate.
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation, radiation, or heat. [3]
Early research has suggested that cells which are better able to synthesize stress proteins and do so at the appropriate time are better able to withstand damage caused by ischemia and reperfusion. [15] In addition, many stress proteins overlap with immune proteins. These similarities have medical applications in terms of studying the structure ...