scholarly journals Death in the sauna-vitality markers for heat exposure

2021 ◽  
Author(s):  
Anja Wegner ◽  
Elke Doberentz ◽  
Burkhard Madea
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Case Reports ◽  
Heat Exposure ◽  
The Body ◽  
The Other ◽  
Aquaporin 3 ◽  
Family Home ◽  
Shock Proteins

AbstractIn sauna-associated deaths, the vitality of heat exposure is of great importance. Two case reports address this. First, we present the case of a 77-year-old man who was found dead in the sauna of his family home. When found, the sauna door was closed, and the sauna indicated a temperature of 78 °C. The body had already begun to decay and was partially mummified when it was found. In the other case, a 73-year-old woman was found dead in the sauna by her husband. In this case, the sauna door was also closed. The sauna was still in operation at a temperature of approximately 70 °C. Epidermal detachments were found. In both autopsies and their follow-up examinations, there were no indications of a cause of death competing with heat shock. The expression of heat shock proteins in kidneys and lungs and the expression of aquaporin 3 in skin were investigated to detect pre-mortal temperature influences.

Heat shock proteins and exercise: a primer

2008 ◽  
Vol 33 (5) ◽  
pp. 1050-1075 ◽  
Author(s):  
Earl G. Noble ◽  
Kevin J. Milne ◽  
C.W. James Melling
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ion Channel ◽  
The Other ◽  
Cellular Environment ◽  
Shock Proteins ◽  
Fertile Area ◽  
Area Of Study

Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this review is to introduce the reader to the major HSP families, the control of their expression, and some of their biologic functions, specifically with respect to the influence of exercise. Moreover, as the first in a series of reviews from a common symposium, we will briefly introduce the concepts presented by the other authors, which include the effects of different exercise paradigms on skeletal muscle HSPs in the adult and aged systems, HSPs as regulators of inflammation, and the ion channel stabilizing effects of HSPs.

Stress protein systems of mammalian cells

1986 ◽  
Vol 250 (1) ◽  
pp. C1-C17 ◽  
Author(s):  
J. R. Subjeck ◽  
T. T. Shyy
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Heat Exposure ◽  
Stress Protein ◽  
Protective Role ◽  
Living Organisms ◽  
Shock Proteins ◽  
Glucose Regulated Proteins

Living organisms are known to react to a heat stress by the selective induction in the synthesis of several polypeptides. In this review we list the major stress proteins of mammalian cells that are induced by heat shock and other environments and categorize these proteins into specific subgroups: the major heat shock proteins, the glucose-regulated proteins, and the low-molecular-weight heat shock proteins. Characteristics of the localization and expression of proteins in each of these subgroups are presented. Specifically, the nuclear/nucleolar locale of certain of the major heat shock proteins is considered with respect to their association with RNA and the recovery of cells after a heat exposure. The induction of these major heat shock proteins and the repression of the glucose-regulated proteins as a result of reoxygenation of anoxic cells or by the addition of glucose to glucose-deprived cultures is described. Changes in the expression of these protein systems during embryogenesis and differentiation in mammalian and nonmammalian systems is summarized, and the protective role that some of these proteins appear to play in protecting the animal against the lethal effects of a severe heat treatment and against teratogenesis is critically examined.

scholarly journals The Role of Heat Shock Proteins in Type 1 Diabetes

2021 ◽  
Vol 11 ◽  
Author(s):  
Abu Saleh Md Moin ◽  
Manjula Nandakumar ◽  
Abdoulaye Diane ◽  
Mohammed Dehbi ◽  
Alexandra E. Butler
Keyword(s):  
Type 1 Diabetes ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Clinical Laboratory ◽  
Tyrosine Phosphatase ◽  
The Body ◽  
Acid Decarboxylase ◽  
Β Cells ◽  
Shock Proteins

Type 1 diabetes (T1D) is a T-cell mediated autoimmune disease characterized by recognition of pancreatic β-cell proteins as self-antigens, called autoantigens (AAgs), followed by loss of pancreatic β-cells. (Pre-)proinsulin ([P]PI), glutamic acid decarboxylase (GAD), tyrosine phosphatase IA-2, and the zinc transporter ZnT8 are key molecules in T1D pathogenesis and are recognized by autoantibodies detected in routine clinical laboratory assays. However, generation of new autoantigens (neoantigens) from β-cells has also been reported, against which the autoreactive T cells show activity. Heat shock proteins (HSPs) were originally described as “cellular stress responders” for their role as chaperones that regulate the conformation and function of a large number of cellular proteins to protect the body from stress. HSPs participate in key cellular functions under both physiological and stressful conditions, including suppression of protein aggregation, assisting folding and stability of nascent and damaged proteins, translocation of proteins into cellular compartments and targeting irreversibly damaged proteins for degradation. Low HSP expression impacts many pathological conditions associated with diabetes and could play a role in diabetic complications. HSPs have beneficial effects in preventing insulin resistance and hyperglycemia in type 2 diabetes (T2D). HSPs are, however, additionally involved in antigen presentation, presenting immunogenic peptides to class I and class II major histocompatibility molecules; thus, an opportunity exists for HSPs to be employed as modulators of immunologic responses in T1D and other autoimmune disorders. In this review, we discuss the multifaceted roles of HSPs in the pathogenesis of T1D and in autoantigen-specific immune protection against T1D development.

scholarly journals Short Review on Types of Heat Shock Proteins and Their Fundamental Characters for Body Maintenance Together With Role in Cancer

2020 ◽  
pp. 103-108
Author(s):  
Muhammad Muneeb ◽  
Moazam Ali ◽  
Tahir Sarfaraz ◽  
Wajid Ali ◽  
Zeeshan Ahmad Bhutta
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Significant Role ◽  
Cancer Diagnosis ◽  
Short Review ◽  
The Body ◽  
Normal Functions ◽  
Wide Range ◽  
Shock Proteins

Body of living thing is a complex machine that works on multifunctional processes and needs maintenance. Heat shock protein is a specific type of protein that cares about many normal functions of the body. These proteins have many dynamic occupations to shield the body from various diseases and also a key role in the coiling and uncoiling of proteins, prevent from apoptosis and transportation of proteins. Along with these all properties, the foremost function of these proteins is prevention from cancer and a significant role in cancer diagnosis. Commonly heat shock protein known as chaperones and a wide range of their types have been discovered with their functions as well. Recently many scientists are working on additional investigation of heat shock proteins. This review concludes some basic types of heat shock proteins and their elegant purposes and also providing an open eye for new scientist about a further investigation of heat shock protein.

The Role of Heat Shock Proteins in the Mechanisms of Neurodegeneration and Neuroprotection in Primary Glaucoma: Literature Review

2021 ◽  
pp. 122-131
Author(s):  
N. S. Lutsenko ◽  
T. V. Nedilka
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Neurodegenerative Diseases ◽  
Retinal Ganglion Cells ◽  
Defense Mechanism ◽  
Ganglion Cells ◽  
The Body ◽  
Retinal Ganglion ◽  
Shock Proteins

Heat shock proteins (HSP) are important components of the defense mechanism that increases the survival of body cells in adverse conditions due to antiapoptotic and cytoprotective effects. Since their discovery, numerous studies and experimental models have proved the role of HSPs as a key link in the processes of both repair and coagulation of proteins, as well as in the protection of cells from oxidative stress. The potential for pharmacological induction of HSPs in the human body makes them an attractive therapeutic target for many neurodegenerative diseases. This review examines the role of HSPs, especially fraction 70, in the mechanisms of neuroprotection of retinal ganglion cells in primary open-angle glaucoma being one of the common neurodegenerative diseases that can lead to complete loss of visual functions. A number of studies have shown the protective effect of HSP70 on retinal ganglion cells in animals with artificially induced glaucoma. But in the course of experiments on animal models, it was also proved that direct immunization with HSP through intravitreal injections induced pressure-independent degeneration of retinal ganglion cells. This indicates the need for indirect stimulation of HSP70 in order to activate their neuroprotective properties. To date, there are insufficient data on the circulation of HSP70 in the body of a person with glaucoma. These data indicate the prospects for further study of the role of HSP70 in glaucoma degeneration and elucidation of the ways of their mediated induction. Keywords: heat shock protein, HSP70, glaucoma, ganglion cells, retina, neuroprotection.

scholarly journals Response to thermal and infection stresses in an American vector of visceral leishmaniasis

2020 ◽  
Author(s):  
Kelsilandia A. Martins ◽  
Caroline S. Morais ◽  
Susan J. Broughton ◽  
Claudio R. Lazzari ◽  
Paul A. Bates ◽  
...  
Keyword(s):  
Heat Shock ◽  
Body Temperature ◽  
Visceral Leishmaniasis ◽  
Heat Shock Proteins ◽  
Blood Meal ◽  
Blood Feeding ◽  
The Body ◽  
Sand Fly ◽  
Sand Flies ◽  
Shock Proteins

AbstractThe phlebotomine sand fly Lutzomyia longipalpis is the primary insect vector of visceral leishmaniasis in the Americas. For ectothermic organisms such as sand flies, the ambient temperature is a critical factor influencing all aspects of their life. However, the impact of temperature has been ignored in previous investigations of stress-induced responses by the vector, such as taking a blood meal or during Leishmania infection. Therefore, this study explored the interaction of Lu. longipalpis with temperature by evaluating sand fly behaviour across a thermal gradient after sugar or blood-feeding, and infection with Leishmania mexicana. Thermographic recordings of sand fly females fed on mice were analysed, and the gene expression of heat shock proteins HSP70 and HSP90(83) was evaluated when insects were exposed to extreme temperatures or infected. The results showed that 72h after blood ingestion females of Lu. longipalpis became less active and preferred relatively low temperatures. However, at later stages of blood digestion females increased their activity and remained at higher temperatures prior to taking a second blood meal; this behaviour seems to be correlated with the evolution of their oocysts and voracity for a second blood meal. No changes in the temperature preferences of female sand flies were recorded in the presence of a gut infection by Le. mexicana, indicating that this parasite has not triggered behavioural immunity in Lu. longipalpis. Real-time imaging showed that the body temperature of female flies feeding on mice increased to the same temperature as the host within a few seconds after landing. The body temperature of females remained around 35 ± 0.5 °C until the end of blood-feeding, revealing a lack of thermoregulatory behaviour. Analysis of expression of heat shock proteins revealed insects increased expression of HSP90(83) when exposed to higher temperatures, such as during blood feeding. Our findings suggest that Lu. longipalpis interacts with the environmental temperature by using its behaviour to avoid temperature-related physiological damage during the gonotrophic cycle. However, the expression of certain heat shock proteins might be triggered to mitigate against thermal stress in situations where a behavioural response is not the best option.

Constitutive and Induced Synthesis of Heat Shock Proteins in Transplantable Hepatomas

1987 ◽  
Vol 73 (6) ◽  
pp. 559-565 ◽  
Author(s):  
Luisa Schiaffonati ◽  
Lidia Bardella ◽  
Gaetano Cairo ◽  
Emilia Rappocciolo ◽  
Lorenza Tacchini ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Rat Liver ◽  
Growth Rates ◽  
The Other ◽  
Constitutive Synthesis ◽  
Shock Proteins ◽  
Slow Growing

The synthesis of heat shock proteins (HSP) was studied in rat liver and in a series of transplantable Morris hepatomas with different growth rates, subjected to heat shock in vivo and in vitro. Different from the liver, hepatomas synthesized HSP constitutively, i.e., also before exposure to heat. This constitutive synthesis was low and limited to one HSP in the slowest-growing tumor, more marked and involving other HSP in the intermediate- and fast-growing hepatomas. In tumor that synthesized HSP constitutively, the induction of HSP in response to heat was proportionately reduced. These patterns of reaction were essentially similar in vivo ad in vitro. The amount of HSP 68 was well correlated to the levels of its mRNA in liver and in all hepatomas, whereas the increase in HSP 89 was accompanied by a corresponding increase in the related mRNA in liver and in slow-growing hepatoma, not in the other tumors, thus suggesting a different mechanism of control of HSP 89 synthesis in the more malignant hepatomas.

Periodic segmental anomalies induced by heat shock in the chick embryo are associated with the cell cycle

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 119-130 ◽  
Author(s):  
D.R. Primmett ◽  
W.E. Norris ◽  
G.J. Carlson ◽  
R.J. Keynes ◽  
C.D. Stern
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Heat Shock ◽  
Simple Model ◽  
Chick Embryo ◽  
Heat Shock Proteins ◽  
Cell Division Cycle ◽  
The Other ◽  
Chick Embryos ◽  
Shock Proteins

This study provides evidence that cells destined to segment together into somites have a degree of cell division synchrony. We have measured the duration of the cell division cycle in somite and segmental plate cells of the chick embryo as 9.5 h using [3H]thymidine pulse- and-chase. Treatment of embryos with any of a variety of inhibitors known to affect the cell division cycle causes discrete periodic segmental anomalies: these anomalies appear about 6–7 somites after treatment and, in some cases, a second anomaly is observed 6 to 7 somites after the first. Since somites take 1.5 h to form, the 6- to 7- somite interval corresponds to about 9–10 h, which is the duration of the cell cycle as determined in these experiments. The anomalies are similar to those seen after heat shock of 2-day chick embryos. Heat shock and some of the other treatments induce the expression of heat-shock proteins (hsp); however, since neither the expression nor the distribution of these proteins relate to the presence or distribution of anomalies seen, we conclude that hsps are not responsible for the pattern of segmental anomalies observed. The production of periodic segmental anomalies appears to be linked to the cell cycle. A simple model is proposed, in which we suggest that the cell division cycle is involved directly in gating cells that will segment together.

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