scholarly journals Soft ticks perform evaporative cooling during blood-feeding

2020 ◽  
Author(s):  
Claudio R. Lazzari ◽  
Aurélie Fauquet ◽  
Chloé Lahondère ◽  
Ricardo N. Araújo ◽  
Marcos H. Pereira
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tick Species ◽  
Adaptive Strategies ◽  
Blood Feeding ◽  
The Body ◽  
Blood Sucking ◽  
Shock Proteins ◽  
Cuticular Surface

AbstractFeeding on the blood of warm-blooded vertebrates is associated to thermal stress in haematophagous arthropods. It has been demonstrated that blood-sucking insects protect their physiological integrity either by synthesising heat-shock proteins or by means of thermoregulatory mechanisms. In this work, we describe the first thermoregulatory mechanism in a tick species, Ornithodoros rostratus. By performing real-time infrared thermography during feeding on mice we found that this acarian eliminates big amounts of fluid (urine) through their coxal glands; this fluid quickly spreads over the cuticular surface and its evaporation cools-down the body of the tick. The spread of the fluid is possible thanks to capillary diffusion through the sculptured exoskeleton of Ornithodoros. We discuss our findings in the frame of the adaptive strategies to cope with the thermal stress experienced by blood-sucking arthropods at each feeding event warm-blooded hosts.

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.

scholarly journals Expression pattern of heat shock proteins during acute thermal stress in the Antarctic sea urchin, Sterechinus neumayeri

2016 ◽  
Vol 89 (1) ◽  
Author(s):  
Karina González ◽  
Juan Gaitán-Espitia ◽  
Alejandro Font ◽  
César A. Cárdenas ◽  
Marcelo González-Aravena
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Expression Pattern ◽  
Sea Urchin ◽  
Sterechinus Neumayeri ◽  
Shock Proteins ◽  
The Antarctic

scholarly journals Influence of Heating and Cyclic Tension on the Induction of Heat Shock Proteins and Bone-Related Proteins by MC3T3-E1 Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-16 ◽  
Author(s):  
Eunna Chung ◽  
Alana Cherrell Sampson ◽  
Marissa Nichole Rylander
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tensile Stress ◽  
Bone Cells ◽  
Cyclic Strain ◽  
Fold Increase ◽  
Shock Proteins ◽  
Related Proteins ◽  
The Impact

Stress conditioning (e.g., thermal, shear, and tensile stress) of bone cells has been shown to enhance healing. However, prior studies have not investigated whether combined stress could synergistically promote bone regeneration. This study explored the impact of combined thermal and tensile stress on the induction of heat shock proteins (HSPs) and bone-related proteins by a murine preosteoblast cell line (MC3T3-E1). Cells were exposed to thermal stress using a water bath (44°C for 4 or 8 minutes) with postheating incubation (37°C for 4 hours) followed by exposure to cyclic strain (equibiaxial 3%, 0.2 Hz, cycle of 10-second tensile stress followed by 10-second rest). Combined thermal stress and tensile stress induced mRNA expression of HSP27 (1.41 relative fold induction (RFI) compared to sham-treated control), HSP70 (5.55 RFI), and osteopontin (1.44 RFI) but suppressed matrix metalloproteinase-9 (0.6 RFI) compared to the control. Combined thermal and tensile stress increased vascular endothelial growth factor (VEGF) secretion into the culture supernatant (1.54-fold increase compared to the control). Therefore, combined thermal and mechanical stress preconditioning can enhance HSP induction and influence protein expression important for bone tissue healing.

scholarly journals Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe

2015 ◽  
Vol 21 (2) ◽  
pp. 327-338 ◽  
Author(s):  
Attila Glatz ◽  
Ana-Maria Pilbat ◽  
Gergely L. Németh ◽  
Katalin Vince-Kontár ◽  
Katalin Jósvay ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Schizosaccharomyces Pombe ◽  
Stress Management ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

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.

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