Synthesis of heat shock proteins (HSP70) in blood leukocytes as a criterion of the resistance to stress injury

Pshennikova, M. G.; Zelenina, O. M.; Kruglov, S. V.; Pokidyshev, D. A.; Shimkovich, M. V.; Malyshev, I. Yu.

doi:10.1007/s10517-006-0444-1

Cited by 5 publications

(3 citation statements)

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“…Furthermore, the recovery of heart function upon reperfusion occurred faster in geneti cally modified mice. The more resistant rats are to acute myocardial infarction, the higher the accumula tion of HSP in their heart muscles [18]. Moreover, the concentration of HSP70 in blood plasma is increased more than 20 fold in disseminated intravascular coag ulation (DIC) and thromboses, which is largely due to the release of protein from decaying cells [7][8][9]29].…”

Section: The Role Of Heat Shock Proteins In the Development Of Atheromentioning

confidence: 99%

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Heat shock proteins: Changes related to aging, development of thrombotic complications, and peptide regulation of the genome

2012

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Heat shock proteins (HSPs), which have been shown by A. Tissieres et al. [78] to be strongly induced by elevated temperatures, have recently attracted spe cial attention from researchers. In addition to temper ature elevation, the biosynthesis of HSPs is induced by other factors: toxins, anoxia, hypoxia, ischemia, che motherapeutic agents, carcinogens, and even con comitantly the differentiation and development of cells and tissues. Intensive HSP synthesis occurs in infectious diseases, inflammation, fever, ultraviolet irradiation, exposure to electromagnetic fields and heavy metal salts, alkalosis and acidosis, exposure to lipopolysaccharides, ischemia, hypoxia, cytokine attack, and exposure to animal and plant toxins. Con sequently, these proteins are also called stress proteins [79]. HSPs are found both inside the cell and on the cell membrane [13,27].According to the universally accepted classification, all HSPs are subdivided into six families depending on their molecular mass in kilodaltons. Heat shock pro teins with molecular mass lower than 40 kDa are included into the small HSP (sHSP) family. Other HSP proteins belong to families called HSP70, HSP80, HSP90, HSP100, and HSP with molecular masses of 1 A review of published data and the authors' own results. 110 kDa and above. HSPs with molecular masses of 70 kDa are of special interest due to the high levels of these proteins in tissues under stressful conditions. These proteins have been studied in the greatest detail and their role in the functioning of organs and tissues has been established. HSP70 was shown to be the main molecular chaperone involved in the utilization of irre versibly damaged proteins, or folding [40,43,44].What do chaperone (chaperone is a French word for an elderly lady accompanying a young girl to the ball) functions include? Newly synthesized proteins are known to have tertiary and quaternary structure. High temperature and stress to which the cell is exposed cause the formation of anomalous proteins due to aggregation. The functions of HSP in the regu lation of correct folding (structure formation) of newly synthesized proteins and the destruction of anomalous protein aggregates are called chaperone functions, and the proteins themselves are called chaperones. There fore, the main function of HSPs is the protection of the cell from damaging factors. Furthermore, HSPs are nonspecific adaptogens that protect the cells from various stressors.In addition to HSP70, the chaperone group includes HSP22, HSP27, HSP60, and HSP90. The propensity for chaperoning is determined by the struc ture of the chaperone proteins, which are able to Abstract-The present review of published data and the authors' own results addresses the role of heat shock proteins in the regulation of cell and tissue homeostasis and considers the decrease in their expression levels as one of the main factors of aging. Heat shock proteins are involved in the regulation of proliferation, apop tosis, and differentiation of cells, as well as in that of intracellular homeos...

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Section: The Role Of Heat Shock Proteins In the Development Of Atheromentioning

confidence: 99%

“…In the case of the significant activation of stress limiting systems, i.e., HSP70 in the leukocytes and NO in blood plasma, the defensive reaction to stres sors is more pronounced [18].…”

Section: The Role Of Heat Shock Proteins In the Development Of Atheromentioning

confidence: 99%

Heat shock proteins: Changes related to aging, development of thrombotic complications, and peptide regulation of the genome

2012

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“…This family is expressed under most physiological conditions, although expression is tightly regulated by heat shock factors (HSF) (Pockley 2003). Heat shock proteins are present in the circulation of rats (Fleshner et al 2004), humans (Campisi et al 2003;Lancaster and Febbraio 2005;Pshennikova et al 2006;Ruell et al 2007) and cattle (Kristensen et al 2004). The presence of HSPs in circulation is yet to be fully understood, but it appears they play a role in the innate immune system and inflammation (Terry et al 2006) and are released intra-and extracellularly in response to stress (Hightower and Guidon 1989).…”

Section: Introductionmentioning

confidence: 99%

Dietary betaine supplementation has energy-sparing effects in feedlot cattle during summer, particularly in those without access to shade

DiGiacomo¹,

Warner

Leury³

et al. 2014

Anim. Prod. Sci.

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Abstract. Dietary betaine supplementation improves water retention in steers and may influence lean-tissue deposition, while also acting as an osmolyte to help regulate cellular osmotic balance. This study investigated the interactions between shade and dietary betaine on carcass characteristics, tissue enzyme activity and gene expression in 48 feedlot steers during summer. Steers were randomly allocated to a 4 · 2 factorial design with the factors being dietary betaine (0, 10, 20 or 40 g) and shade (with and without shade) for 120 days. Tissue samples were obtained at slaughter and analysed for gene expression of heat shock proteins 70 and 90 (HSP70/90) and expression of heat shock factor 1 (HSF1), and enzyme activity of fatty acid synthase (FAS) and glycerol-6-phosphate dehydrogenase (G6PDH). Carcasses were evaluated for quality. Carcass weight at slaughter was not altered by shade (P = 0.18) but tended to be increased by dietary betaine (306 v. 314 kg, P = 0.09). The P8 backfat was not altered by shade (P = 0.43) or dietary betaine (P = 0.32), although there was a within dietary betaine effect whereby P8 backfat tended to be greater in steers fed 10 g compared with 40 g betaine/day (17.4 v. 14.5 mm, P = 0.06). Muscle pH at 1 h (5.97 v. 6.03, P = 0.01) and 2 h (5.73 v. 5.80, P = 0.04) post-slaughter was higher in shaded steers, and muscle pH at 1 h post-slaughter was higher in steers fed 10 or 20 g than those fed 40 g betaine/day (6.03 v. 6.03 v. 5.95, P = 0.005). Gene expression was not altered by betaine, while adipose tissues expressed more of each gene than muscle (P < 0.001). The mRNA expression of HSF1 and HSP90 was influenced by a shade · betaine interaction, although the direction of this interaction was irregular (P = 0.03 and 0.03, respectively). Adipose tissue FAS and G6PDH enzyme activity was unaffected by shade and betaine. The results of this study indicate that betaine supplementation may be a successful carcass modifier in growing feedlot steers during summer. Provision of shade during summer may reduce the rate of pH decline in the first 2 h after slaughter and reduce the risk of high rigor temperature.

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Effect of Interleukin-1β on Peripheral Blood Leukocytes in Rats with Various Behavioral Characteristics during Acute Stress

2014

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We studied the effect of a pro-inflammatory cytokine IL-1β (5 μg/kg intraperitoneally) on blood leukocytes in Wistar rats various behavioral characteristics during acute emotional stress (1-h immobilization with simultaneous delivery of subthreshold electrocutaneous stimulation). Stress exposure was accompanied by a decrease in the total number of peripheral blood leukocytes in rats. Active animals were characterized by the increase in neutrophil count during stress. The number of eosinophils in passive specimens was shown to decrease under these conditions. Emotional stress was followed by a decrease in the lymphocyte index (by Shaganin) of active rats and increase in the leukocyte intoxication index (according to Kalf-Kalif) of passive specimens. Stress-induced changes in leukocytes differed after pretreatment with IL-1β. The number of blood leukocytes increased in animals receiving a cytokine injection before stress exposure. Exogenous IL-1β inverted (in active rats) or prevented (in passive specimens) a change in the percentage of various types of blood leukocytes, which was found after stress exposure. These data contribute to the understanding of peripheral mechanisms for the involvement of immunomodulatory cytokines in the systemic organization of physiological functions in specimens with different prognostic resistance to a similar stress exposure.

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Synthesis of heat shock proteins (HSP70) in blood leukocytes as a criterion of the resistance to stress injury

Cited by 5 publications

References 5 publications

Heat shock proteins: Changes related to aging, development of thrombotic complications, and peptide regulation of the genome

Heat shock proteins: Changes related to aging, development of thrombotic complications, and peptide regulation of the genome

Dietary betaine supplementation has energy-sparing effects in feedlot cattle during summer, particularly in those without access to shade

Effect of Interleukin-1β on Peripheral Blood Leukocytes in Rats with Various Behavioral Characteristics during Acute Stress

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