scholarly journals Transcriptional and translational regulation of heat shock proteins in leukocytes of endurance runners

2000 ◽  
Vol 89 (2) ◽  
pp. 704-710 ◽  
Author(s):  
Elvira Fehrenbach ◽  
Andreas Michael Niess ◽  
Elke Schlotz ◽  
Frank Passek ◽  
Hans-Herrmann Dickhuth ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Translational Regulation ◽  
Antioxidant Systems ◽  
Mrna Levels ◽  
Adaptive Mechanisms ◽  
Peripheral Leukocytes ◽  
Exercise Induced ◽  
Shock Proteins

Heat shock proteins (HSP) represent cell-protective and antioxidant systems that may be induced by reactive oxygen species, cytokines, and hyperthermia. In the present study, we evaluated the influence of heavy endurance exercise and training on HSP27 and HSP70 in peripheral leukocytes of 12 athletes (before and at 0, 3, and 24 h after a half-marathon) and 12 untrained controls on protein and mRNA levels by flow cytometry and RT/PCR, respectively. HSP transcripts increased significantly immediately after acute exertion accompanied by elevated levels of corresponding proteins. HSP protein expression remained high until 24 h postexercise. Significant increases of plasma interleukin-8, myeloperoxidase, and creatine kinase occurred after exercise. Basal HSP expression was usually lower in trained compared with untrained subjects. Applying in vitro heat shock to resting blood samples of all subjects significantly stimulated HSP mRNA, showing higher increases in trained individuals. The exercise-induced alterations indicate that immunocompetent cells became activated. In addition to heat stress, other exercise-associated stress agents (oxidants, cytokines) may have also participated in stimulation of HSP expression in leukocytes. The expression pattern of HSP due to training status may be attributed to adaptive mechanisms.

In Vitro Holdase Activity of E. coli Small Heat-Shock Proteins IbpA, IbpB and IbpAB: A Biophysical Study with Some Unconventional Techniques

2014 ◽  
Vol 21 (6) ◽  
pp. 564-571 ◽  
Author(s):  
Sourav Roy ◽  
Monobesh Patra ◽  
Suman Nandy ◽  
Milon Banik ◽  
Rakhi Dasgupta ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
E Coli ◽  
Biophysical Study ◽  
Shock Proteins

Translation of Some Maize Small Heat Shock Proteins Is Initiated From Internal In-Frame AUGs

Genetics ◽  
1998 ◽  
Vol 148 (1) ◽  
pp. 471-477
Author(s):  
J Roger H Frappier ◽  
David B Walden ◽  
Burr G Atkinson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Single Gene ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

Abstract Etiolated maize radicles (inbred Oh43) subjected to a brief heat shock synthesize a family of small heat shock proteins (≃18 kD) that is composed of at least 12 members. We previously described the cDNA-derived sequence of three maize shsp mRNAs (cMHSP18-1, cMHSP18-3, and cMHSP18-9). In this report, we demonstrate that the mRNA transcribed in vitro from one of these cDNAs (cMHSP 18-9) is responsible for the synthesis of three members of the shsp family, and we suggest that cMHSP18-3 may be responsible for the synthesis of three additional members and cMHSP18-1 for the synthesis of two other members of this family. The fact that these genes do not contain introns, coupled with the observations reported herein, suggest that maize may have established another method of using a single gene to produce a number of different proteins.

scholarly journals Exercise, heat shock proteins and insulin resistance

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160529 ◽  
Author(s):  
Ashley E. Archer ◽  
Alex T. Von Schulze ◽  
Paige C. Geiger
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Metabolic Effects ◽  
Diabetic Patients ◽  
Alcoholic Fatty Liver ◽  
Insulin Resistant ◽  
Exercise Induced ◽  
Shock Proteins

Best known as chaperones, heat shock proteins (HSPs) also have roles in cell signalling and regulation of metabolism. Rodent studies demonstrate that heat treatment, transgenic overexpression and pharmacological induction of HSP72 prevent high-fat diet-induced glucose intolerance and skeletal muscle insulin resistance. Overexpression of skeletal muscle HSP72 in mice has been shown to increase endurance running capacity nearly twofold and increase mitochondrial content by 50%. A positive correlation between HSP72 mRNA expression and mitochondrial enzyme activity has been observed in human skeletal muscle, and HSP72 expression is markedly decreased in skeletal muscle of insulin resistant and type 2 diabetic patients. In addition, decreased levels of HSP72 correlate with insulin resistance and non-alcoholic fatty liver disease progression in livers from obese patients. These data suggest the targeted induction of HSPs could be a therapeutic approach for preventing metabolic disease by maintaining the body's natural stress response. Exercise elicits a number of metabolic adaptations and is a powerful tool in the prevention and treatment of insulin resistance. Exercise training is also a stimulus for increased HSP expression. Although the underlying mechanism(s) for exercise-induced HSP expression are currently unknown, the HSP response may be critical for the beneficial metabolic effects of exercise. Exercise-induced extracellular HSP release may also contribute to metabolic homeostasis by actively restoring HSP72 content in insulin resistant tissues containing low endogenous levels of HSPs. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

A family of related proteins is encoded by the major Drosophila heat shock gene family

1982 ◽  
Vol 2 (3) ◽  
pp. 286-292
Author(s):  
S C Wadsworth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Sodium Dodecyl ◽  
Heat Shock Gene ◽  
Partial Digestion ◽  
Shock Gene ◽  
Shock Proteins

At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.

Expressions of heat shock proteins under heat-stress and interferon-treatment: An in vitro study on osteosarcoma

1996 ◽  
Vol 3 (4) ◽  
pp. 233-239 ◽  
Author(s):  
Toshikazu Kubo ◽  
Yuji Tamura ◽  
Kenji Takahashi ◽  
Jiro Imanishi ◽  
Yasusuke Hirasawa
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
In Vitro Study ◽  
Vitro Study ◽  
Interferon Treatment ◽  
Shock Proteins

Expression of heat shock genes of Neurospora crassa: effect of hyperthermia and other stresses on mRNA levels

1988 ◽  
Vol 66 (2) ◽  
pp. 81-92 ◽  
Author(s):  
Carol A. Curle ◽  
M. Kapoor
Keyword(s):  
Heat Shock ◽  
Neurospora Crassa ◽  
Sodium Arsenite ◽  
Gene Probe ◽  
Mrna Levels ◽  
Hsp 70 ◽  
Northern Blots ◽  
Stressed Cells ◽  
Shock Proteins

Neurospora crassa mycelium was heat shocked for intervals varying from 15–180 min. Heat shock mRNA was monitored by hybridization of Northern blots with the Drosophila hsp-70 gene probe and an inducible member of the yeast hsp-70 gene family, YG100. A 2.7 kilobase (kb) transcript, with homology to these two probes, was detected in cultures shocked for 15 min; its levels increased up to 60–90 min and declined thereafter. Sodium arsenite, too, induced the synthesis of this transcript. An additional, constitutively synthesized 2.4-kb transcript was revealed by hybridization with the yeast probe. The synthesis of this message was terminated during heat shock. Hybridization of Northern blots with the Drosophila actin gene probe demonstrated two size classes, 1.85 and 1.63 kb; the former decreased dramatically following heat shock. Recovery, as assessed by the disappearance of the 2.7-kb hsp-70-mRNA and restoration of the 1.85-kb actin message to the prestress levels, was essentially complete within 60 min of transfer to 28 °C. In vitro translations of RNA from stressed cells showed the heat shock messages to be stable and readily translatable. RNA of cells subjected to heat shock plus CdCl2 showed a higher content of messages for heat shock proteins of 70, 80, and 90 kilodaltons.

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