Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean

The suborder Notothenioidae is comprised of Antarctic fishes, several of which have lost their ability to rapidly upregulate heat shock proteins in response to thermal stress, instead adopting a pattern of expression resembling constitutive genes. Given the cold-denaturing effect that sub-zero waters have on proteins, evolution in the Southern Ocean has likely selected for increased expression of molecular chaperones. These selective pressures may have also enabled retention of gene duplicates, bolstering quantitative output of cytosolic heat shock proteins (HSPs). Given that newly duplicated genes are under more relaxed selection, it is plausible that gene duplication enabled altered regulation of such highly conserved genes. To test for evidence of gene duplication, copy number of various isoforms within major heat shock gene families were characterized via qPCR and compared between the Antarctic notothen, Trematomus bernacchii, which lost the inducible heat shock response, and the non-Antarctic notothen, Notothenia angustata, which maintains an inducible heat shock response. The results indicate duplication of isoforms within the hsp70 and hsp40 super families have occurred in the genome of T. bernacchii. The findings suggest gene duplications may have been critical in maintaining protein folding efficiency in the sub-zero waters and provided an evolutionary mechanism of alternative regulation of these conserved gene families.

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Physical Activity, Muscle, and the HSP70 Response

Canadian Journal of Applied Physiology ◽

10.1139/h98-013 ◽

1998 ◽

Vol 23 (3) ◽

pp. 245-260 ◽

Cited By ~ 37

Author(s):

J. Lon Kilgore ◽

Timothy I. Musch ◽

Christopher R. Ross

Keyword(s):

Physical Activity ◽

Heat Shock ◽

Heat Shock Proteins ◽

Heat Shock Protein ◽

Heat Shock Response ◽

Shock Response ◽

Potential Applications ◽

Shock Proteins ◽

External Stimuli ◽

Exercise And Training

Selye (1936) described how organisms react to various external stimuli (i.e., stressors). These reactions generally follow a programmed series of events and help the organism adapt to the imposed stress. The heat shock response is a common cellular reaction to external stressors, including physical activity. A characteristic set of proteins is synthesised shortly after the organism is exposed to stress. Researchers have not determined how heat shock proteins affect the exercise response. However, their role in adaptation to exercise and training might he inferred, since the synthetic patterns correlate well with the stress adaptation syndrome that Selye described. This review addresses the 70 kilodalton heat shock protein family (HSP70), the most strongly induced heat shock proteins. This paper provides an overview of the general heat shock response and a brief review of literature on HSP70 function, structure, regulation, and potential applications. Potential applications in health, exercise, and medicine are provided. Key words: heat shock, protein, exercise

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Expression of a Conserved Family of Cytoplasmic Low Molecular Weight Heat Shock Proteins during Heat Stress and Recovery

PLANT PHYSIOLOGY ◽

10.1104/pp.96.4.1038 ◽

1991 ◽

Vol 96 (4) ◽

pp. 1038-1047 ◽

Cited By ~ 87

Author(s):

Amy E. DeRocher ◽

Kenneth W. Helm ◽

Lisa M. Lauzon ◽

Elizabeth Vierling

Keyword(s):

Molecular Weight ◽

Heat Stress ◽

Heat Shock ◽

Heat Shock Proteins ◽

Low Molecular Weight ◽

Shock Proteins

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