scholarly journals Developmental Expression and Functions of the Small Heat Shock Proteins in Drosophila

2018 ◽  
Vol 19 (11) ◽  
pp. 3441 ◽  
Author(s):  
Teresa Jagla ◽  
Magda Dubińska-Magiera ◽  
Preethi Poovathumkadavil ◽  
Małgorzata Daczewska ◽  
Krzysztof Jagla
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Large Family ◽  
Active Role ◽  
Stress Conditions ◽  
Developmental Expression ◽  
Shsp Gene ◽  
Time Specific ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (Hsps) form a large family of evolutionarily conserved molecular chaperones that help balance protein folding and protect cells from various stress conditions. However, there is growing evidence that Hsps may also play an active role in developmental processes. Here, we take the example of developmental expression and function of one class of Hsps characterized by low molecular weight, the small Hsps (sHsps). We discuss recent reports and genome-wide datasets that support vital sHsps functions in the developing nervous system, reproductive system, and muscles. This tissue- and time-specific sHsp expression is developmentally regulated, so that the enhancer sequence of an sHsp gene expressed in developing muscle, in addition to stress-inducible elements, also carries binding sites for myogenic regulatory factors. One possible reason for sHsp genes to switch on during development and in non-stress conditions is to protect vital developing organs from environmental insults.

scholarly journals Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets

Cells ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 1263 ◽  
Author(s):  
Maxim Shevtsov ◽  
Zsolt Balogi ◽  
William Khachatryan ◽  
Huile Gao ◽  
László Vígh ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Intracellular Localization ◽  
Large Family ◽  
Basic Research ◽  
Stress Factors ◽  
Small Hsps ◽  
Stress Oxidative ◽  
Shock Proteins

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.

scholarly journals Modulation of Heat-Shock Proteins Mediates Chicken Cell Survival against Thermal Stress

Animals ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 2407
Author(s):  
Abdelrazeq M. Shehata ◽  
Islam M. Saadeldin ◽  
Hammed A. Tukur ◽  
Walid S. Habashy
Keyword(s):  
Oxidative Stress ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Survival ◽  
Cell Damage ◽  
Stress Conditions ◽  
Economic Losses ◽  
Chicken Cell ◽  
Shock Proteins

Heat stress is one of the most challenging environmental stresses affecting domestic animal production, particularly commercial poultry, subsequently causing severe yearly economic losses. Heat stress, a major source of oxidative stress, stimulates mitochondrial oxidative stress and cell dysfunction, leading to cell damage and apoptosis. Cell survival under stress conditions needs urgent response mechanisms and the consequent effective reinitiation of cell functions following stress mitigation. Exposure of cells to heat-stress conditions induces molecules that are ready for mediating cell death and survival signals, and for supporting the cell’s tolerance and/or recovery from damage. Heat-shock proteins (HSPs) confer cell protection against heat stress via different mechanisms, including developing thermotolerance, modulating apoptotic and antiapoptotic signaling pathways, and regulating cellular redox conditions. These functions mainly depend on the capacity of HSPs to work as molecular chaperones and to inhibit the aggregation of non-native and misfolded proteins. This review sheds light on the key factors in heat-shock responses for protection against cell damage induced by heat stress in chicken.

Developmental expression of Drosophila melanogaster small heat-shock proteins

1990 ◽  
Vol 96 (3) ◽  
pp. 413-418
Author(s):  
C. Haass ◽  
U. Klein ◽  
P.M. Kloetzel
Keyword(s):  
Nervous System ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Developmental Expression ◽  
Germ Band ◽  
Small Hsp ◽  
Small Hsps ◽  
Shock Proteins ◽  
The Brain

We have investigated the developmental expression of the small heat-shock proteins (hsps) during embryogenesis and in adult flies by immunocytology using an antibody that specifically identifies the small hsps. Antibody staining of unstressed early embryos reveals a predominantly cytoplasmic, homogeneous distribution of the small hsps throughout the embryo. At 6h of development small hsp expression can be identified in large, neuroblast-like cells within the extended germ band and in the brain of the embryo. During germ band contraction these cells appear to migrate to the midline where they align pairwise in a segmental pattern. After germ band contraction is complete a high level of small hsp expression can be observed in the midline glia (MECs) and in a cluster of six non-neuronal cells within the midline. In contrast to several other genes that are known to be important for embryogenesis and are expressed in the central nervous system (CNS) of embryos, CNS-specific expression of the small hsps is not restricted to the embryo but is also observed in the adult fly. In adult flies strong small hsp expression is observed in the brain, the thoracic ganglion and the leg nerves. Since the small hsps seem to be expressed predominantly in the glia of the nervous system, our data suggest a protective or stabilizing function of the small hsps within the nervous system during normal fly development, which is independent of the stress response.

scholarly journals Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Arman Kilic ◽  
Kaushik Mandal
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Vascular Endothelial Cell ◽  
Vascular Wall ◽  
Protective Role ◽  
Therapeutic Implications ◽  
Endothelial Cell Surface ◽  
Disease States ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiologic and pathologic roles of these proteins. This paper summarizes the role of HSPs in normal vascular wall processes as well as in the development and progression of atherosclerosis. The potential implications of HSPs in clinical therapies for atherosclerosis are also discussed.

scholarly journals Structure and Function of Small Heat Shock Proteins from the Magnetotactic Bacterium Magnetospirillum magneticum AMB-1

2010 ◽  
Vol 67 (12) ◽  
pp. 698-704 ◽  
Author(s):  
Tetsuya ABE ◽  
Shinpei ITO ◽  
Naoya NISHI ◽  
Yoshihiro TSUKADA ◽  
Takuo YASUNAGA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Magnetotactic Bacterium ◽  
Shock Proteins ◽  
And Function ◽  
Magnetospirillum Magneticum

scholarly journals Evolution, structure and function of the small heat shock proteins in plants

1996 ◽  
Vol 47 (3) ◽  
pp. 325-338 ◽  
Author(s):  
Elizabeth R. Waters ◽  
Garrett J. Lee ◽  
Elizabeth Vierling
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Heat Shock Proteins ◽  
Structure And Function ◽  
Shock Proteins ◽  
And Function
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