Heat shock induced changes in the gene expression of terminally differentiating avian red blood cells

1986 ◽  
Vol 28 (6) ◽  
pp. 1053-1063 ◽  
Author(s):  
Burr G. Atkinson ◽  
Rob L. Dean ◽  
Timothy W. Blaker
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Temperature Separation ◽  
Shock Proteins ◽  
Separation Of Proteins ◽  
Induced Changes ◽  
Cellular Compartments ◽  
Triton X

Reticulocytes, purified from the blood of quail and chickens recovering from anaemia, respond to heat shock by (i) the new and (or) enhanced synthesis of heat-shock protein (HSPs) with relative molecular masses of > 400 000, 90 000, 70 000, and 26 000 (quail) or 24 000 (chicken) and (ii) the depressed synthesis of many proteins normally produced at a control temperature. The synthesis of these HSPs is noncoordinate since the expression of each protein depends upon the particular temperature and duration of the time at that temperature. Separation of proteins from quail reticulocytes into Triton X-100 soluble and insoluble fractions demonstrates that the 70 000 and 26 000 Da HSPs are found in both fractions, whereas the > 400 000 and 90 000 Da HSPs are located only in the detergent-soluble fraction. Triton X-100 fractionation also reveals that there are three isoelectric variants of the 70 000 Da HSP and that they are constitutively synthesized and selectively partitioned between cellular compartments. Heat shock induced synthesis of the 90 000, 70 000, and 26 000 Da quail HSPs is prevented by actinomycin D, while enhanced synthesis of the > 400 000 Da HSP is unaffected by this inhibitor. These results demonstrate that nucleated, terminally differentiating avian red blood cells are capable of responding to heat stress by rapid changes in their highly restricted "program" of gene expression.Key words: heat shock, heat-shock proteins, reticulocytes, avian, red blood cells, gene expression.

Effect of heat shock on gene expression in human epidermoid carcinoma cells (strain KB) and in primary cultures of mammalian and avian cells

1982 ◽  
Vol 60 (3) ◽  
pp. 316-327 ◽  
Author(s):  
Burr G. Atkinson ◽  
Michael Pollock
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Primary Cultures ◽  
Apparent Molecular Weight ◽  
Carcinoma Cells ◽  
Epidermoid Carcinoma ◽  
Kb Cells ◽  
Shock Proteins ◽  
Triton X ◽  
Human Epidermoid Carcinoma

The brief incubation of human epidermoid carcinoma (KB) cells, and of primary cultures of quail myoblasts and hamster fibroblasts, at an elevated temperature causes the pattern of gene expression to shift from the production of a broad spectrum of different proteins to the enhanced synthesis of a small number of heat-shock proteins. Comparison of the heat-shock polypeptides synthesized by each of these vertebrate cells demonstrates the similarity of some, as well as the uniqueness of other, heat-inducible gene products synthesized by cells from different vertebrates. A major polypeptide, commonly synthesized in response to heat by each of these vertebrate cells, has an apparent molecular weight of 64 000 and an isoelectric point of 5.8. Triton X-100 completely extracts this polypeptide from quail myoblasts and hamster fibroblasts, and partially extracts it from KB cells. This particular response to heat shock, by cells from different vertebrates, suggests that it may involve the expression of a gene(s) with an analogous and potentially crucial cellular function. This specific heat-shock polypeptide, as well as others, is not detectably synthesized in quail cells prior to heat shock or 6–8 h after recovery from heat shock which suggests that in this cell type it may be a product of a normally quiescent gene(s) and that its expression is subject to thermal regulation.

scholarly journals Heat-induced expression of albumin during early stages of rat embryo development.

1987 ◽  
Vol 7 (12) ◽  
pp. 4599-4602 ◽  
Author(s):  
U K Srinivas ◽  
C J Revathi ◽  
M R Das
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Embryonic Liver ◽  
Rat Embryo ◽  
Adult Liver ◽  
Stages Of Development ◽  
Induced Expression ◽  
Molecular Events ◽  
Internal Change ◽  
Shock Proteins

An examination of heat-induced expression of proteins in tissues from adult and embryonic liver in rats shows that albumin, which is constitutively expressed in adult liver and is not synthesized in embryos before 16 days of gestation, appears in liver cells at earlier stages of development upon heat shock. On the basis of available evidence for the expression of heat shock proteins at distinct stages of development and on the basis of our findings, it may be argued that there could be common molecular events taking place during development and as a result of heat shock. We suggest also that one of the consequences of heat shock could be an internal change of pH within the cell which, in turn, might trigger alterations in gene expression.

Coordination of Chemical (Trimethylamine Oxide) and Molecular (Heat Shock Protein 70) Chaperone Responses to Heat Stress in Elasmobranch Red Blood Cells

2014 ◽  
Vol 87 (5) ◽  
pp. 652-662 ◽  
Author(s):  
Ashra Kolhatkar ◽  
Cayleih E. Robertson ◽  
Maria E. Thistle ◽  
A. Kurt Gamperl ◽  
Suzanne Currie
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Heat Shock Protein 70 ◽  
Trimethylamine Oxide

Synthesis of stress protein 70 (Hsp70) in rainbow trout (Oncorhynchus mykiss) red blood cells

1997 ◽  
Vol 200 (3) ◽  
pp. 607-614 ◽  
Author(s):  
S Currie ◽  
B Tufts
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Heat Shock ◽  
Oncorhynchus Mykiss ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Stress Proteins ◽  
Stress Protein ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Hsp70 Synthesis

Unlike enucleated mammalian red blood cells (rbcs), the nucleated rbcs of lower vertebrates are capable of protein synthesis and may, therefore, serve as a valuable model to investigate the adaptive significance of stress protein synthesis in cells. This study examined the synthesis of stress protein 70 (Hsp70) in rbcs of the temperature-sensitive rainbow trout Oncorhynchus mykiss in response to heat shock and anoxia. Through western blot analysis, we have demonstrated that rainbow trout rbcs synthesize Hsp70 both constitutively and in response to an increase in temperature. Radioisotopic labelling experiments indicated that the temperature at which Hsp70 synthesis was induced in fish acclimated to 10 °C was between 20 and 25 °C. Actinomycin D blocked de novo Hsp70 synthesis, implying that synthesis of Hsp70 is regulated at the level of transcription in rainbow trout rbcs. Since trout rbcs rely heavily on aerobic metabolism, but may also experience very low oxygen levels within the circulation, we also examined the relative importance of (1) anoxia as a stimulus for Hsp70 synthesis and (2) oxygen as a requirement for protein synthesis under control and heat-shock conditions. We found that trout rbcs were capable of protein synthesis during 2 h of anoxia, but did not increase Hsp70 synthesis. Moreover, rbcs subjected to combined anoxia and heat shock exhibited increases in Hsp70 synthesis that were similar in magnitude to those in cells exposed to heat shock alone. The latter results suggest that rainbow trout rbcs are (1) able to synthesize non-stress proteins during anoxia, (2) capable of tolerating periods of reduced oxygen availability without increased synthesis of stress proteins and (3) able to maintain the integrity of their heat-shock response even during periods of anoxia.

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