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.

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.

Comparison of the effects of heat shock and metal-ion stress on gene expression in cells undergoing myogenesis

1983 ◽  
Vol 61 (6) ◽  
pp. 404-413 ◽  
Author(s):  
Burr G. Atkinson ◽  
Tanja Cunningham ◽  
Rob L. Dean ◽  
Martin Somerville
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Thermal Stress ◽  
Heat Shock ◽  
Metal Ion ◽  
Breast Tissue ◽  
Primary Cultures ◽  
In Ovo ◽  
Isoelectric Points ◽  
Shock Proteins

Subjecting 9-day-old quail embryos to an elevated temperature in ovo causes limb, breast, and brain tissues to shift their patterns of protein synthesis from the production of a broad spectrum of different proteins to the new and (or) enhanced synthesis of a small number of heat-shock proteins (HSPs). The HSPs synthesized by undifferentiated breast tissue in ovo (relative masses (Mrs) 88 000, 82 000, 64 000, and 25 000) are similar to those synthesized by explanted breast tissue or by primary cultures of breast myoblasts heat-shocked in culture. Heat-shocked, 120-hour-old myotube cultures synthesize HSPs similar to those detected in heat-shocked myoblasts except that myotubes also exhibit enhanced synthesis of a 55 000 dalton polypeptide and little or no synthesis of a 25 000 dalton HSP; the failure to thermally induce a 25 000 dalton polypeptide in myotubes is related to the fused nature of these cells rather than to their state of differentiation. Myoblasts, as well as myotubes, cultured in the presence of elevated amounts of arsenite, copper, or zinc also synthesize new and (or) enhanced amounts of polypeptides with isoelectric points and immunochemical properties similar to the 25 000 and 64 000 dalton HSPs. However, elevated levels of these metal ions fail to stimulate new and (or) enhanced synthesis of other HSP-like proteins. These results demonstrate that, although the protein synthetic response of myogenic cells to chemical and thermal stress may be similar in some respects, a number of the synthetic responses are clearly different.

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.

EGF induces cell cycle arrest of A431 human epidermoid carcinoma cells

1986 ◽  
Vol 127 (1) ◽  
pp. 175-182 ◽  
Author(s):  
Carol L. MacLeod ◽  
Andrew Luk ◽  
Janice Castagnola ◽  
Maureen Cronin ◽  
John Mendelsohn
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Carcinoma Cells ◽  
Epidermoid Carcinoma ◽  
Cycle Arrest ◽  
Human Epidermoid Carcinoma
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