Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia

Hickey, Eileen; Brandon, Susan E.; Sadis, Seth; Smale, Georgeann; Weber, Lee A.

doi:10.1016/0378-1119(86)90018-1

Cited by 126 publications

(83 citation statements)

References 23 publications

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“…The human Hsp27 cDNA insert of the plasmid pHS 208 (Hickey et al, 1986) was radiolabelled with [ 32 P]dCTP using a Random Primers DNA Labeling System (Life Technologies, Gaithersburg, MD, USA) and used as a probe for Northern and Southern blot analysis. A glutathione-S-transferase pi (GSTπ) cDNA probe was made according to a nucleotide sequence derived from the human glutathione-S-transferase pi cDNA (Moscow et al, 1989).…”

Section: Dna Constructs and Probesmentioning

confidence: 99%

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

et al. 1999

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SummaryThe protein expression patterns of normal, metaplastic and malignant oesophageal tissues were analysed by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) to identify changes associated with Barrett's metaplasia and transformation to oesophageal adenocarcinoma. Heat-shock protein 27 (Hsp27), a small heat-shock protein which is protective against cytotoxic stresses, was abundant in normal oesophagus. However, Hsp27 expression was markedly lower in Barrett's metaplasia and oesophageal adenocarcinomas. This was confirmed by immunohistochemical analysis. Hsp27 protein was most highly expressed in the upper layers of squamous epithelium and exhibited a pattern of expression that corresponded with the degree of squamous maturation. Northern and Southern analysis demonstrated Hsp27 to be regulated at the level of mRNA transcription or abundance. Normal oesophageal tissues were examined for gender differences in Hsp27 expression. Women expressed fourfold higher levels of Hsp27 mRNA, however, this difference was not appreciable in protein expression. Hsp27 protein was inducible by heat shock in Barrett's adenocarcinoma cell lines and an immortalized oesophageal epithelial cell line (HET-1A), but not by oestradiol. These results demonstrate abundant constitutive expression of the stress-response protein Hsp27 in the normal oesophagus, and suggest that low-level expression in Barrett's metaplasia may be one factor which may influence susceptibility to oesophageal adenocarcinoma development.

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Section: Dna Constructs and Probesmentioning

confidence: 99%

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

et al. 1999

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“…RESULTS Induction of hsp89. To assay the expression of the various hsp genes during an adenovirus infection of HeLa cells, we used a group of cDNA clones that detect mRNAs encoding two forms of hsp89 (a and I), hsp70, and hsp27 (12). A Northern blot analysis of RNA from control and heatshocked HeLa cells that were probed with three of these cDNAs (hsp89a, hsp7O, and hsp27) is shown in Fig.…”

Section: Cellsmentioning

confidence: 99%

“…Translation of hybrid-selected mRNAs has identified the product of each mRNA and thus the labeling as hsp89, hsp27, etc. (12,19).…”

Section: Cellsmentioning

confidence: 99%

Selective induction of human heat shock gene transcription by the adenovirus E1A gene products, including the 12S E1A product.

Simon¹,

Kitchener²,

Kao³

et al. 1987

Mol. Cell. Biol.

111

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We have previously shown that the human 70-kilodalton heat shock protein gene (hsp7O) is induced by the adenovirus ElA gene product and during the S-G2 phase of the cell cycle. In this study, we investigated the effect of ElA on the expression of other human hsp genes. A gene encoding one form of the hsp89 protein (hsp89a) was activated during an adenovirus infection with kinetics similar to those of activation of hsp7O. The induction required a functional ElA gene. However, the hsp89 transcript was not cell cycle regulated. Genes encoding another form of hsp89 and the hsp27 protein were not induced by ElA or during the cell cycle. Further examination of hsp7O expression revealed a greater complexity than previously seen. Si nuclease analysis using an hsp70 cDNA as well as a distinct hsp7O genomic clone demonstrated three related hsp70 transcripts; two were induced by ElA, and one was not. Both of the ElA-inducible genes were regulated during the cell cycle. All three were induced by heat shock. These results suggest common aspects of control among certain members of this family of cellular genes distinct from heat shock control. Finally, using viruses that express the individual ElA proteins, we found that the hsp70 gene is induced by the 12S and the 13S ElA products. The efficiency of induction by the 12S product was somewhat less than that by the 13S product but only by a factor of less than 2. This is in contrast to the induction of early viral genes, for which the 13S product is considerably more efficient than the 12S product.

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“…Fhe human heat shock protein 60 gene probe was a 1.5 kb PstI fragment of the corresponding cDNA isolated from the plasmid pIICHS601 as supplied by StressGen Biotechnologies Corp. Victoria, BC, Canada [13]. The human catalase gene probe was a single copy cl ~NA obtained by screening a human cDNA library with an oligom~cleotide corresponding to 17 bp of the human erythrocyte catalase.…”

Section: / Gene Sequence Probesmentioning

confidence: 99%

Hydrogen peroxide and sequence‐specific DNA damage in human cells

et al. 1996

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Exposure of HeLa cells in monolayer culture to increasing concentrations of exogenously added H202 causes damage to cellular DNA. When the DNA is subsequently isolated from the non-apoptotic cells remaining in such cultures, evidence was obtained to suggest that the DNA damage elicited in intact cells was non-random and that certain nucleotide sequences associated with, or related to, the genes for heat shock protein 60 and catalase were more susceptible to damage than others. In contrast, these particular sequences were not specifically susceptible to damage when naked human DNA was exposed directly to H202 in vitro. On an overall comparative basis, sequences in the genes encoding catalase, ¢x-1 antitrypsin and D-actin appear more vulnerable to H202 in vivo, than sequences in H-ras and the p53 gene which seem surprisingly resistant.

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Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia

Cited by 126 publications

References 23 publications

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

Differential expression of Hsp27 in normal oesophagus, Barrett’s metaplasia and oesophageal adenocarcinomas

Selective induction of human heat shock gene transcription by the adenovirus E1A gene products, including the 12S E1A product.

Hydrogen peroxide and sequence‐specific DNA damage in human cells

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