scholarly journals Interleukin 1 induces the expression of a heat-shock gene in chondrocytes

1991 ◽  
Vol 277 (2) ◽  
pp. 327-330 ◽  
Author(s):  
T F Cruz ◽  
R A Kandel ◽  
I R Brown
Keyword(s):  
Heat Shock ◽  
Interleukin 1 ◽  
Heat Shock Gene ◽  
Proteoglycan Synthesis ◽  
Hsp70 Mrna ◽  
Mrna Species ◽  
Shock Gene ◽  
Shock Proteins ◽  
Arthritic Joints

The presence of T cells and antibodies reactive with heat-shock proteins (hsps) in the joints of patients with rheumatoid arthritis may indicate a role of hsps in this disease. In the present study we examined whether increased temperature and interleukin 1 (IL 1), both of which are elevated in arthritic joints, induced the expression of two hsp70 genes in bovine chondrocyte cultures. We found that heat shock resulted in increased expression of constitutive and inducible hsp70 mRNA species. IL 1 and phorbol 12-myristate 13-acetate (PMA) also induced an increase in the constitutive hsp70 mRNA species, but without affecting the expression of the inducible hsp70 gene. The increase induced by IL 1 was observed only after 3 h, whereas increases induced by PMA were observed within 1 h. For all treatments, the hsp70 mRNA decreased by 24 h. Heat treatment of chondrocytes did not affect levels of collagenase and caseinase activity in the medium, nor did it alter proteoglycan synthesis by these cells.

Thermotolerant desert lizards characteristically differ in terms of heat-shock system regulation

2000 ◽  
Vol 203 (6) ◽  
pp. 1017-1025 ◽  
Author(s):  
O.G. Zatsepina ◽  
K.A. Ulmasov ◽  
S.F. Beresten ◽  
V.B. Molodtsov ◽  
S.A. Rybtsov ◽  
...  
Keyword(s):  
Heat Shock ◽  
Gene Promoter ◽  
Heat Shock Gene ◽  
Ecological Niches ◽  
Lizard Species ◽  
Hsp70 Mrna ◽  
Desert Species ◽  
Shock System ◽  
Shock Gene ◽  
Shock Proteins

We compare the properties and activation of heat-shock transcription factor (HSF1) and the synthesis of a major family of heat-shock proteins (HSP70) in lizard species inhabiting ecological niches with strikingly different thermal parameters. Under normal non-heat-shock conditions, all desert-dwelling lizard species studied so far differ from a northern, non-desert species (Lacerta vivipara) in the electrophoretic mobility and content of proteins constitutively bound to the regulatory heat-shock elements in the heat-shock gene promoter. Under these conditions, levels of activated HSF1 and of both HSP70 mRNA and protein are higher in the desert species than in the non-desert species. Upon heat shock, HSF1 aggregates in all species studied, although in desert species HSF1 subsequently disaggregates more rapidly. Cells of the northern species have a lower thermal threshold for HSP expression than those of the desert species, which correlates with the relatively low constitutive level of HSPs and high basal content of HSF1 in their cells.

A family of related proteins is encoded by the major Drosophila heat shock gene family

1982 ◽  
Vol 2 (3) ◽  
pp. 286-292
Author(s):  
S C Wadsworth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Sodium Dodecyl ◽  
Heat Shock Gene ◽  
Partial Digestion ◽  
Shock Gene ◽  
Shock Proteins

At least four proteins of 70,000 to 75,000 molecular weight (70-75K) were synthesized from mRNA which hybridized with a cloned heat shock gene previously shown to be localized to the 87A and 87C heat shock puff sites. These in vitro-synthesized proteins were indistinguishable from in vivo-synthesized heat shock-induced proteins when analyzed on sodium dodecyl sulfate-polyacrylamide gels. A comparison of the pattern of this group of proteins synthesized in vivo during a 5-min pulse or during continuous labeling indicates that the 72-75K proteins are probably not kinetic precursors to the major 70K heat shock protein. Partial digestion products generated with V8 protease indicated that the 70-75K heat shock proteins are closely related, but that there are clear differences between them. The partial digestion patterns obtained from heat shock proteins from the Kc cell line and from the Oregon R strain of Drosophila melanogaster are very similar. Genetic analysis of the patterns of 70-75K heat shock protein synthesis indicated that the genes encoding at least two of the three 72-75K heat shock proteins are located outside of the major 87A and 87C puff sites.

scholarly journals Role of DnaK in In Vitro and In Vivo Expression of Virulence Factors of Vibrio cholerae

1999 ◽  
Vol 67 (3) ◽  
pp. 1025-1033 ◽  
Author(s):  
Sabyasachi Chakrabarti ◽  
Nilanjan Sengupta ◽  
Rukhsana Chowdhury
Keyword(s):  
Heat Shock ◽  
Vibrio Cholerae ◽  
Virulence Factors ◽  
Heat Shock Gene ◽  
Insertion Mutant ◽  
In Vivo Expression ◽  
Shock Gene

ABSTRACT The dnaK gene of Vibrio cholerae was cloned, sequenced, and used to construct a dnaK insertion mutant which was then used to examine the role of DnaK in expression of the major virulence factors of this important human pathogen. The central regulator of several virulence genes of V. choleraeis ToxR, a transmembrane DNA binding protein. The V. cholerae dnaK mutant grown in standard laboratory medium exhibited phenotypes characteristic of cells deficient in ToxR activity. Using Northern blot analysis and toxR transcriptional fusions, we demonstrated a reduction in expression of the toxR gene in the dnaK mutant strain together with a concomitant increase in expression of a htpG-like heat shock gene that is located immediately upstream and is divergently transcribed fromtoxR. This may be due to increased heat shock induction in the dnaK mutant. In vivo, however, although expression from heat shock promoters in the dnaK mutant was similar to that observed in vitro, expression of both toxR andhtpG was comparable to that by the parental strain. In both strains, in vivo expression of toxR was significantly higher than that observed in vitro, but no reciprocal decrease inhtpG expression was observed. These results suggest that the modulation of toxR expression in vivo may be different from that observed in vitro.

Neuroprotective Mechanisms of Heat Shock Gene Expression

1998 ◽  
Vol 4 (4) ◽  
pp. 236-239
Author(s):  
B. Joy Snider
Keyword(s):  
Heat Shock ◽  
Molecular Chaperones ◽  
Cell Types ◽  
Heat Shock Gene ◽  
Cellular Injury ◽  
Genetic Manipulations ◽  
Enhanced Expression ◽  
Shock Gene ◽  
Heat Shock Gene Expression ◽  
Shock Proteins

Heat shock proteins were initially described as the predominant proteins expressed immediately after a thermal stress. These ubiquitously expressed proteins function as molecular chaperones; they aid in the folding, subcellular translocation, and assembly of other proteins. Although most of these proteins are expressed constitutively, enhanced expression, induced by stress or genetic manipulations, can reduce subsequent cellular injury in many cell types, including neurons and glia. Further understanding of how the expression of these proteins is controlled in the nervous system, and how they can be manipulated to attenuate injury, could provide therapeutic targets for cerebral ischemia and neurodegenerative disorders.

Heat stress regulates the human 70-kDa heat-shock gene through the 3'-untranslated region

1993 ◽  
Vol 264 (6) ◽  
pp. L533-L537 ◽  
Author(s):  
P. L. Moseley ◽  
E. S. Wallen ◽  
J. D. McCafferty ◽  
S. Flanagan ◽  
J. A. Kern
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Posttranscriptional Regulation ◽  
Untranslated Region ◽  
Heat Shock Gene ◽  
Beta Globin ◽  
Sv40 Promoter ◽  
Posttranscriptional Control ◽  
Hsp70 Mrna ◽  
Shock Proteins

Cells respond to a variety of stresses by synthesizing a family of proteins termed heat-shock proteins (HSP). Recently, the 3'-untranslated regions (UTRs) of some mRNAs have been shown to be important in the posttranscriptional regulation of protein production. Therefore, we hypothesized that heat could regulate HSP70 production through the HSP70 3'-UTR, in addition to its known effects on transcription. To test this hypothesis, cells were transfected with either a plasmid containing sequences encoding the human HSP70 or beta-globin 3'-untranslated region placed downstream of a chloramphenicol acetyltransferase (CAT) reporter gene. In both plasmids, the CAT gene was driven by an SV40 promoter. Following heat stress, cells transfected with the CAT construct containing the HSP70 3'-UTR showed increased CAT activity relative to the beta-globin 3'-UTR construct. This effect paralleled increases in HSP70 mRNA and levels of the inducible HSP70 protein by Western blot. These studies identify a heat-induced mechanism of posttranscriptional control of HSP70 synthesis utilizing the HSP70 3'-UTR, which may be important in the cells ability to regulate the heat-shock response.

scholarly journals Regulated transcription of the genes for actin and heat-shock proteins in culture drosophila cells

1981 ◽  
Vol 88 (2) ◽  
pp. 323-328 ◽  
Author(s):  
RC Findly ◽  
T Pederson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Gene Transcription ◽  
Dna Sequences ◽  
Heat Shock Gene ◽  
Nuclear Rna ◽  
Gene Transcripts ◽  
Shock Gene ◽  
Shock Proteins ◽  
Drosophila Cells

The transcription of three specific genes has been examined in heat-shocked drosophila cells by hybridizing pulse-labeled nuclear RNA with cloned DNA sequences. Actin gene transcription is rapidly and profoundly suppressed upon heat shock but returns to near- normal levels after cells are placed back at their normal culture temperature (23 degrees C). Conversely, the transcription of genes coding from 70,000- and 26,000-dalton heat- shock proteins increases dramatically and with extraordinary rapidity (60 s) after heat shock. The temporal patterns of 70,000- and 26,000-dalton heat-shock gene transcription are nearly superimposable, indicating that, although they are closely linked cytologically, these genes are nevertheless tightly coregulated. The abundance of heat- shock gene transcripts reaches remarkable levels, e.g., 70,000-dalton heat-shock gene transcripts account for 2-3 percent of the nuclear RNA labeled during the first 30 min of heat shock. When heat-shocked cells are returned to 25 degrees C, the rates of transcription of the heat-shock genes fall back to the low levels characteristic of untreated cells. To confirm the low level of heat-shock gene transcription in normal cells, nuclear RNA was purified from unlabeled (and otherwise unhandled) 25 degrees C cells, end-labeled in vitro with (32)P, and hybridized to cloned heat-shock DNA sequences. These and other data establish that the genes for 70,000- and 26,000-dalton heat-shock proteins in culture drosophila cells are active at 25 degrees C, and that their rate of transcription is greatly accelerated upon heat shock rather than being activated from a true "off" state. The rapidity, magnitude, and reversibility of the shifts in actin and heat-shock gene transcription constitute compelling advantages for the use of cultured drosophila cells in studying the transcriptional regulation of eukaryotic genes, including one related to the cytoskeleton.

scholarly journals Acceleration of HSP70 and HSC70 Heat Shock Gene Expression following Transient Ischemia in the Preconditioned Gerbil Hippocampus

1993 ◽  
Vol 13 (5) ◽  
pp. 781-788 ◽  
Author(s):  
M. Aoki ◽  
K. Abe ◽  
J. Kawagoe ◽  
S. Nakamura ◽  
K. Kogure
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Gene ◽  
Peak Time ◽  
Hsp70 Mrna ◽  
Mrna Induction ◽  
Hsp70 Protein ◽  
Morphological Studies ◽  
Shock Gene ◽  
Heat Shock Gene Expression

To evaluate the mechanism of tolerance to ischemia, inductions of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs in gerbil hippocampus were compared with in situ hybridization between cases of a single 3.5-min period of forebrain ischemia and a 3.5-min period of ischemia 2 days after 2-min pretreatment with ischemia. Immunohistochemistry for HSP70 protein and morphological studies were also performed in the same brains up to 7 days after the reperfusion. Following a single 3.5-min period of ischemia, HSP70 and HSC70 mRNAs were induced in all hippocampal cells. However, the hippocampal CA1 cells produced only a minimum of HSP70 protein, and the cells were almost lost by 7 days. Following 3.5 min of ischemia after 2-min pretreatment, large populations of the CA1 cells survived at 7 days. The peak time of the HSP70 and HSC70 mRNA induction shifted to an earlier period of reperfusion in all hippocampal cells as compared with the case of a single episode of ischemia. The peak of HSP70 and HSC70 mRNA induction shifted from 1 day to 3 h in the CA1 cells. The CA1 cells produced strongly immunoreactive HSP70 from 3 hr to 2 days. These results suggest that pretreatment with an initial period of ischemia (for 2 min) accelerated HSP70 and HSC70 gene expression at the transcriptional level, ameliorated the translational disturbance of HSP70 mRNA to protein, and saved the CA1 cells from subsequent lethal ischemia (for 3.5 min). These changes of heat shock gene expression might play important roles in the acquisition of ischemic tolerance of hippocampal CA1 neurons.

Role of the S' mRNA leader in heat shock gene expression in yeast

1991 ◽  
Vol 19 (3) ◽  
pp. 280S-280S ◽  
Author(s):  
ALAN D. HARTLEY ◽  
BIRGIT GIRSTEL ◽  
JOHN E. G. McCARTHY ◽  
MICK F. TUITE
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Gene ◽  
Shock Gene ◽  
Heat Shock Gene Expression
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