AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress

Bochner, Barry R.; Lee, Philip C.; Wilson, Scott W.; Cutler, Christine W.; Ames, Bruce N.

doi:10.1016/0092-8674(84)90318-0

Cited by 294 publications

(185 citation statements)

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“…Therefore, it would appear that organisms might respond in part in a similar fashion to heat and oxidative stress. Additional evidence in support of this hypothesis comes from the observation that a variety of oxidative stresses as well as heat shock induce in bacteria the rapid accumulation of alarmones (4,10,19). A relationship between oxidative stress and heat shock response can be found in the report that Neurospora crassa induces higher levels of peroxidase upon exposure to hyperthermal conditions (9).…”

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confidence: 82%

“…However, the appearance of heat shock proteins is not confined to thermal stress conditions. Oxidative stress, either in the form of exposure of cells to oxygen after brief anaerobiosis or the exposure to substrates which generate active oxy-intermediates, also elicits the synthesis of many heat shock proteins (4,6,10,19). Therefore, it would appear that organisms might respond in part in a similar fashion to heat and oxidative stress.…”

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confidence: 99%

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Elevation of superoxide dismutase in Halobacterium halobium by heat shock

Begonia

Salin

1991

J Bacteriol

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Exposure of Halobacterium halobium to 50°C for 2.5 h in an aerobic environment resulted in a greater than twofold increase in the activity of the manganese-containing superoxide dismutase. Nondenaturing polyacrylamide gels stained for enzymatic activity did not reveal any additional isozymes of superoxide dismutase induced by the heat shock. The maximal effect was observed at 50°C, and the elevated levels of activity remained constant during 5 h of recovery at 40°C. The induction of enzymatic activity was sensitive to protein synthesis inhibitors. The results are discussed relative to heat shock and stress-related proteins as well as alterations in metabolism brought about by elevated temperatures.Following exposure to elevated temperatures, many organisms rapidly synthesize a highly conserved set of proteins termed heat shock proteins (19). Enhanced synthesis of heat-shock proteins has been found in eubacteria and archaebacteria as well as eukaryotes (1,7,20), and their induction appears to correlate with the organism's adaptation to hyperthermal stress (1,19). However, the appearance of heat shock proteins is not confined to thermal stress conditions. Oxidative stress, either in the form of exposure of cells to oxygen after brief anaerobiosis or the exposure to substrates which generate active oxy-intermediates, also elicits the synthesis of many heat shock proteins (4,6,10,19). Therefore, it would appear that organisms might respond in part in a similar fashion to heat and oxidative stress. Additional evidence in support of this hypothesis comes from the observation that a variety of oxidative stresses as well as heat shock induce in bacteria the rapid accumulation of alarmones (4,10,19). A relationship between oxidative stress and heat shock response can be found in the report that Neurospora crassa induces higher levels of peroxidase upon exposure to hyperthermal conditions (9). Finally, a recent report by Privalle and Fridovich (16) (14). Culture flasks were shaken at 150 rpm in a water bath maintained at 40°C. At the middle of the log phase of growth, flasks were removed and transferred to a water bath set at 500C or another designated temperature. After shaking at 150 rpm for 2.5 h at the designated temperature, the flasks were removed and placed once more in the shaking water bath set at 400C. Cells were then allowed to recover for an additional 5 h. Where indicated, various concentrations of inhibitors were added to the culture medium just prior to the initiation of the heat shock. For experiments on cells in still culture, flasks were maintained in a water bath set at 40°C. After the cells reached mid-log phase, the culture flasks were transferred to a 50°C water bath and were maintained there for an additional 2.5 h. Thereafter, the cultures were allowed to recover in a 40°C water bath for 3 h.Aliquots (50 ml) of each culture were taken at the initiation of heat treatment, after the termination of heat treatment, and during phases of recovery. Cells were spun at 7,500 x g for 15 min at 40C and was...

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confidence: 82%

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Elevation of superoxide dismutase in Halobacterium halobium by heat shock

Begonia

Salin

1991

J Bacteriol

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“…Several studies have illustrated a key role for HMOX1 in promoting cell survival during inflammation, and HMOX1 expression has multiple functions in smoking-mediated lung cancers. 20,[62][63][64][65] Because HMOX1 promotes cell proliferation and increases resistance to oxidative stress, overexpression of HMOX1 imparts a selective advantage to cells in the early stages of carcinogenesis and correlates with resistance to many chemotherapeutics in malignancy. 20,29,31,56 Thus, our data link loss of Fhit to a key pathway in the establishment and maintenance of the malignant state.…”

Section: Discussionmentioning

confidence: 99%

“…61 Indeed, the intracellular concentration of ApppA increases in cells exposed to oxidative stressors. [62][63][64][65] Because mutation of the Fhit enzyme active site histidine residue greatly retards ApppA cleavage without a strong effect on ApppA binding or proapoptotic activity After knockdown, cells were exposed to 1% CSE for 4 hours. Hmox1 protein abundance was assessed by western blot.…”

Section: Discussionmentioning

confidence: 99%

A knockdown with smoke model reveals FHIT as a repressor of Heme oxygenase 1

Boylston

Brenner²

2014

Cell Cycle

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Fragile histidine triad (FHIT) gene deletions are among the earliest and most frequent events in carcinogenesis, particularly in carcinogen-exposed tissues. Though FHIT has been established as an authentic tumor suppressor, the mechanism underlying tumor suppression remains opaque. Most experiments designed to clarify FHIT function have analyzed the consequence of re-expressing FHIT in FHIT-negative cells. However, carcinogenesis occurs in cells that transition from FHIT-positive to FHIT-negative. To better understand cancer development, we induced FHIT loss in human bronchial epithelial cells with RNA interference. Because FHIT is a demonstrated target of carcinogens in cigarette smoke, we combined FHIT silencing with cigarette smoke extract (CSE) exposure and measured gene expression consequences by RNA microarray. The data indicate that FHIT loss enhances the expression of a set of oxidative stress response genes after exposure to CSE, including the cytoprotective enzyme heme oxygenase 1 (HMOX1) at the RNA and protein levels. Data are consistent with a mechanism in which Fhit protein is required for accumulation of the transcriptional repressor of HMOX1, Bach1 protein. We posit that by allowing superinduction of oxidative stress response genes, loss of FHIT creates a survival advantage that promotes carcinogenesis.

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“…The induction of HPI protein was shown to occur at the transcriptional level (Morgan et al, 1986) with oxyRl mutants containing 5Ox the norrnl level of HPI mRNA. Morgan et al (1986) (Bochner et al, 1984;Lee et al, f983). These dinucleotides have been termed alarrÐnes (Stephens et al, 1975) (Teo et al,1986).…”

Section: List Of Figures Pagementioning

confidence: 99%