Ethanol-induced tolerance to heat and to adriamycin

Li, Gloria C.; Hahn, George M.

doi:10.1038/274699a0

Cited by 194 publications

(56 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In low doses, ethanol might serve a signaling role by specifically altering the physiology of the bacterial cells. It has long been known that ethanol can induce thermotolerance in yeast and mammals (24,31), and we reason that ethanol may similarly induce tolerance of other stresses in Acinetobacter.…”

Section: Resultsmentioning

confidence: 90%

Microbial Synergy via an Ethanol-Triggered Pathway

Smith

Etages

Snyder

2004

Molecular and Cellular Biology

121

View full text Add to dashboard Cite

We have discovered a microbial interaction between yeast, bacteria, and nematodes. Upon coculturing, Saccharomyces cerevisiae stimulated the growth of several species of Acinetobacter, including, A. baumannii, A. haemolyticus, A. johnsonii, and A. radioresistens, as well as several natural isolates of Acinetobacter. This enhanced growth was due to a diffusible factor that was shown to be ethanol by chemical assays and evaluation of strains lacking ADH1, ADH3, and ADH5, as all three genes are involved in ethanol production by yeast. This effect is specific to ethanol: methanol, butanol, and dimethyl sulfoxide were unable to stimulate growth to any appreciable level. Low doses of ethanol not only stimulated growth to a higher cell density but also served as a signaling molecule: in the presence of ethanol, Acinetobacter species were able to withstand the toxic effects of salt, indicating that ethanol alters cell physiology. Furthermore, ethanol-fed A. baumannii displayed increased pathogenicity when confronted with a predator, Caenorhabditis elegans. Our results are consistent with the concept that ethanol can serve as a signaling molecule which can affect bacterial physiology and survival.

show abstract

Section: Resultsmentioning

confidence: 90%

Microbial Synergy via an Ethanol-Triggered Pathway

Smith

Etages

Snyder

2004

Molecular and Cellular Biology

121

View full text Add to dashboard Cite

show abstract

“…Increased expression of HSPs 27, 70 and 90 renders tumor cells more resistant to various cytotoxic agents including camptothecin, etoposide and actinomycin D [66][67][68][69][70]. Transfection of human cancer cell lines with hsp27 increased cell resistance to cisplatin, doxorubicin and etoposide but not to 5-fluorouracil nor to nitrosoureas [71][72][73].…”

Section: Drug Induced Cell Death and The Effector Phase Of Apoptosismentioning

confidence: 99%

New insights into the kinetic resistance to anticancer agents

Chauffert

Dimanche‐Boitrel

Garrido

et al. 1998

Multiple Drug Resistance in Cancer 2

View full text Add to dashboard Cite

Kinetic resistance plays a major role in the failure of chemotherapy towards many solid tumors. Kinetic resistance to cytotoxic drugs can be reproduced in vitro by growing the cells as multicellular spheroids (Multicellular Resistance) or as hyperconfluent cultures (Confluence-Dependent Resistance). Recent findings on the cell cycle regulation have permitted a better understanding why cancer cells which arrest in long quiescent phases are poorly sensitive to cell-cycle specific anticancer drugs. Two cyclin-dependent kinase inhibitors (CDKI) seem particularly involved in the cell cycle arrest at the G1 to S transition checkpoint: the p53-dependent p21 cip1 protein which is activated by DNA damage and the p27 kip1 which is a mediator of the contact inhibition signal. Cell quiescence could alter drug-induced apoptosis which is partly dependent on an active progression in the cell cycle and which is facilitated by overexpression of oncogenes such as c-Myc or cyclins. Investigations are yet necessary to determine the influence of the cell cycle on the balance between antagonizing (bcl-2, bcl-X L ...) or stimulating (Bax, Bcl-X S , Fas...) factors in chemotherapy-induced apoptosis. Quiescent cells could also be protected from toxic agents by an enhanced expression of stress proteins, such as HSP27 which is induced by confluence. New strategies are required to circumvent kinetic resistance of solid tumors: adequate choice of anticancer agents whose activity is not altered by quiescence (radiation, cisplatin), recruitment from G1 to S/G2 phases by cell pretreatment with alkylating drugs or attenuation of CDKI activity by specific inhibitors.

show abstract

“…Lenses of 10-d-old rats were incubated in 0.5 ml complete minimum essential medium supplemented with either L-azetidine-2-carboxylic acid (5 mM; Serva Fine Biochemicals Inc., Garden City Park, NY; 12 h incubation at 37'C) (47), sodium arsenite ( 150 ~M; 1 h at 37"C) (19), zinc chloride (500 #M; l h at 37"C) (12), ethanol (6%; 1 h at 37"C) (22), or calcium chloride (6 raM, 24 h at 4"C) (14). Incubation with calcium ionophore A23187 (7 zM; Eli Lilly Co., Indianapolis, IN; l0 h at 37"C) (21) was carried out in 0.5 ml minimum essential medium containing l0 t~Ci [3~S]methionine.…”

Section: Other Stress Conditionsmentioning

confidence: 99%

Heat shock response of the rat lens.

Jong¹,

Hoekman²,

Mulders³

et al. 1986

The Journal of Cell Biology

View full text Add to dashboard Cite

Abstract. The sequence relationship between the small heat shock proteins and the eye lens protein acrystallin (Ingolia, T. D., and E. E. Craig, 1982, Proc. Natl. Acad. Sci. USA, 79:2360-2364 prompted us to subject rat lenses in organ culture to heat shock and other forms of stress. The effects on protein synthesis were followed by labeling with [35S]methionine and analysis by one-and two-dimensional gel electrophoresis and fluorography. Heat shock gave a pronounced induction of a protein that could be characterized as the stress protein SP71. This protein probably corresponds to the major mammalian heat shock protein hsp70. Also two minor proteins of 16 and 85 kD were induced, while the synthesis of a constitutive heat shock-related protein, P73, was considerably increased. The synthesis of SP71 started between 30 and 60 min after heat shock, reached its highest level after 3 h, and had stopped again after 8 h. In rat lenses that were preconditioned by an initial mild heat shock, a subsequent shock did not cause renewed synthesis of SP71. This effect resembles the thermotolerance phenomenon observed in cultured cells. The proline analogue azetidine-2-carboxylic acid, zinc chloride, ethanol, and calcium chloride did not, under the conditions used, induce stress proteins in the rat lens. Sodium arsenite, however, had very much the same effects as heat shock. Calcium ionophore A23187 specifically and effectively induced the synthesis of the glucose-regulated protein GRP78. No special response to stress on crystallin synthesis was noticed.T HE heat shock response of eukaryotic cells is characterized by the induction of a specific set of heat shock or stress proteins, and the concurrent development of thermotolerance, i.e., increased resistance to subsequent stress (34,42). It has been shown that also in vivo and in organ culture several mammalian tissues respond to heat shock or other forms of stress by the synthesis of one or more heat shock proteins (5-7, 9, 10, 28).A study of the effects of stress on the vertebrate eye lens is of interest for a number of reasons. The eye lens might be expected to need a very efficient protection or resistance against chemical and physical insults, because the differentiated lens fiber cells are never broken down or replaced (3, 11), and hence have to maintain a reasonable degree of structural and functional integrity throughout life. On the other hand the lens is quite likely to become exposed to stressful conditions because of its superficial location in combination with the absence of direct blood supply and innervation which hampers an efficient and rapid homeostatic regulation of the intraceUular environment. Moreover, the older lens fiber cells loose their nuclei and ribosomes (3) and hence the ability to respond to stress by the synthesis of heat shock proteins. Chronic exposure of the lens to elevated temperatures induces cortical cataracts (39).Also the intriguing structural relationships between the heat shock proteins and the lens-specific crystallins make a study of ...

show abstract

Ethanol-induced tolerance to heat and to adriamycin

Cited by 194 publications

References 12 publications

Microbial Synergy via an Ethanol-Triggered Pathway

Microbial Synergy via an Ethanol-Triggered Pathway

New insights into the kinetic resistance to anticancer agents

Heat shock response of the rat lens.

Contact Info

Product

Resources

About