Disease relevance of Propenol

• Mice of the alcohol dehydrogenase-negative (AdhN) strain which lack alcohol dehydrogenase activity were resistant to allyl alcohol toxicity [1].
• Treatment of 1 with allyl alcohol gave a C(3)S(2) five-membered ring complex, [[Ru(P(OCH(3))(3))(2)(CH(3)CN)(3)](2)[mu-SCH(2)CH(2)CH(OCH(2)CH=CH(2))S]](CF(3)SO(3))(4) (2), via C-S bond formation after C-H bond activation and intermolecular dehydration [2].
• METHODS: Rats fasted for 12 h received acetaminophen 3.5 or 5.6 g per kg body weight, or allyl alcohol 100 or 125 microl by gastric tube, doses producing no and about 30% mortality, respectively, within 2 days [3].
• Thus, the allyl alcohol-induced hemolysis appears to be a model for iron delocalization from iron stores [4].
• Mutants of Escherichia coli resistant to allyl alcohol were selected [5].

Psychiatry related information on Propenol

• When intracellular calcium concentrations were measured directly, using fura-2 as the calcium indicator, there was no effect of allyl alcohol on cytosolic free calcium during the first 60 min of exposure, a critical period for development of irreversible damage [6].

High impact information on Propenol

• And second, ADH1- pollen grains survive allyl alcohol (C=C-C-OH) vapour concentrations which kill ADH1+ grains; this selection scheme was developed for yeast by Megnet [7].
• A chemical perfusion mixture of allyl alcohol and glutaraldehyde was used to fix the acetylcholine in the nervous tissue [8].
• Liver progenitor cells (LPCs) cloned from adult rat livers following allyl alcohol injury express hematopoietic stem cell and early hepatic lineage markers when cultured on feeder layers; under these conditions, neither mature hepatocyte nor bile duct, Ito, stellate, Kupffer cell, or macrophage markers are detected [9].
• Participation of small intraportal stem cells in the restitutive response of the liver to periportal necrosis induced by allyl alcohol [10].
• This new method was combined with standard procedures to monitor parenchymal cell function (e.g., oxygen uptake and release of lactate dehydrogenase), Kupffer cell phagocytic activity and parenchymal cell injury simultaneously during perfusion with the hepatotoxicant allyl alcohol [11].

Chemical compound and disease context of Propenol

• Characterization of a Pseudomonas putida allylic alcohol dehydrogenase induced by growth on 2-methyl-3-buten-2-ol [12].
• The treatment of mice with desferrioxamine after allyl alcohol intoxication completely prevents lipid peroxidation and hemolysis, suggesting the involvement of iron in the allyl alcohol-induced erythrocyte damage [4].
• Allyl alcohol exerted a dose-dependent toxicity on the cells which was inversely related to cellular glutathione (GSH) content and accordingly influenced by stimulation as well as inhibition of GSH synthesis [13].
• The effect of aldehyde dehydrogenase inhibition on allyl alcohol toxicity was determined by pretreating rats with cyanamide or disulfiram prior to treatment with allyl alcohol [14].
• An inhibitor of alcohol dehydrogenase, pyrazole, prevented both the toxicity of allyl alcohol and the rapid depletion of GSH [15].

Biological context of Propenol

• Effect of pd nanoparticle size on the catalytic hydrogenation of allyl alcohol [16].
• The active sites of supported gold catalysts, favoring the adsorption of C=O groups of acrolein and subsequent reaction to allyl alcohol, have been identified as edges of gold nanoparticles [17].
• Cytosolic metabolism of allyl alcohol also leads, in a dose-dependent manner, to extensive lipid peroxidation [18].
• What distinguishes these mutants from other temperature-sensitive mutants is that the temperature-conditional growth phenotypes described here must be due to interactions between allyl alcohol levels and ADHI functional properties and cannot be due to lability of the enzyme at the restrictive temperature [19].
• Unlike previous work with this this system using haploid strains, the NAD+/NADH ratios show no negative correlation with allyl alcohol resistance [20].

Anatomical context of Propenol

• To determine the involvement of different hepatocyte populations in response to periportal injury, the restitutive response to allyl alcohol (AA) injury was examined [10].
• Hepatocellular injury was produced by pretreatment of rats with allyl alcohol or carbon tetrachloride; ligation of the bile duct simulated obstructive biliary disease [21].
• Thirty minutes after the i.p. injection of a necrogenic dose of allyl alcohol in vivo, the concentrations of allyl alcohol in the portal vein and vena cava were 1210 and 530 microM, respectively [22].
• Studies carried out with reconstituted systems of erythrocyte lysates, containing ghosts and different fractions of erythrocyte cytosol and incubated in the presence of acrolein (the major metabolite of allyl alcohol), strongly suggest that iron is released from hemoglobin [4].
• In vivo administration of allyl alcohol did not reduce the GSH dependent protection of the microsomes [23].

Associations of Propenol with other chemical compounds

• Single necrogenic doses of CCl4, allyl alcohol (AA), and alpha-naphthylisothiocyanate (ANIT) were used to produce cell specific injury in centrilobular hepatocytes, periportal hepatocytes, and bile duct cells, respectively [24].
• From the interdependence between the twix/twin regioselectivity and the threo/erythro diastereoselectivity, it has been recognized that the enophile also attacks the allylic alcohol from the erythro pi face without assistance by hydrogen bonding with the allylic hydroxy functionality [25].
• 4-Methylpyrazole (80 microM), an inhibitor of alcohol dehydrogenase, prevented the fluorescence increase due to allyl alcohol in both regions, indicating that the changes were due entirely to NADH generated from alcohol dehydrogenase-dependent allyl alcohol metabolism [22].
• Aldose reductase (EC 1.1.1.21), a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of acrolein to allyl alcohol (Km = 80 microM, kcat = 87 min-1) [26].
• The mRNA of the urea cycle enzymes and glutamine synthetase was uniformly reduced by allyl alcohol, whereas that of most urea cycle enzymes was above the controls after the non-lethal, but not after the sub-lethal, dose of acetaminophen [3].

Gene context of Propenol

• Here we report an example of overdominance that is temperature- and allyl alcohol-dependent and due to heterozygosity at the ADH1 locus, involving two ADHI functional mutants [20].
• Selection for resistance to allyl alcohol in respiration-incompetent Saccharomyces cerevisiae produces a high proportion of mutants that can be localized within the ADH2 structural gene and that still, because of the type of selection employed, retain enzyme activity [27].
• Allyl alcohol administration increased serum ALT activity but had no effect on GGT activity [24].
• The COX-2 product prostaglandin D(2) (PGD(2)) increases hepatocyte killing by allyl alcohol in vitro [28].
• Hepatotoxicity due to allyl alcohol in deermice depends on alcohol dehydrogenase [1].

Analytical, diagnostic and therapeutic context of Propenol

• METHODS: Periportal liver injury in rats was induced by intraperitoneal injection of allyl alcohol [29].
• For a variety of reasons, these mutants are even more favorable subjects for population genetic analysis and the dissection of molecular microevolution than are allyl alcohol-resistant mutants [27].
• FTIR studies of iron-carbonyl intermediates in allylic alcohol photoisomerization [30].
• The pattern of hepatocellular metabolism of allyl alcohol was monitored by high-pressure liquid chromatography (HPLC) analysis [13].
• Quantitative determination of allyl alcohol and its toxic metabolite, acrolein, was performed using headspace gas chromatography with flame-ionization detection [31].

References