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Induction of enzymes of the glycerophosphate pathway in leu-5 mutants of Neurospora crassa.

The inducible cytosolic glycerokinase and mitochondrial glycerol-3-phosphate dehydrogenase have been examined during the glycerol-specific induction in Neurospora crassa. Although both the fully induced levels and the respective rates of synthesis of these two enzymes were less than observed with wild-type cells, there were no major differences in the relative rates of induction of the glycerol-3-phosphate dehydrogenase at either permissive or restrictive temperatures. These results indicate that the processes involved in the assembly of this enzyme into the mitochondrial inner membrane are normal in a mutant lacking the mitochondrial leucyl tRNA synthetase and suggest that the functions of the mitochondrial synthetase may be replaced by those of the cytosolic leucyl tRNA synthetase.

Amino Acyl-tRNA Synthetases↗

Effect of hepatic cytochrome P-450 inducing agents on mutagen activity in the host-mediated assay.

Intraperitoneal treatment of female BALB/c mice with either phenobarbitone or beta-naphthoflavone led to the induction of various hepatic enzymes associated with xenobiotic metabolism and to increased abilities of hepatic S9 fractions to convert the dietary carcinogen 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline (MeIQx) to an active bacterial mutagen. In the case of another carcinogen, aflatoxin B1 an increase in in vitro hepatic activation was seen only in mice treated with phenobarbitone. In contrast, pretreatment with either phenobarbitone or beta-naphthoflavone reduced the in vivo activity of both aflatoxin B1 and MeIQx in the host mediated bacterial mutation assay. These data indicate that, for some carcinogens at least, the host-mediated assay may be used to predict the carcinogenic consequences of hepatic enzyme induction.

Aflatoxins↗

Uterine peroxidase as a marker for estrogen action.

Administration of a single dose of estradiol to immature rats gives rise to the appearance of substantial amounts of peroxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) enzyme activity in the uterus. This enzyme induction, which is inhibited by administration of actinomycin D and cycloheximide, can be detected at 4 hr after administration of estradiol, reaches a maximum level by 20 hr, and thereafter declines. The amount of uterine peroxidase seen at 20 hr after a single dose increases with dose from 0.1 to 100 microgram of estradiol. Estrone and estriol also show dose-dependent induction of peroxidase, and the quantitative peroxidase responses to these steroids follow their uterotropic capacities. The antiestrogen CI628, capable of low levels of enzyme induction by itself, can inhibit the induction due to estrogen. Solubilization of the uterine enzyme with divalent cations, especially calcium, results in a substantially increased yield of peroxidase. This extraction method provides an enzyme of about 50,000 molecular weight in distinction to the large aggregated form obtained by the usual extraction with sodium chloride.

Animals↗

The influence of chronic administration of hypnotics and analgesics on rate of recovery from inhalation anesthesia in rats.

A series of groups of Sprague-Dawley rats were given either secobarbital, phenobarbital, morphine, pentazocine, diazepam, methotrimeprazine, or saline (control) intraperitoneally on 4 consecutive days and then, on day 5, anesthetized with chloroform, trichlorethylene, fluroxene, halothane, methoxyflurane, enflurane, isoflurane, bromotrifluorocyclobutane, or chlorotrifluorocyclobutane. One control group received neither pretreatment nor anesthetics and another was given pretreatment but no anesthetics. The factor of "enzyme induction" is also evaluated, as are SGPT elevation and liver and kidney lesions. If enzyme induction occurred with the drugs used for pretreatment, the anesthetics suppressed the expected response. SGPT levels were generally within normal range. The combinations of all pretreatments with enflurane, halothane, or methoxyflurane had the fastest recovery; recovery was slower with the other anesthetic agents, but none of the prior chemotherapeutic drugs accelerated recovery from the inhalation anesthetics.

Alanine Transaminase↗

Catabolite repression of induction of aldose reductase activity and utilization of mixed hemicellulosic sugars in Candida guilliermondii.

NADPH-dependent aldose reductase activity induced by D-xylose or L-arabinose was detected in cell-free extracts of Candida guilliermondii, but only negligible activities were observed if D-glucose served as carbon source. The induction of aldose reductase activity on mixed sugars was investigated under resting cell conditions. D-Glucose repressed enzyme induction by D-xylose or L-arabinose to varying degrees, and L-arabinose inhibited enzyme induction by D-xylose. During incubation in a mixture of D-xylose-D-glucose, glucose consumption by cells was fast and simultaneous with D-xylose utilization. Repression of D-xylose consumption by D-glucose was dependent on hexose initial concentration. L-arabinose consumption was poor when it was present as the only sugar and in a mixture with D-glucose; this pentose depletion occurred only when all hexose was consumed. When D-xylose and L-arabinose were present in a mixture, the consumption of both pentoses was reduced by the presence of the second sugar, although both sugars were consumed simultaneously by cells. The results show that induction of aldose reductase activity and D-xylose utilization by cells of Candida guilliermondii are under control of glucose repression.

Aldehyde Reductase↗

Induction of glutathione transferases and NAD(P)H:quinone reductase by fumaric acid derivatives in rodent cells and tissues.

Dimethyl fumarate and dimethyl maleate are potent inducers of cytosolic NAD(P)H:(quinone acceptor) oxidoreductase (here designated quinone reductase) activity in Hepa 1c1c7 murine hepatoma cells in culture, whereas fumaric and maleic acids are much less potent, in agreement with the much greater reactivity of the esters as Michael reaction acceptors (P. Talalay, M. J. De Long, and H. J. Prochaska, Proc. Natl. Acad. Sci. USA, 85:8261-8265, 1988). Dimethyl fumarate also induced quinone reductase in mutants of the Hepa 1c1c7 cell line that were either defective in the Ah receptor or in cytochrome P1-450 activity, thereby establishing that this compound is a monofunctional inducer (H. J. Prochaska and P. Talalay, Cancer Res., 48: 4776-4782, 1988). Addition of dimethyl fumarate to the diet of female CD-1 mice and female Sprague-Dawley rats at 0.2-0.5% concentrations elevated cytosolic glutathione transferases and quinone reductase activities in a variety of organs, whereas much higher concentrations of fumaric acid were only marginally active. The widespread induction of such detoxication enzymes by dimethyl fumarate suggests the potential value of this compound as a protective agent against chemical carcinogenesis and other forms of electrophile toxicity. This proposal is supported by the finding that the concentrations of dimethyl fumarate required to obtain substantial enzyme inductions were well tolerated by rodents. Furthermore, the parent fumaric acid has low chronic toxicity and is a naturally occurring metabolic intermediate that is already in the food chain as an additive, and fumarate salts and esters are used for therapeutic purposes in man.

Animals↗

Effects of Eleutherococcus senticosus extracts on hexobarbital metabolism in vivo and in vitro.

Eleutherococcus senticosus (Siberian Ginseng) is widely exported from China as a health food. Pharmacologically it has been classified as an adaptogen and enzyme induction has been proposed as its mechanism of action. To evaluate this hypothesis E. senticosus was administered to mice on an acute (40-320 mg/kg i.p., X 1 day) or chronic (80-320 mg/kg i.p., X 4-5 days) basis. Sleep latency and duration, in response to hexobarbital sodium (100 mg/kg i.p.), were determined either 1 h (acute and chronic) or 24 h (chronic) following the last E. senticosus injection. E. senticosus produced a sedative effect which decreased the sleep latency (47%) and increased sleep duration (45-228%) following acute administration. A similar effect was seen following chronic administration (125-202% increase in sleep duration). E. senticosus was also shown to produce an inhibition (66%) of hexobarbital metabolism, in vitro, as compared to controls. These data support enzyme inhibition rather than enzyme induction as a mechanism for the actions of Siberian Ginseng.

Animals↗

Transcriptional regulation of the Kluyveromyces lactis beta-galactosidase gene.

We examined the molecular basis for beta-D-galactosidase (EC 3.2.1.23) induction in the yeast Kluyveromyces lactis. The protein synthesis inhibitor anisomycin effectively blocked both protein synthesis and enzyme induction by lactose. Further, hybridization analysis with the cloned beta-galactosidase gene indicated coordinate increases in the concentration of beta-galactosidase messenger ribonucleic acid and enzyme activity. The half-life of beta-galactosidase messenger ribonucleic acid was the same (4.8 +/- 0.4 min) when measured both before and at succeeding times during enzyme induction. These results strongly support the hypothesis that expression of the yeast beta-galactosidase gene is subject to transcriptional regulation.

Anisomycin↗

Activity of hepatic drug metabolizing enzymes following oxazepam-dosed feed treatment in B6C3F1 mice.

Oxazepam has been determined to be a potent hepatocarcinogen in mice. Evidence in the literature indicates that oxazepam is capable of inducing drug metabolizing enzymes in rodents and an association between enzyme induction and carcinogenesis has been proposed for other compounds such as phenobarbital. We examined the pattern of enzyme induction that occurs under bioassay conditions in male B6C3F1 mice. The results indicate that oxazepam is capable of inducing multiple drug metabolizing enzymes under bioassay conditions. Closer examination of the most induced samples suggests that oxazepam is a phenobarbital-type enzyme inducer.

Aminopyrine N-Demethylase↗

Fetal morphine metabolism and clearance are constant during late gestation.

Fetal metabolism significantly contributes to the clearance of drugs from the fetus. To understand how the changes in fetal metabolism expected in late gestation alter fetal drug clearance, serial measurements of morphine metabolism were made in the fetal baboon over the latter third of gestation. Clearance and metabolism were evaluated in the context of fetal growth, onset of labor, and the administration of classical enzyme induction agents. Morphine, a probe substrate for the enzyme uridine diphosphate glucuronosyltransferase 2B7 (UGT2B7), was continuously infused to chronically catheterized fetal baboons while measuring morphine, morphine-3-beta-glucuronide, and morphine-6-beta-glucuronide concentrations. In some animals, intermittent infusions of the metabolites provided estimates of metabolite clearance and, hence, the rate of formation of metabolites and metabolic clearance. Overall, metabolic clearance of morphine from the fetus was 27 +/- 9.0 ml x min(-1) or 32% of total clearance. This is similar to the overall clearance in the adult baboon when standardized to weight. No change in any measure of metabolism or clearance of morphine or its glucuronide metabolites was found with gestational age, the presence of labor, or administration of UGT enzyme induction agents. Interpreting these findings using a physiologically based approach suggests that the intrinsic clearance of the fetal liver toward morphine is of sufficient magnitude that fetal hepatic clearance is flow-limited. The implication of a high intrinsic clearance is for significant placento-hepatic first-pass metabolism when drugs are administered to the mother. The previously held view of the "inadequacy of perinatal glucuronidation" needs to be reconsidered.

Analgesics, Opioid↗

[Cytochrome P450. Its importance in toxicology. II. Regulation of its biosynthesis and its activity. Activation and inhibition].

The authors emphasize the influence of hormonal and nutritional factors on the activity level of microsomal enzymes. Induction process of hepatic cytochrome P450 and microsomal enzymes by xenobiotics are described. The existence of different types of hemoprotein P450 in response to the action of different inductors is discussed. We also propose some hypothesis concerning the action mechanism of inhibitors of microsomal enzymes and we point out the role of environmental pollutants.

Animals↗

[Co-genotoxic potential of PCB mixtures from pediatric fatty tissue].

In the present study a mixture containing the 11 PCB major components identified in fatty tissues of children was examined for its potency to enhance the toxification of pregenotoxicants (cogenotoxicity) in the liver. As a basis for the study GC/MS PCB analyses of 207 fatty tissue samples of children were used. The PCB mixture was produced on this basis. As a model for the identification of the cogenotoxic potency of the PCB mixtures an in vivo/in vitro enzyme induction assay was developed. The goal of the study was to clarify the question, whether the in vivo pretreatment of rats with a complex PCB pattern derived from children led to a synergism of cogenotoxicants and pregenotoxicants with regard to the enhancement of the in vitro toxification of benzo[a]pyrene (B[a]P) and 2-aminoanthracene (2-AA) to DNA reactive metabolites. Using the SOS-Chromotest as the in vitro part of the induction assay, all liver enzyme fractions of PCB pretreated rats (S9PCB) showed an increase of the toxification of the pregenotoxicants B[a]P and 2-AA in comparison to enzyme factions of untreated animals (S9(0)). With regard to the reactivity pattern it may be supposed that the PCB mixture probably induced cytochrome P450-dependent oxigenases of the subclasses CYP1A1 and CYP1A2. Additionally, it seems to be of interest that the use of S9(0) fractions did not lead to any or only to weak toxification of B[a]P and 2-AA. Thus, a synergism of cogenotoxicants and pregenotoxicants could be confirmed. PCB could be identified in fatty tissues of children in amounts up to 1 mg/kg. Additionally, pregenotoxicants like polycyclic aromates, mycotoxins and/or aminocontaining compounds, are available in almost all environmental sources. Therefore, from the present point of view, a genetic risk caused by PCB in humans (children) cannot be excluded.

Adipose Tissue↗

New hepatocyte in vitro systems for drug metabolism: metabolic capacity and recommendations for application in basic research and drug development, standard operation procedures.

Primary hepatocytes represent a well-accepted in vitro cell culture system for studies of drug metabolism, enzyme induction, transplantation, viral hepatitis, and hepatocyte regeneration. Recently, a multicentric research program has been initiated to optimize and standardize new in vitro systems with hepatocytes. In this article, we discuss five of these in vitro systems: hepatocytes in suspension, perifusion culture systems, liver slices, co-culture systems of hepatocytes with intestinal bacteria, and 96-well plate bioreactors. From a technical point of view, freshly isolated or cryopreserved hepatocytes in suspension represent a readily available and easy-to-handle in vitro system that can be used to characterize the metabolism of test substances. Hepatocytes in suspension correctly predict interspecies differences in drug metabolism, which is demonstrated with pantoprazole and propafenone. A limitation of the hepatocyte suspensions is the length of the incubation period, which should not exceed 4hr. This incubation period is sufficiently long to determine the metabolic stability and to allow identification of the main metabolites of a test substance, but may be too short to allow generation of some minor, particularly phase II metabolites, that contribute less than 3% to total metabolism. To achieve longer incubation periods, hepatocyte culture systems or bioreactors are used. In this research program, two bioreactor systems have been optimized: the perifusion culture system and 96-well plate bioreactors. The perifusion culture system consists of collagen-coated slides allowing the continuous superfusion of a hepatocyte monolayer with culture medium as well as establishment of a constant atmosphere of 13% oxygen, 82% nitrogen, and 5% CO2. This system is stable for at least 2 weeks and guarantees a remarkable sensitivity to enzyme induction, even if weak inducers are tested. A particular advantage of this systemis that the same bioreactor can be perfused with different concentrations of a test substance in a sequential manner. The 96-well plate bioreactor runs 96 modules in parallel for pharmacokinetic testing under aerobic culture conditions. This system combines the advantages of a three-dimensional culture system in collagen gel, controlled oxygen supply, and constant culture medium conditions, with the possibility of high throughput and automatization. A newly developed co-culture system of hepatocytes with intestinal bacteria offers the possibility to study the metabolic interaction between liver and intestinal microflora. It consists of two chambers separated by a permeable polycarbonate membrane, where hepatocytes are cultured under aerobic and intestinal bacteria in anaerobic conditions. Test substances are added to the aerobic side to allow their initial metabolism by the hepatocytes, followed by the metabolism by intestinal bacteria at the anaerobic side. Precision-cut slices represent an alternative to isolated hepatocytes and have been used fo the investigation of hepatic metabolism, hepatotoxicity, and enzyme induction. A specific advantage of liver slices is the possibility to study toxic effects on hepatocytes that are mediated or modified by nonparenchymal cells (e.g., by cytokine release from Kupffer cells) because the physiological liver microarchitecture is maintained in cultured slices. For all these in vitro systems, a prevalidation has been performed using standard assays for phase I and II enzymes. Representative results with test substances and recommendations for application of these in vitro systems, as well as standard operation procedures are given.

Animals↗

Evaluation of time-dependent cytochrome P450 inhibition using cultured human hepatocytes.

Primary human hepatocytes in culture are commonly used to evaluate cytochrome P450 (P450) induction via an enzyme activity endpoint. However, other processes can confound data interpretation. To this end, the impact of time-dependent P450 inhibition in this system was evaluated. Using a substrate-cassette approach, P450 activities were determined after incubation with the prototypic inhibitors tienilic acid (CYP2C9), erythromycin, troleandomycin, and fluoxetine (CYP3A4). Kinetic analysis of enzyme inactivation in hepatocytes was used to describe the effect of these time-dependent inhibitors and derive the inhibition parameters kinact and KI) which generally were in good agreement with the values derived using recombinant P450s and human liver microsomes (HLMs). Tienilic acid selectively inhibited CYP2C9-dependent diclofenac 4'-hydroxylation activity, and erythromycin, troleandomycin, and fluoxetine inhibited CYP3A4-dependent midazolam 1'-hydroxylation in a time- and concentration-dependent manner. Fluoxetine also inhibited CYP2C19-dependent S-mephenytoin 4'-hydroxylation in a time- and concentration-dependent manner in hepatocytes, HLMs, and recombinant CYP2C19 (KI 0.4 microM and kinact 0.5 min(-1)). As expected, the effect of fluoxetine on CYP2D6 in hepatocytes was consistent with potent yet reversible inhibition. A very weak time-dependent CYP2C9 inhibitor (AZ1, a proprietary AstraZeneca compound; KI 30 microM and kinact 0.02 min(-1)) effectively abolished CYP2C9 activity over 24 h at low (micromolar) concentrations in primary cultured human hepatocytes. This work demonstrates that caution is warranted in the interpretation of enzyme induction studies with metabolically stable, weak time-dependent inhibitors, which may have dramatic inhibitory effects on P450 activity in this system. Therefore, in addition to enzyme activity, mRNA and/or protein levels should be measured to fully evaluate the P450 induction potential of a drug candidate.

Aged↗

Differential induction of rat hepatic microsomal epoxide hydrolase and rGSTA2 by diazines: the role of cytochrome P450 2E1-mediated metabolic activation.

Previous studies have shown that pyridazine (PD) and pyrazine (PZ) are efficacious in inducing microsomal epoxide hydrolase (mEH) in the liver with elevation of the mRNA level. The present study was designed to investigate the expression of mEH and rGSTA2 genes in response to the diazines including PD, PZ and pyrimidine (PM) and the basis for their enzyme induction. Rats treated with either PD or PZ for 3 days resulted in marked increases in mEH and rGSTA2 mRNA levels with concomitant induction of the proteins, whereas PM failed to elevate the mRNA levels. Treatment of rats with a single dose of PD or PZ showed dose-dependent increases in mEH and rGSTA2 mRNA levels at 24 h with ED50 values being approximately 10 mg/kg. Time-course studies showed that the mRNA levels were increased to maximal extents at 24-48 h after treatment. Studies were extended to assess the mechanistic basis for the enzyme induction by PD and PZ. beta-Naphthoflavone (BNF) caused a 6-fold increase of rGSTA2 mRNA in the liver (100 mg/kg per day, p.o., 3 days), as compared to control, whereas the agent failed to increase mEH mRNA level. Administration of PD or PZ (50 mg/kg) to BNF-pretreated rats resulted in no enhanced increase of the mEH mRNA as compared to the individual treatment, while the rGSTA2 mRNA level was additively elevated, suggesting the possibility that increases of the mEH and rGSTA2 mRNAs by PD or PZ might be mediated with antioxidant responsive element(s) in the genes, but not with xenobiotic responsive element. Western blot analysis revealed that cytochrome P450 2E1 was induced 3- to 4-fold by both PD and PZ, whereas PM failed to induce P450 2E1. Concomitant treatment of rats with PD or PZ in combination with acetone, a substrate for P450 2E1, caused no significant increase in the mEH and rGSTA2 mRNA levels relative to that in untreated animals, whereas PD or PZ treatment without a concomitant acetone administration resulted in marked increases of the mRNAs. Diazine-inducible mEH and rGSTA2 mRNA levels were approximately 2-fold enhanced in P450 2E1-induced starved rats, as compared to those in diazine-treated unstarved animals. These data indicate that P450 2E1-mediated bioactivation of the diazines might contribute to transcriptional activation of the mEH and GST genes. These results provide evidence that both PD and PZ efficaciously induce mEH and rGSTA2 in the liver with increases in the mRNA levels, while PM is ineffective, and that induction of mEH and rGSTA2 may be mediated through bioactivation of the diazines by P450 2E1.

Acetone↗

The dynamics of single-substrate continuous cultures: the role of transport enzymes.

A chemostat limited by a single growth-limiting substrate displays a rich spectrum of dynamics. Depending on the flow rate and feed concentration, the chemostat settles into a steady state or executes sustained oscillations. The transients in response to abrupt increases in the flow rate or the feed concentration are also quite complex. For example, if the increase in the flow rate is small, there is no perceptible change in the substrate concentration. If the increase in the flow rate is large, there is a large increase in the substrate concentration lasting several hours or days before the culture adjusts to a new steady state. In the latter case, the substrate concentration and cell density frequently undergo damped oscillations during their approach to the steady state. In this work, we formulate a simple structured model containing the inducible transport enzyme as the key intracellular variable. The model displays the foregoing dynamics under conditions similar to those employed in the experiments. The model suggests that long recovery times (on the order of several hours to several days) can occur because the initial transport enzyme level is too small to cope with the increased substrate supply. The substrate concentration, therefore, increases until the enzyme level is built up to a sufficiently high level by the slow process of enzyme induction. Damped and sustained oscillations can occur because transport enzyme synthesis is autocatalytic, and hence, destabilizing. At low dilution rates, the response of stabilizing processes, such as enzyme dilution and substrate consumption, becomes very slow, leading to damped and sustained oscillations.

Bacteria↗

Analysis of marker enzymes in the K562 erythroleukaemia cell line: no coordinate expression of red cell enzymes on induction of haemoglobin synthesis.

Six sublines of the K562 erythroleukaemic cell line were examined by starch gel electrophoresis for the red cell enzymes carbonic anhydrase, CA I and II, pyruvate kinase, PK1 (R), and lactic dehydrogenase, LDH (B), both uninduced and following induction of haemoglobin synthesis with sodium butyrate or haemin. Neither CA or PK1 (R) enzymes were present constitutively found to be inducible characteristics; the LDH isoenzyme pattern showed equal expression of A and B subunits and did not change to the red cell form (B greater than A) on induction. Subline heterogeneity was also examined by analysis of a further 11 polymorphic enzymes, and cell line contamination was found not to account for the previously reported variations in inducibility by sodium butyrate.

Carbonic Anhydrases↗

Induction of plasminogen activator by alkylating agents in a repair defective human glioblastoma cell strain.

Alkylating agents, mechlorethamine and N-methyl-N'-nitro-N-nitrosoguanidine, induce the production of plasminogen activator in U-87MG cells, an alkylation DNA repair deficient (Mer-) human glioblastoma strain. Enzyme induction was not observed, however, in U-178MG and SH-101 cells, alkylation repair proficient (Mer+) glioblastoma strains, or in HeLa cells, which reactivated and supported well the growth of alkylation damaged adenovirus 3. In the alkylation repair defective U-87MG strain, enhanced production of plasminogen activator occurred in a narrow concentration range of treatment with either alkylating agent, causing a 20 to 50% inhibition of [3H]thymidine incorporation. Maximum plasminogen activator induction was observed between 32 and 48 h after alkylation treatment and the levels of enzyme produced were 5 to 10 times those of untreated control levels. This alkylation dependent enzyme induction required protein synthesis for it did not occur in the presence of cycloheximide. It was hence concluded that plasminogen activator induction in alkylation repair deficient human cells is caused by unrepaired DNA damage and that it may represent an eukaryotic SOS-like function. In addition, plasminogen activator induction may be useful as a sensitive assay for the identification of alkylation repair defective human tumors for which the susceptibility to alkylation chemotherapy should be expected to increase.

Alkylating Agents↗