PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 12198405

Brain catalase inhibition blocks ethanol-related decrease of blood luteinizing hormone levels in mice.

Carles Sanchis-Segura·Carlos M G Aragon
View original source ↗Export metadata ↓

Abstract

BACKGROUND: It has been demonstrated that ethanol decreases blood luteinizing hormone (LH) levels in rodents. This effect seems to be produced by the capacity of ethanol to release beta-endorphins from the hypothalamic arcuate nucleus and, in a second step, by a mu-receptor-mediated inhibitory effect of these peptides on hypothalamic LH-releasing hormone-synthesizing neurons. However, it has been reported that, in primary hypothalamic cultures, the ethanol-produced beta-endorphin release is mediated by the enzyme catalase. Therefore, the aim of this study was to assess whether catalase inhibition modifies ethanol effects on blood LH levels. METHODS: Swiss albino mice were pretreated with the catalase inhibitor 3-amino-1,2,4-triazole (AT; 0.0-0.5 g/kg) and, 3.5 hr later, saline, ethanol (2.5 g/kg), or morphine (30 mg/kg) was administered. Blood samples were collected 2 hr after ethanol administration, and LH levels were immunoenzymatically assayed. RESULTS: The catalase inhibitor AT dose-dependently blocked the ethanol-produced decrease in blood LH levels without altering those observed after saline or morphine administration. This effect was highly correlated with the decrease in brain catalase activity produced by AT. CONCLUSIONS: These results show an antagonistic effect between AT and ethanol on blood LH levels and suggest a role of brain catalase activity on this effect of ethanol. Data are discussed in terms of a possible functional relationship between brain catalase and beta-endorphins in the mediation of some of the psychopharmacological consequences observed after ethanol administration.

Explore related subjects

AmitroleAnimalsBrainCatalaseDose-Response Relationship, DrugEnzyme InhibitorsEthanolLuteinizing HormoneMaleMiceJournal ArticleResearch Support, Non-U.S. Gov't

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Carles Sanchis-Segura, Carlos M G Aragon. 2002. Brain catalase inhibition blocks ethanol-related decrease of blood luteinizing hormone levels in mice.. https://doi.org/10.1097/01.alc.0000024268.72859.76

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Antioxidant enzyme inhibitors enhance peroxynitrite-induced cell death in U937 cells.

Peroxynitrite, a potent physiological inorganic toxin, is known to play a critical role in cellular oxidative damage. The protective role of antioxidant enzymes against peroxynitrite-induced oxidative damage in U937 cells was investigated in control and cells pre-treated with diethyldithiocarbamic acid, aminotriazole, and oxlalomalate, specific inhibitors of superoxide dismutase, catalase, and NADP(+)-dependent isocitrate dehydrogenase, respectively. Upon exposure to 1 mM 3-morpholinosydnomine N-ethylcarbamide (SIN-1), a generator of peroxynitrite through the reaction between nitric oxide and superoxide anion, to U937 cells, the viability was lower and the protein oxidation, lipid peroxidation and oxidative DNA damage reflected by an increase in 8-hydroxy-2'-deoxyguanosine, were higher in the inhibitor-treated cells as compared to the control cells. We also observed the significant increase in the endogenous production of reactive oxygen species, as measured by the oxidation of 2'7'-dichlorodihydrofluorescin as well as the significant decrease in the intracellular GSH level in the inhibitor-treated U937 cells upon exposure to SIN-1. These results suggest that antioxidant enzymes play an important role in cellular defense against peroxynitrite-induced cell death.

Amitrole↗
PubMed2006

Oxidative stress impairs heme detoxification in the midgut of the cattle tick, Rhipicephalus (Boophilus) microplus.

In the cattle tick Rhipicephalus (Boophilus) microplus digestion of blood is intracellular, accomplished by the so-called digest cells that fill the midgut lumen. Hydrolysis of hemoglobin in the digestive vesicles of these cells results in the release of large amounts of heme, a pro-oxidant compound, whose iron atom, together with H(2)O(2), may participate in the Fenton reaction and lead to the production of hydroxyl radicals. Here, we investigated the role of catalase, an enzyme responsible for H(2)O(2) detoxification. Fully engorged female ticks injected with 3-amino-1,2,4-triazole (AT), a catalase inhibitor, showed increased H(2)O(2) in the gut, together with diminished life span and lower egg-laying rates. Increased mortality observed upon AT injection was reversed by further injection of exogenous catalase, 2 days after AT treatment, confirming that increased death was due to inhibition of this enzyme by AT. In primary cultures of digest cells, intracellular H(2)O(2) is limited to specific organelles, while treatment with AT in vitro resulted in increased H(2)O(2) spreading all over the cell, confirming the role of catalase in regulating H(2)O(2) levels. Ticks fed on a calf that had been injected with AT showed marked inhibition of catalase activity in the gut and diminished life span, oviposition and engorgement. Digest cells of these ticks had an altered morphology, showing heme spread all over the cytosol, instead of being limited to the hemosomes. The amount of aggregated heme found in isolated hemosome was also strongly decreased in AT-treated cattle. All together, our results indicate that catalase performs an important role in the control of redox balance in R. microplus, which dramatically affects hemosome formation and stability. This enzyme may be a target in the development of new methods for tick control.

Amitrole↗
PubMed2006

Relationship between glutathione S-transferase, catalase, oxygen consumption, lipid peroxidation and oxidative stress in eggs and larvae of Boophilus microplus (Acarina: Ixodidae).

Glutathione S-transferases (GSTs) are enzymes that act in excretion of physiologic and xenobiotic substances, protecting cells against chemical toxicity and stress. In this work, we characterized the enzymatic activity of GST in eggs and larvae of cattle tick Boophilus microplus, on different days after oviposition and eclosion. The results showed that the GST activity varied depending on the time elapsed after oviposition and eclosion. Molecules involved in mechanism of protection from oxidative stress are correlated with the increase in GST activity. The oxygen consumption kinetics showed a positive correlation with the increase in GST activity during embryogenesis. A high content of thiobarbituric acid reactive substances were observed in egg and larva extracts, indicating that ticks face high oxidative stress during embryogenesis and aging. In eggs and larvae, GST activity can be correlated to kinetic parameters of oxidative stress such as catalase and glutathione. In addition, GST activity showed strong positive correlation with lipid peroxidation, an indication that it plays a role in oxidant defences in eggs.

Amitrole↗