| Name | monoamine oxidase |
|---|---|
| Synonyms | Adrenalin oxidase; Amine oxidase; Amine oxidase [flavin containing] B; MAO B; MAOB; Monoamine oxidase; Monoamine oxidase B; Monoamine oxidase type B… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2174585 | Medvedev AE: [Regulation by biogenic amines of energy functions of mitochondria] . Vopr Med Khim. 1990 Sep-Oct;36(5):18-21. Biogenic amines (phenylethylamine, and decreased activities of the rotenone-insensitive -cytochrome c reductase, the cytochrome c reductase and the succinate dehydrogenase in incubation mixtures containing mitochondrial membranes and the monoamine oxidase inhibitors chlorgyline and deprenyl. |
32(0,1,1,2) | Details |
| 2528539 | Levrat C, Louisot P, Morelis R: Topological investigations. J Biochem. 1989 Jul;106(1):133-8. The trypsin action on mitochondrial membrane was checked by measuring the activities of marker enzymes (rotenone-insensitive cytochrome c reductase, kinase, and monoamine oxidase). |
81(1,1,1,1) | Details |
| 10854571 | Lamensdorf I, Eisenhofer G, Harvey-White J, Nechustan A, Kirk K, Kopin IJ: 3,4-Dihydroxyphenylacetaldehyde potentiates the toxic effects of metabolic stress in PC12 cells. Brain Res. 2000 Jun 23;868(2):191-201. Both the potentiation of toxicity and the increase in DOPAL levels were blocked by inhibition of monoamine oxidase with clorgyline indicating that accumulation of DOPAL was responsible for the potentiated rotenone-induced toxicity following combined inhibition of ALDH and ARs. |
31(0,1,1,1) | Details |
| 15659109 | Liu HQ, Zhu XZ, Weng EQ: Intracellular oxidation mediates rotenone-induced apoptosis in PC12 cells. Acta Pharmacol Sin. 2005 Jan;26(1):17-26. However, when cells were first incubated with deprenyl, a monoamine oxidase-B inhibitor for 30 min then co-incubated with rotenone plus deprenyl, a brief treatment with reserpine enhanced cell injury. |
31(0,1,1,1) | Details |
| 226438 | Bouhnik J, Clot JP, Baudry M, Michel R: Early effects of thyroidectomy and administration on rat-liver mitochondria. Mol Cell Endocrinol. 1979 Jul;15(1):1-12. The decrease in the activity of the inner-membrane enzymes closely followed the disappearance of T3 and T4 from serum. 10 h after administration of 25 micrograms/100 g T3 to thyroidectomized rats, the activity of and cytochrome c reductases and the consumption rate with or were significantly increased, while, in the outer membrane, the activity of monoamine oxidase and rotenone-insensitive -cytochrome c reductase remained unchanged. |
6(0,0,1,1) | Details |
| 6245185 | Scholte HR, Busch HF: Early changes of muscle mitochondria in Duchenne dystrophy. J Neurol Sci. 1980 Mar;45(2-3):217-34. Muscles from boys and adults without neuromuscular disease were treated likewise. (2) In adults, muscle possesses a significantly higher specific activity (on protein basis) of monoamine oxidase and rotenone-insenitive -cytochrome c reductase (RINCR) than in boys. |
9(0,0,1,4) | Details |
| 1804136 | Anokhina IP, Gorkin VZ, Medvedev AE, Ovchinnikova LN, Khristolyubova NA: Studies on mitochondrial metabolic processes in offspring of alcoholized rats--I. Alcohol Alcohol. 1991;26(5-6):559-65. In the liver mitochondrial fraction of the first generation offspring of alcoholized male rats, decreased activities of monoamine oxidase (MAO) types A and B, rotenone-insensitive -cytochrome c-reductase and succinate dehydrogenase were observed. |
7(0,0,1,2) | Details |
| 4309122 | Shephard EH, Hubscher G: Phosphatidate biosynthesis in mitochondrial subfractions of rat liver. . Biochem J. 1969 Jun;113(2):429-40. Phosphatidate formation was measured in all subcellular fractions and subfractions and was compared with the distribution of succinate dehydrogenase, monoamine oxidase, rotenone-insensitive cytochrome c reductase, arylsulphatase, urate oxidase, arylesterase and glucose 6-phosphatase. 3. |
6(0,0,1,1) | Details |
| 224923 | Bers DM: Isolation and characterization of cardiac sarcolemma. Biochim Biophys Acta. 1979 Jul 19;555(1):131-46. There may, however, be some contamination by outer mitochondrial membranes (as judged by monoamine oxidase and rotenone-insensitive cytochrome c reductase activities) which have rarely been monitored in cardiac sarcolemmal preparations. |
6(0,0,1,1) | Details |
| 5563754 | Okamoto H: Influence of on kynurenine 3-hydroxylase, monoamine oxidase, and rotenone-insensitive -cytochrome c reductase in mitochondrial outer membrane. Biochem Biophys Res Commun. 1971 May 21;43(4):827-33. |
6(0,0,1,1) | Details |
| 2541720 | Tenang EM, McCaldin B: Further serum related alterations in the activities of some membrane marker enzymes in normal and virus transformed cells. Biochem Int. 1989 Jan;18(1):197-202. We have assayed the levels of 5'nucleotidase, monoamine oxidase and rotenone insensitive ferricyanide reductase in these cells grown to sparse and confluent cultures in medium supplemented with 10% newborn calf serum (n.c.s.) or in medium supplemented with 10% foetal bovine serum (f.b.s.). |
6(0,0,1,1) | Details |
| 1759390 | Medvedev AE, Gorkin VZ: [The role of monoamine oxidase in the regulation of mitochondrial energy functions]. Vopr Med Khim. 1991 Sep-Oct;37(5):2-6. Incubation of aldehyde dehydrogenase-free mitochondrial preparations with biogenic amines and resulted in inhibition of enzymes activity of both outer (rotenone-insensitive -cytochrome c reductase) and inner (succinate dehydrogenase, cytochrome c reductase) mitochondrial membranes. |
2(0,0,0,2) | Details |
| 22598 | Della Corte L, Callingham BA: The influence of adrenalectomy on monoamine oxidase and cytochrome c reductase in the rat heart. J Pharm Pharmacol. 1977 Nov;29(11):657-63. However, both the total and the rotenone-insensitive NCR activities increased, with that of the rotenone-insensitive being about half of the total, which indicated that the effect of adrenalectomy was exerted on components of this enzyme localized on both the inner and outer membranes of the mitochondrion. |
2(0,0,0,2) | Details |
| 11038276 | Lizcano JM, Unzeta M, Tipton KF: A spectrophotometric method for determining the oxidative deamination of by the amine oxidases. Anal Biochem. 2000 Nov 1;286(1):75-9. Interference from the presence of a rotenone-insensitive oxidase activity in crude tissue homogenates and microsomal fractions can be minimized by pretreating samples with Triton X-100 or substituting NAD (+) by APAD (+) in the coupled assay. |
2(0,0,0,2) | Details |
| 223146 | Hayes LW, Goguen CA, Stevens AL, Magargal WW, Slakey LL: Enzyme activities in endothelial cells and smooth muscle cells from swine aorta. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2532-5. In populations of cultured arterial endothelial and smooth muscle cells grown under the same conditions, we have measured the total activity per cell of 10 enzymes commonly used as "markers" for subcellular organelles: ferricyanide reductase, NADH:cytochrome c reductase (rotenone insensitive). NADPH:cytochrome c reductase, alpha-glucosidase, 5'-nucleotidase, alkaline phosphodiesterase I, cytochrome oxidase, monoamine oxidase, cathepsin D, and N-acetyl-beta-glucosaminidase. |
1(0,0,0,1) | Details |
| 10797558 | Lamensdorf I, Eisenhofer G, Harvey-White J, Hayakawa Y, Kirk K, Kopin IJ: Metabolic stress in PC12 cells induces the formation of the endogenous dopaminergic neurotoxin, 3,4-dihydroxyphenylacetaldehyde. J Neurosci Res. 2000 May 15;60(4):552-8. 3,4-Dihydroxyphenylacetaldehyde (DOPAL) has been reported to be a toxic metabolite formed by the oxidative-deamination of (DA) catalyzed by monoamine oxidase. |
1(0,0,0,1) | Details |
| 19605638 | Bao L, Avshalumov MV, Patel JC, Lee CR, Miller EW, Chang CJ, Rice ME: Mitochondria are the source of peroxide for dynamic brain-cell signaling. J Neurosci. 2009 Jul 15;29(28):9002-10. Here we addressed three possible sources of H (2) O (2) produced for rapid neuronal signaling in striatum: mitochondrial respiration, monoamine oxidase (MAO), and oxidase (Nox). Using direct fluorescence imaging of H (2) O (2) and tissue analysis of ATP, we found that coapplication of rotenone (50 nM), a mitochondrial complex I inhibitor, and (5 mM), a complex II substrate, limited H (2) O (2) production, but maintained tissue ATP content. |
1(0,0,0,1) | Details |
| 3486869 | Ramsay RR, Singer TP: Energy-dependent uptake of N-methyl-4-phenylpyridinium, the metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, by mitochondria. J Biol Chem. 1986 Jun 15;261(17):7585-7. Neurotoxicity depends on oxidation of MPTP by monoamine oxidase in brain cells to the dihydropyridinium form, which is further oxidized to N-methyl-4-phenylpyridinium (MPP+), the 4-electron oxidation product. |
1(0,0,0,1) | Details |
| 2253761 | Singer TP, Ramsay RR: Mechanism of the neurotoxicity of MPTP. FEBS Lett. 1990 Nov 12;274(1-2):1-8. Recent experiments suggest that the binding site is at or near the combining site of the classical respiratory inhibitors, rotenone and piericidin A. The initial biochemical event is a two-step oxidation by monoamine oxidase B in glial cells to MPP+ (1-methyl-4-phenylpyridinium). |
1(0,0,0,1) | Details |
| 18579341 | Sai Y, Wu Q, Le W, Ye F, Li Y, Dong Z: Rotenone-induced PC12 cell toxicity is caused by oxidative stress resulting from altered metabolism. Toxicol In Vitro. 2008 Sep;22(6):1461-8. Epub 2008 May 4. The activity of monoamine oxidase (MAO) was also increased. |
1(0,0,0,1) | Details |
| 3571184 | Nishino H, Ito A: Subcellular distribution of OM cytochrome b-mediated -semidehydroascorbate reductase activity in rat liver. J Biochem. 1986 Dec;100(6):1523-31. The ratio of the OM cytochrome b-mediated activities of -SDA reductase to rotenone-insensitive -cytochrome c reductase varied among these tissues. Among the submicrosomal fractions, OM cytochrome b-mediated -SDA reductase activity was highest in the cis-Golgi membrane fraction, in which monoamine oxidase activity was also highest. |
1(0,0,0,1) | Details |
| 2313288 | Scotcher KP, Irwin I, DeLanney LE, Langston JW, Di Monte D: Effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and 1-methyl-4-phenylpyridinium ion on ATP levels of mouse brain synaptosomes. J Neurochem. 1990 Apr;54(4):1295-301. MPTP-induced ATP depletion was completely prevented by the monoamine oxidase B inhibitor deprenyl, which, on the contrary, was ineffective against MPP+. |
1(0,0,0,1) | Details |
| 2788714 | Danias P, Nicklas WJ, Ofori S, Shen J, Mytilineou C: Mesencephalic neurons become less sensitive to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity during development in vitro. J Neurochem. 1989 Oct;53(4):1149-55. The in vitro development of monoamine oxidase (MAO) activity and [3H] (DA) uptake capacity of dissociated cell cultures from rat embryo mesencephalon were correlated with the potency of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and 1-methyl-4-phenylpyridine (MPP+) neurotoxicity. The damage to DA neurons caused by the mitochondrial toxin, rotenone, also showed a similar reduction in the older cultures. |
1(0,0,0,1) | Details |
| 3912685 | Heikkila RE, Nicklas WJ, Vyas I, Duvoisin RC: Dopaminergic toxicity of rotenone and the 1-methyl-4-phenylpyridinium ion after their stereotaxic administration to rats: implication for the mechanism of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine toxicity. Neurosci Lett. 1985 Dec 18;62(3):389-94. MPP+ can be formed by the oxidation of MPTP by monoamine oxidase B to the intermediate dihydropyridinium species, MPDP+, which is spontaneously transformed to MPP+. |
1(0,0,0,1) | Details |
| 3435468 | Vamecq J, Schepers L, Parmentier G, Mannaerts GP: Inhibition of peroxisomal fatty acyl- oxidase by antimycin A. Biochem J. 1987 Dec 1;248(2):603-7. The peroxisomal D-amino acid oxidase was also inhibited by antimycin, but the peroxisomal L-alpha-hydroxyacid oxidase and oxidase and the mitochondrial monoamine oxidase were not. |
1(0,0,0,1) | Details |
| 10079182 | Boldyrev AA, Carpenter DO, Huentelman MJ, Peters CM, Johnson P: Sources of reactive species production in excitotoxin- stimulated cerebellar granule cells. Biochem Biophys Res Commun. 1999 Mar 16;256(2):320-4. Exposure of stimulated cells to rotenone (a respiratory chain inhibitor) did not decrease ROS levels and did not affect short-term cell viability. In cells stimulated by and KA, exposure to indomethacin (a cyclooxygenase inhibitor) and nialamide (a monoamine oxidase inhibitor) caused a decrease in ROS levels and increased cell viability occurred in -treated cells. |
1(0,0,0,1) | Details |
| 6317478 | Kopeikina-Tsiboukidou L, Deliconstantinos G: Functional changes of rat brain mitochondrial enzymes induced by monomeric Int J Biochem. 1983;15(12):1403-7. The specific activity of the outer mitochondrial membrane enzyme monoamine oxidase was linearly decreased at different concentration of or its glucoside. The specific activity of the inner mitochondrial membrane enzyme -cytochrome c reductase was linearly decreased, while that of Rotenone-sensitive -cytochrome c reductase was exponentially increased, at different concentrations of |
1(0,0,0,1) | Details |
| 15953813 | Naoi M, Maruyama W, Shamoto-Nagai M, Yi H, Akao Y, Tanaka M: Oxidative stress in mitochondria: decision to survival and death of neurons in neurodegenerative disorders. Mol Neurobiol. 2005;31(1-3):81-93. In mitochondria, oxidative phosphorylation and enzymatic oxidation of biogenic amines by monoamine oxidase produce reactive and species, which are proposed to cause neuronal cell death in neurodegenerative disorders, including Parkinson's and Alzheimer's disease. The interactions among these factors were studied by use of a -generating agent, N-morpholino sydnonimine (SIN-1) and an inhibitor of complex I, rotenone, in human dopaminergic SH-SY5Y cells. |
1(0,0,0,1) | Details |
| 3032255 | Sikpi MO, Das SK: The localization of cholinephosphotransferase in the outer membrane of guinea-pig lung mitochondria. Biochim Biophys Acta. 1987 May 12;899(1):35-43. Similar subcellular distribution patterns were observed for both cholinephosphotransferase and rotenone-insensitive -cytochrome c reductase, an enzyme associated with the outer membrane of mitochondria and endoplasmic reticulum, suggesting that cholinephosphotransferase may be localized in both of these organelles. The distribution of cholinephosphotransferase activity in the subfractions of mitochondria and the intermediate fractions recovered by linear density gradient paralleled that of the mitochondrial outer membrane marker enzyme, monoamine oxidase. |
1(0,0,0,1) | Details |
| 5499970 | Gear AR: Inner- and outer-membrane enzymes of mitochondria during liver regeneration. Biochem J. 1970 Dec;120(3):577-87. The behaviour of the rotenone-insensitive, cytochrome c reductase did not parallel the other outer-membrane enzymes for intact mitochondria, but did so when assayed in highly purified fractions of outer membrane. However, the specific activities of monoamine oxidase and kynurenine hydroxylase, both outer-membrane markers, fell by 67% and 49% respectively from their control values at 4 days after operation, and returned to normal by about 3 weeks. 4. |
1(0,0,0,1) | Details |
| 11295535 | Kristal BS, Conway AD, Brown AM, Jain JC, Ulluci PA, Li SW, Burke WJ: Selective dopaminergic vulnerability: 3,4-dihydroxyphenylacetaldehyde targets mitochondria. Free Radic Biol Med. 2001 Apr 15;30(8):924-31. Association between mitochondrial dysfunction, monoamine oxidase (MAO) activity, and dopaminergic neurotoxicity has been repeatedly observed, but the mechanisms underlying selective dopaminergic neuron depletion in aging and neurodegenerative disorders remain unclear. |
1(0,0,0,1) | Details |
| 15710606 | Zoccarato F, Toscano P, Alexandre A: -derived dopaminochrome promotes H (2) O (2) release at mitochondrial complex I: stimulation by rotenone, control by Ca (2+), and relevance to Parkinson disease. J Biol Chem. 2005 Apr 22;280(16):15587-94. Epub 2005 Feb 14. Thus, the H (2) O (2) formed accumulated in the medium if contaminating Ca (2+) was present; in the absence of Ca (2+), H (2) O (2) was completely removed if it originated from monoamine oxidase, but was less completely removed if it originated from DACHR. |
1(0,0,0,1) | Details |
| 169529 | Zeit-Har SA, Drahota Z: The development of mitochondrial oxidative enzymes in rat heart muscle. . Physiol Bohemoslov. 1975;24(4):289-96. Three different developmental patterns have been found in the heart muscle mitochondria: (a) Activity of inner membrane enzymes, -cytochrome c reductase and rotenone-sensitive -cytochrome c reductase, was found to increase rapidly after birth till the 25th day; no further increase was found till the 60th day. |
0(0,0,0,0) | Details |