Inhibitor structure-guided design and synthesis of near-infrared fluorescent probes for monoamine oxidase A (MAO-A) and its application in living cells and in vivo

2019 ◽  
Vol 55 (17) ◽  
pp. 2477-2480 ◽  
Author(s):  
Zhengmin Yang ◽  
Wenxiu Li ◽  
Hua Chen ◽  
Qingyuan Mo ◽  
Jun Li ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Fluorescent Probes ◽  
Near Infrared ◽  
Living Cells ◽  
Monoamine Oxidase A ◽  
Specific Detection ◽  
Design And Synthesis ◽  
Mao A ◽  
In Cells

A series of near-infrared fluorescent probes based on inhibitor (clorgyline) structure-guided design were synthesized for the specific detection of MAO-A in cells and in vivo.

Fluorinated near-infrared fluorescent probes for specific detection of Hg2+ in an aqueous medium and mitochondria of living cells

2017 ◽  
Vol 41 (17) ◽  
pp. 8899-8904 ◽  
Author(s):  
Lei Long ◽  
Xu Tan ◽  
Shenglin Luo ◽  
Chunmeng Shi
Keyword(s):  
Aqueous Medium ◽  
Fluorescent Probe ◽  
Fluorescent Probes ◽  
Near Infrared ◽  
Living Cells ◽  
Specific Detection

A near-infrared fluorescent probe (IR-DFT) could be used for specifically and sensitively detecting Hg2+ in mitochondria of living cells.

Brain monoamine oxidase A in hyperammonemia is regulated by NMDA receptors

2009 ◽  
Vol 4 (3) ◽  
pp. 321-326
Author(s):  
Elena Kosenko ◽  
Yury Kaminsky
Keyword(s):  
Oxidative Stress ◽  
Nmda Receptor ◽  
Monoamine Oxidase ◽  
Nmda Receptors ◽  
Monoamine Oxidase A ◽  
Mk 801 ◽  
Mao A ◽  
Vitro Effect

AbstractMitochondrial enzyme monoamine oxidase A (MAO-A) generates hydrogen peroxide (H2O2) and is up-regulated by Ca2+ and presumably by ammonia. We hypothesized that MAO-A may be under the control of NMDA receptors in hyperammonemia. In this work, the in vivo effects of single dosing with ammonia and NMDA receptor antagonist MK-801 and the in vitro effect of Ca2+ on MAO-A activity in isolated rat brain mitochondria were studied employing enzymatic procedure. Intraperitoneal injection of rats with ammonia led to an increase in MAO-A activity in mitochondria indicating excessive H2O2 generation. Calcium added to isolated mitochondria stimulated MAO-A activity by as much as 84%. MK-801 prevented the in vivo effect of ammonia, implying that MAO-A activation in hyperammonemia is mediated by NMDA receptors. These data support the conclusion that brain mitochondrial MAO-A is regulated by the function of NMDA receptors. The enzyme can contribute to the oxidative stress associated with hyperammonemic conditions such as encephalopathy and Alzheimer’s disease. The attenuation of the oxidative stress highlights MAO-A inactivation and NMDA receptor antagonists as sources of novel avenues in the treatment of mental disorders.

11C-harmine as a tracer for monoamine oxidase a (MAO-A): In vitro and in vivo studies

1997 ◽  
Vol 24 (4) ◽  
pp. 287-293 ◽  
Author(s):  
Mats Bergström ◽  
Göran Westerberg ◽  
Bengt Långström
Keyword(s):  
Monoamine Oxidase ◽  
Monoamine Oxidase A ◽  
In Vivo Studies ◽  
Mao A

The design and synthesis of novel “turn-on” fluorescent probes to visualize monoamine oxidase-B in living cells

RSC Advances ◽  
2013 ◽  
Vol 3 (15) ◽  
pp. 4876 ◽  
Author(s):  
Yumi Xiang ◽  
Bingyong He ◽  
Xuefeng Li ◽  
Qing Zhu
Keyword(s):  
Monoamine Oxidase ◽  
Fluorescent Probes ◽  
Living Cells ◽  
Monoamine Oxidase B ◽  
Design And Synthesis ◽  
Turn On

Phenoxazine‐based Near‐infrared Fluorescent Probes for the Specific Detection of Copper (II) Ions in Living Cells

2020 ◽  
Vol 15 (18) ◽  
pp. 2864-2867
Author(s):  
Yang Shen ◽  
Wubin Zheng ◽  
Yusi Yao ◽  
Dongmei Wang ◽  
Guanglei Lv ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Near Infrared ◽  
Living Cells ◽  
Specific Detection

Thyroid iodide transport is reduced by administration of monoamine oxidase A inhibitors to rats

1994 ◽  
Vol 143 (2) ◽  
pp. 303-308 ◽  
Author(s):  
A M Cabanillas ◽  
A M Masini-Repiso ◽  
M E Costamagna ◽  
C Pellizas ◽  
A H Coleoni
Keyword(s):  
Monoamine Oxidase ◽  
Transport Mechanism ◽  
Monoamine Oxidase A ◽  
Mao Inhibitors ◽  
Iodide Uptake ◽  
Mao B ◽  
Iodide Transport ◽  
Mao A ◽  
Mao Activity

Abstract The present work was addressed to study a possible relationship between monoamine oxidase (MAO) and the thyroid iodide transport mechanism. Normal rats treated with clorgyline (a selective MAO-A inhibitor) or tranylcypromine (a non-selective MAO inhibitor) showed a significantly diminished thyroid MAO activity, while deprenyl and pargyline (MAO-B inhibitors) did not modify the thyroidal enzyme activity with respect to the control group. Under these conditions, in vivo iodide transport was reduced both by clorgyline and tranylcypromine administration whereas it remained unchanged after treatment with MAO-B inhibitors. The effect of MAO inhibitors on thyroid MAO activity and in vivo iodide transport was also evaluated in rats treated with exogenous thyrotrophin (TSH) after endogenous TSH secretion blockade produced by T4 administration. In this condition, thyroid MAO activity was significantly lowered by clorgyline and was not modified by deprenyl. In contrast to the results observed in normal rats, in vivo iodide transport in TSH-treated rats remained unaltered after treatment either with clorgyline or deprenyl. MAO activity evaluated in bovine thyroid follicles in primary culture was highly sensitive to low concentrations of clorgyline (<10 nmol/l) and relatively insensitive to deprenyl, a finding that indicates a predominance of the MAO-A isoform in the follicular cells in culture. When clorgyline (0·1 and 1 μmol/l) or deprenyl (1 μmol/l) were added to the culture medium, no modifications in the active transport of iodide were observed. These results indicate the absence of a direct linkage between thyroid MAO activity and the active iodide transport. MAO inhibitors (particularly MAO-A inhibitors) do not appear to be responsible for an in vivo diminished thyroid iodide uptake through a direct action on the iodide transport mechanism. An indirect effect of MAO-A inhibitors on thyroid iodide transport mediated by the accumulation of monoamines in neuroendocrine areas involved in TSH regulation is suggested. Journal of Endocrinology (1994) 143, 303–308

scholarly journals Microbial Metabolite Urolithin B Inhibits Recombinant Human Monoamine Oxidase A Enzyme

Metabolites ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 258
Author(s):  
Rajbir Singh ◽  
Sandeep Chandrashekharappa ◽  
Praveen Kumar Vemula ◽  
Bodduluri Haribabu ◽  
Venkatakrishna Rao Jala
Keyword(s):  
Monoamine Oxidase ◽  
Enzyme Inhibitor ◽  
Monoamine Oxidase A ◽  
Mao B ◽  
Functional Activities ◽  
Mao A ◽  
Mao Activity ◽  
Anti Oxidant ◽  
Urolithin B

Urolithins are gut microbial metabolites derived from ellagitannins (ET) and ellagic acid (EA), and shown to exhibit anticancer, anti-inflammatory, anti-microbial, anti-glycative and anti-oxidant activities. Similarly, the parent molecules, ET and EA are reported for their neuroprotection and antidepressant activities. Due to the poor bioavailability of ET and EA, the in vivo functional activities cannot be attributed exclusively to these compounds. Elevated monoamine oxidase (MAO) activities are responsible for the inactivation of monoamine neurotransmitters in neurological disorders, such as depression and Parkinson’s disease. In this study, we examined the inhibitory effects of urolithins (A, B and C) and EA on MAO activity using recombinant human MAO-A and MAO-B enzymes. Urolithin B was found to be a better MAO-A enzyme inhibitor among the tested urolithins and EA with an IC50 value of 0.88 µM, and displaying a mixed mode of inhibition. However, all tested compounds exhibited higher IC50 (>100 µM) for MAO-B enzyme.

scholarly journals In vivo Quantification of Monoamine Oxidase A in Baboon Brain: A PET Study Using [11C]befloxatone and the Multi-Injection Approach

2009 ◽  
Vol 30 (4) ◽  
pp. 792-800 ◽  
Author(s):  
Michel Bottlaender ◽  
Héric Valette ◽  
Jacques Delforge ◽  
Wadad Saba ◽  
Ilonka Guenther ◽  
...  
Keyword(s):  
Monoamine Oxidase ◽  
Binding Site ◽  
Binding Sites ◽  
Brain Structures ◽  
Monoamine Oxidase A ◽  
Model Parameters ◽  
Site Density ◽  
Mao A ◽  
The Brain

[11C]befloxatone is a high-affinity, reversible, and selective radioligand for the in vivo visualization of the monoamine oxidase A (MAO-A) binding sites using positron emission tomography (PET). The multi-injection approach was used to study in baboons the interactions between the MAO-A binding sites and [11C]befloxatone. The model included four compartments and seven parameters. The arterial plasma concentration, corrected for metabolites, was used as input function. The experimental protocol—three injections of labeled and/or unlabeled befloxatone—allowed the evaluation of all the model parameters from a single PET experiment. In particular, the brain regional concentrations of the MAO-A binding sites ( B′max) and the apparent in vivo befloxatone affinity ( Kd) were estimated in vivo for the first time. A high binding site density was found in almost all the brain structures (170±39 and 194±26 pmol/mL in the frontal cortex and striata, respectively, n=5). The cerebellum presented the lowest binding site density (66±13 pmol/mL). Apparent affinity was found to be similar in all structures ( Kd VR=6.4±1.5 nmol/L). This study is the first PET-based estimation of the Bmax of an enzyme.

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