Monoamine Oxidase A Contributes to Serotonin—But Not Norepinephrine-Dependent Damage of Rat Ventricular Myocytes

Knittel, James J.; Itani, Nozomi; Schreckenberg, Rolf; Heger, Jacqueline; Rohrbach, Susanne; Schulz, Ronald; Schlüter, Klaus‐Dieter

doi:10.3390/biom13061013

Cited by 3 publications

(1 citation statement)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The two MAO isoforms have common substrates, such as dopamine but also specific substrates: MAO-B can metabolize 1-methyl histamine, produced by the histamine-N-methyltransferase, while MAO-A metabolizes serotonin (or 5-hydroxytryptamin, 5-HT) and catecholamines. Interestingly, MAO-A contributes to serotonin- but not norepinephrine-dependent damage of rat ventricular myocytes [ 384 ]. MAO requires flavin adenine dinucleotide as a cofactor that is reduced by the reaction and subsequently re-oxidized by molecular oxygen, generating hydrogen peroxide.…”

Section: Pathophysiological Mechanisms Of Noise Exposurementioning

confidence: 99%

Health position paper and redox perspectives - Disease burden by transportation noise

Sørensen,

Pershagen,

Thacher

et al. 2024

Redox Biology

Self Cite

View full text Add to dashboard Cite

Section: Pathophysiological Mechanisms Of Noise Exposurementioning

confidence: 99%

Health position paper and redox perspectives - Disease burden by transportation noise

Sørensen,

Pershagen,

Thacher

et al. 2024

Redox Biology

Self Cite

View full text Add to dashboard Cite

Characterization of Oxygenated Propenylbenzene Derivatives Binding to MAO-A Using Isothermal Titration Calorimetry and Molecular Modeling

Grzelczyk,

Pérez-Sánchez,

Carmena-Bargueño

et al. 2024

Applied Sciences

View full text Add to dashboard Cite

Monoamine oxidase A (MAO-A) is the main enzyme that deaminates serotonin. Correct serotonin concentration regulates appetite, improves well-being, reduces symptoms of depression, but also improves memory and heart function. In this study, the use of new compounds chemo-enzymatically synthesized from propenylbenzene derivatives as MAO-A inhibitors was proposed. Isothermal titration calorimetry analysis and molecular modeling were used to determine the inhibitory effect of MAO-A. The main compounds such as propenylbenzenes were observed to have no inhibitory effect. However, in the case of diols and hydroxy ketones, the compounds showed MAO-A inhibitory effects. In particular, 1-(4-hydroxy-3-methoxyphenyl)propane-1,2-diol, both in isothermal titration calorimetry (ITC) and molecular modeling, showed high affinity for the MAO-A enzyme, thus protecting serotonin from deamination. The results suggest that propenylbenzene derivatives, such as diols and hydroxy ketones, bind to MAO-A at the active site. This suggests their potential to be used as drugs or food supplements to prevent depression. These studies may constitute a new tool for further in vivo and in vitro studies.

show abstract

Monoamine Oxidase Contributes to Valvular Oxidative Stress: A Prospective Observational Pilot Study in Patients with Severe Mitral Regurgitation

Șoșdean,

Dănilă,

Ionică

et al. 2024

IJMS

View full text Add to dashboard Cite

Monoamine oxidases (MAOs), mitochondrial enzymes that constantly produce hydrogen peroxide (H2O2) as a byproduct of their activity, have been recently acknowledged as contributors to oxidative stress in cardiometabolic pathologies. The present study aimed to assess whether MAOs are mediators of valvular oxidative stress and interact in vitro with angiotensin 2 (ANG2) to mimic the activation of the renin–angiotensin system. To this aim, valvular tissue samples were harvested from 30 patients diagnosed with severe primary mitral regurgitation and indication for surgical repair. Their reactive oxygen species (ROS) levels were assessed by means of a ferrous oxidation xylenol orange (FOX) assay, while MAO expression was assessed by immune fluorescence (protein) and qRT-PCR (mRNA). The experiments were performed using native valvular tissue acutely incubated or not with angiotensin 2 (ANG2), MAO inhibitors (MAOI) and the angiotensin receptor blocker, irbesartan (Irb). Correlations between oxidative stress and echocardiographic parameters were also analyzed. Ex vivo incubation with ANG2 increased MAO-A and -B expression and ROS generation. The level of valvular oxidative stress was negatively correlated with the left ventricular ejection fraction. MAOI and Irb reduced valvular H2O2. production. In conclusion, both MAO isoforms are expressed in pathological human mitral valves and contribute to local oxidative stress and ventricular functional impairment and can be modulated by the local renin–angiotensin system.

show abstract

Monoamine Oxidase A Contributes to Serotonin—But Not Norepinephrine-Dependent Damage of Rat Ventricular Myocytes

Cited by 3 publications

References 48 publications

Health position paper and redox perspectives - Disease burden by transportation noise

Health position paper and redox perspectives - Disease burden by transportation noise

Characterization of Oxygenated Propenylbenzene Derivatives Binding to MAO-A Using Isothermal Titration Calorimetry and Molecular Modeling

Monoamine Oxidase Contributes to Valvular Oxidative Stress: A Prospective Observational Pilot Study in Patients with Severe Mitral Regurgitation

Contact Info

Product

Resources

About