Related Experiment Video
Updated: Aug 2, 2026
07:47
Analysis of Brain Mitochondria Using Serial Block-Face Scanning Electron Microscopy
Published on: July 9, 2016
Modulation of brain mitochondrial function by deprenyl.
Analía Czerniczyniec1, Juanita Bustamante, Silvia Lores-Arnaiz
1Laboratory of Free Radical Biology, School of Pharmacy and Biochemistry, University of Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina.
Neurochemistry International
|November 18, 2005
Summary
Deprenyl, an MAO B inhibitor, impacts mitochondrial function by inhibiting nitric oxide synthase and reducing hydrogen peroxide production. These effects suggest deprenyl influences cellular energy and oxidative stress pathways.
Area of Science:
- Neuroscience
- Biochemistry
- Mitochondrial Biology
Background:
- Deprenyl is a known inhibitor of monoamine oxidase B (MAO B).
- Mitochondrial dysfunction is implicated in various neurological conditions.
- The precise effects of deprenyl on mitochondrial function require further elucidation.
Purpose of the Study:
- To investigate the in vitro effects of deprenyl on mitochondrial function.
- To determine the impact of deprenyl on nitric oxide synthase (NOS) activity.
- To assess deprenyl's influence on mitochondrial respiration, permeability, and hydrogen peroxide production.
Main Methods:
- Incubation of brain submitochondrial membranes, synaptosomes, and cytosolic fractions with varying deprenyl concentrations.
- Measurement of nitric oxide synthase (NOS) and monoamine oxidase activities.
- Assessment of oxygen consumption, calcium-induced permeability transition, and hydrogen peroxide (H(2)O(2)) production in isolated mitochondria.
Main Results:
- Deprenyl inhibited NOS activity in a concentration-dependent manner across different brain fractions.
- Monoamine oxidase activity was inhibited at lower deprenyl concentrations.
- Deprenyl (25 microM) increased oxygen uptake in state 3 and enhanced cytochrome oxidase activity.
- Low deprenyl concentrations (0.5-1 microM) inhibited calcium-induced mitochondrial permeability transition and reduced H(2)O(2) production.
Conclusions:
- In vitro, deprenyl affects mitochondrial function through mechanisms including NOS inhibition and reduced hydrogen peroxide production.
- These findings highlight potential roles of deprenyl in modulating cellular energy metabolism and oxidative stress.
- Further research is warranted to explore the therapeutic implications of these mitochondrial effects.
Related Concept Videos
01:37Mitochondria
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
01:45Mitochondrial Membranes
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
01:46Electron Transport Chain: Complex I and II
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
01:48ATP Synthase: Mechanism
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
01:39Mitochondrial Precursor Proteins
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Most of the mitochondrial precursors...
01:19Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...