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Current Molecular Medicine Feb 2010The Plasmodium falciparum mitochondrion is an organelle that presents structural and physiological characteristics different from mitochondria in other eukaryotes.... (Review)
Review
The Plasmodium falciparum mitochondrion is an organelle that presents structural and physiological characteristics different from mitochondria in other eukaryotes. Moreover, there are substantial differences in the properties of asexual and sexual mitochondria. One of the reasons is the adaptation of the parasite to different environments, in particular the great differences in oxygen tension between the host and the mosquito. In this review, we present a synthesis of the recent data on the ultrastructure, the genome and the physiology of the mitochondrion. We try to clarify the mitochondrial role in the intraerythrocytic environment and particularly focus on mitochondrial metabolic pathways that relate to oxidative phosphorylation, including the tricarboxylic acid cycle, de novo pyrimidine biosynthesis via dihydroorotate dehydrogenase and the particularities of the electron transport chain. In addition, we provide details on certain characteristics like the lack of pyruvate dehydrogenase, the existence of a rotenone-insensitive NADH-dehydrogenase, the possible existence of an alternative oxidase, and uncoupled proteins. Such unique particularities of parasite mitochondria could be promising targets for development of a new therapy. The elucidation of the role of this organelle in microaerophilic respiratory metabolism and the association of antimalarial drugs with hyperbaric oxygen therapy might provide new treatments for infection by P. falciparum.
Topics: Aerobiosis; Animals; Antimalarials; Energy Metabolism; Malaria, Falciparum; Mitochondria; Plasmodium falciparum
PubMed: 20205678
DOI: 10.2174/156652410791065390 -
Nature Biotechnology Mar 2003
Topics: Animals; Electrophoresis; Heart; Humans; Mitochondria; Myocardium; Proteins; Sequence Analysis, Protein; Yeasts
PubMed: 12610566
DOI: 10.1038/nbt0303-239 -
Toxicology in Vitro : An International... Feb 2019The aim of this study was to investigate the effects of excessive copper (Cu)-induced cytotoxicity on oxidative stress and mitochondrial apoptosis in chicken...
The aim of this study was to investigate the effects of excessive copper (Cu)-induced cytotoxicity on oxidative stress and mitochondrial apoptosis in chicken hepatocytes. Chicken hepatocytes were cultured in medium in the absence and presence of copper sulfate (CuSO) (10, 50, 100 μM), in N-acetyl-L-cysteine (NAC) (1 mM), and the combination of CuSO and NAC for 24 h. Morphologic observation and function, reactive oxygen species (ROS) level, antioxidant indices, nitric oxide (NO) content, mitochondrial membrane potential (MMP), and apoptosis-related mRNA and protein levels were determined. These results indicated that excessive Cu could induce release of intracellular lactate dehydrogenase (LDH), aspartate aminotransferase (AST), and alanine aminotransferase (ALT); increase levels of ROS, superoxide dismutase (SOD), malondialdehyde (MDA), catalase (CAT), lipid peroxidation (LPO), and NO; decrease glutathione (GSH) content and MMP; upregulated Bak1, Bax, CytC, and Caspase3 mRNA and protein expression, inhibited Bcl2 mRNA and protein expression, and induced cell apoptosis in a dose effect. The Cu-caused changes of all above factors were alleviated by treatment with NAC. These results suggested that excessive Cu could induce oxidative stress and apoptosis via mitochondrial pathway in chicken hepatocytes.
Topics: Animals; Apoptosis; Cells, Cultured; Chickens; Copper; Hepatocytes; Mitochondria; Oxidative Stress
PubMed: 30389602
DOI: 10.1016/j.tiv.2018.10.017 -
Nature Apr 1971
Topics: DNA; Malate Dehydrogenase; Mitochondria; Neurospora; Oxidative Phosphorylation; Yeasts
PubMed: 4927748
DOI: 10.1038/230504a0 -
Novartis Foundation Symposium 2007Mitochondrial connectivity is characterized by matrix lumen continuity and by dynamic rewiring through fusion and fission events. While these mechanisms homogenize the... (Review)
Review
Mitochondrial connectivity is characterized by matrix lumen continuity and by dynamic rewiring through fusion and fission events. While these mechanisms homogenize the mitochondrial population, a number of studies looking at mitochondrial membrane potential have demonstrated that mitochondria exist as a heterogeneous population within individual cells. To address the relationship between mitochondrial dynamics and heterogeneity, we tagged and tracked individual mitochondria over time while monitoring their mitochondrial membrane potential (deltapsi(m)). By utilizing photoactivatible-GFP (PA-GFP), targeted to the mitochondrial matrix, we determined the boundaries of the individual mitochondrion. A single mitochondrion is defined by the continuity of its matrix lumen. The boundaries set by luminal continuity matched those set by electrical coupling, indicating that the individual mitochondrion is equipotential throughout the entire organelle. Similar results were obtained with PA-GFP targeted to the inner membrane indicating that matrix continuity parallels inner membrane continuity. Sequential photoconversion of matrix PA-GFP in multiple locations within the mitochondrial web reveals that each ramified mitochondrial structure is composed of juxtaposed but discontinuous units. Moreover, as many as half of the events in which mitochondria come into contact, do not result in fusion. While all fission events generated two electrically uncoupled discontinuous matrices, the two daughter mitochondria frequently remained juxtaposed, keeping the tubular appearance unchanged. These morphologically invisible fission events illustrate the difference between mitochondrial fission and fragmentation; the latter representing the movement and separation of disconnected units. Simultaneous monitoring of deltapsi(m) of up to four individual mitochondria within the same cell revealed that subcellular heterogeneity in deltapsi(m) does not represent multiple unstable mitochondria that appear 'heterogeneous' at any given point, but rather multiple stable, but heterogeneous units.
Topics: Animals; Green Fluorescent Proteins; Humans; Light; Membrane Potentials; Mitochondria; Mitochondrial Membranes; Staining and Labeling; Subcellular Fractions
PubMed: 18074629
DOI: 10.1002/9780470725207.ch3 -
No To Hattatsu = Brain and Development Mar 1987
Review
Topics: Electron Transport; Energy Metabolism; Humans; Mitochondria
PubMed: 3548760
DOI: No ID Found -
American Journal of Physiology. Cell... Dec 2006Understanding a complex biological system, such as the mitochondrion, requires the identification of the complete repertoire of proteins targeted to the organelle, the... (Review)
Review
Understanding a complex biological system, such as the mitochondrion, requires the identification of the complete repertoire of proteins targeted to the organelle, the characterization of these, and finally, the elucidation of the functional and physical interactions that occur within the mitochondrion. In the last decade, significant developments have contributed to increase our understanding of the mitochondrion, and among these, computational research has played a significant role. Not only general bioinformatics tools have been applied in the context of the mitochondrion, but also some computational techniques have been specifically developed to address problems that arose from within the mitochondrial research field. In this review the contribution of bioinformatics to mitochondrial biology is addressed through a survey of current computational methods that can be applied to predict which proteins will be localized to the mitochondrion and to unravel their functional interactions.
Topics: Computational Biology; Computer Simulation; Humans; Mitochondria; Mitochondrial Proteins; Mutation
PubMed: 16870830
DOI: 10.1152/ajpcell.00225.2006 -
Mitochondrion Sep 2020
Topics: Animals; Biological Transport; Energy Metabolism; Humans; Mitochondria; Plants
PubMed: 32569844
DOI: 10.1016/j.mito.2020.06.009 -
The American Journal of Physiology Jun 1987The subject of this brief review is the size of the local drops in PO2 around consuming mitochondria. We show that large drops (several Torr or more) are in conflict... (Review)
Review
The subject of this brief review is the size of the local drops in PO2 around consuming mitochondria. We show that large drops (several Torr or more) are in conflict with the predictions of basic diffusion theory, when one uses accepted values for relevant parameters. In particular, oxygen diffusion coefficients must be reduced by at least a factor of 10 below measured values to reconcile Fick's law with large PO2 drops. Experimental evidence offered for large drops is often ambiguous because of system heterogeneities. In those cases where tractable models of heterogeneous systems can be developed, the experimental data are consistent with drops in PO2 on the order of a few hundredths of a Torr between cytosol and mitochondrion.
Topics: Cytosol; Diffusion; Mathematics; Mitochondria; Models, Biological; Oxygen; Oxygen Consumption; Pressure
PubMed: 3296779
DOI: 10.1152/ajpcell.1987.252.6.C583 -
Nature May 2021Organelles called mitochondria divide in at least two contexts: during cell growth and in response to mitochondrial damage. The finding that division is different in...
Organelles called mitochondria divide in at least two contexts: during cell growth and in response to mitochondrial damage. The finding that division is different in these two contexts sheds light on the regulatory pathways involved.
Topics: Mitochondria
PubMed: 33953387
DOI: 10.1038/d41586-021-01173-x