Готові списки джерел за темами / Mitochondrial defects

Добірка наукової літератури з теми "Mitochondrial defects"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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Статті в журналах з теми "Mitochondrial defects"

1

Gorsich, Steven W., and Janet M. Shaw. "Importance of Mitochondrial Dynamics During Meiosis and Sporulation." Molecular Biology of the Cell 15, no. 10 (October 2004): 4369–81. http://dx.doi.org/10.1091/mbc.e03-12-0875.

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Opposing fission and fusion events maintain the yeast mitochondrial network. Six proteins regulate these membrane dynamics during mitotic growth—Dnm1p, Mdv1p, and Fis1p mediate fission; Fzo1p, Mgm1p, and Ugo1p mediate fusion. Previous studies established that mitochondria fragment and rejoin at distinct stages during meiosis and sporulation, suggesting that mitochondrial fission and fusion are required during this process. Here we report that strains defective for mitochondrial fission alone, or both fission and fusion, complete meiosis and sporulation. However, visualization of mitochondria in sporulating cultures reveals morphological defects associated with the loss of fusion and/or fission proteins. Specifically, mitochondria collapse to one side of the cell and fail to fragment during presporulation. In addition, mitochondria are not inherited equally by newly formed spores, and mitochondrial DNA nucleoid segregation defects give rise to spores lacking nucleoids. This nucleoid inheritance defect is correlated with an increase in petite spore colonies. Unexpectedly, mitochondria fragment in mature tetrads lacking fission proteins. The latter finding suggests either that novel fission machinery operates during sporulation or that mechanical forces generate the mitochondrial fragments observed in mature spores. These results provide evidence of fitness defects caused by fission mutations and reveal new phenotypes associated with fission and fusion mutations.
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2

Weidling, Ian, and Russell H. Swerdlow. "Mitochondrial Dysfunction and Stress Responses in Alzheimer’s Disease." Biology 8, no. 2 (May 11, 2019): 39. http://dx.doi.org/10.3390/biology8020039.

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Alzheimer’s disease (AD) patients display widespread mitochondrial defects. Brain hypometabolism occurs alongside mitochondrial defects, and correlates well with cognitive decline. Numerous theories attempt to explain AD mitochondrial dysfunction. Groups propose AD mitochondrial defects stem from: (1) mitochondrial-nuclear DNA interactions/variations; (2) amyloid and neurofibrillary tangle interactions with mitochondria, and (3) mitochondrial quality control defects and oxidative damage. Cells respond to mitochondrial dysfunction through numerous retrograde responses including the Integrated Stress Response (ISR) involving eukaryotic initiation factor 2α (eIF2α), activating transcription factor 4 (ATF4) and C/EBP homologous protein (CHOP). AD brains activate the ISR and we hypothesize mitochondrial defects may contribute to ISR activation. Here we review current recognized contributions of the mitochondria to AD, with an emphasis on their potential contribution to brain stress responses.
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3

Ciceri, E., I. Moroni, G. Uziel, and M. Savoiardo. "Le encefalomiopatie mitocondriali." Rivista di Neuroradiologia 9, no. 6 (December 1996): 775–80. http://dx.doi.org/10.1177/197140099600900623.

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The mitochondrial encephalomyopathies are relatively rare neuromuscular diseases clinically characterised by myopathy and encephalopathy caused by structurally or functionally impaired mitochondria. The biochemical hallmark of this group of disorders is impaired mitochondrial energy production: Kreb's cycle, respiratory chain, oxidative phosphorylation and beta-oxidation of fatty acids. The presence of lactic acidosis and ragged red fibres, i.e. subsarcolemmal accumulations of abnormally sized mitochondria are highly indicative findings for mitochondrial disease. Classification and diagnostic criteria are based on biochemical findings with a search for specific enzyme deficit and molecular genetic information. Molecular genetic studies aim to identify the mitochondrial DNA changes responsible for the enzyme defect. Ragged red fibres are not essential for diagnosis as they are not present in some diseases. In rare cases, mitochondrial diseases are caused by nuclear DNA defects or, more commonly a mitochondrial DNA deficit. Diagnosis may prove difficult given the pathogenetic complexity and clinical and phenotypical variability of these conditions. Despite indirect symptoms of mitochondrial disease, the enzyme defect and genetic alteration cannot be identified in some cases. The mitochondrial encephalopathies can be classified according to the metabolic pathways involved into impaired transport ot uptake of energy, impaired Kreb's cycle or respiratory chain complexes or complex defects due to mitochondrial DNA changes.
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4

Chen, Tsung-Hsien, Kok-Yean Koh, Kurt Ming-Chao Lin, and Chu-Kuang Chou. "Mitochondrial Dysfunction as an Underlying Cause of Skeletal Muscle Disorders." International Journal of Molecular Sciences 23, no. 21 (October 26, 2022): 12926. http://dx.doi.org/10.3390/ijms232112926.

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Mitochondria are an important energy source in skeletal muscle. A main function of mitochondria is the generation of ATP for energy through oxidative phosphorylation (OXPHOS). Mitochondrial defects or abnormalities can lead to muscle disease or multisystem disease. Mitochondrial dysfunction can be caused by defective mitochondrial OXPHOS, mtDNA mutations, Ca2+ imbalances, mitochondrial-related proteins, mitochondrial chaperone proteins, and ultrastructural defects. In addition, an imbalance between mitochondrial fusion and fission, lysosomal dysfunction due to insufficient biosynthesis, and/or defects in mitophagy can result in mitochondrial damage. In this review, we explore the association between impaired mitochondrial function and skeletal muscle disorders. Furthermore, we emphasize the need for more research to determine the specific clinical benefits of mitochondrial therapy in the treatment of skeletal muscle disorders.
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5

Salgado, Josefa, Beatriz Honorato, and Jesús García-Foncillas. "Review: Mitochondrial Defects in Breast Cancer." Clinical medicine. Oncology 2 (January 2008): CMO.S524. http://dx.doi.org/10.4137/cmo.s524.

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Mitochondria play important roles in cellular energy metabolism, free radical generation, and apoptosis. Mitochondrial DNA has been proposed to be involved in carcinogenesis because of its high susceptibility to mutations and limited repair mechanisms in comparison to nuclear DNA. Breast cancer is the most frequent cancer type among women in the world and, although exhaustive research has been done on nuclear DNA changes, several studies describe a variety of mitochondrial DNA alterations present in breast cancer. In this review article, we to provide a summary of the mitochondrial genomic alterations reported in breast cancer and their functional consequences.
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PAL, ARUNA, and SAMIDDHA BANERJEE. "Mitochondrial replacement therapy - a new remedy for defects in reproduction." Indian Journal of Animal Sciences 88, no. 6 (June 22, 2018): 637–44. http://dx.doi.org/10.56093/ijans.v88i6.80860.

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Mitochondria is an important subcellular organelle with the prime function being energy metabolism and supply of energy to the body cells for carrying out the vital functions. Energy is the primary requisite for the reproductive organs of both male and female for carrying out the normal functions. In the present article, we have described how mutation in mitochondrial DNA lead to defects in male and female reproduction. Mitochondria is an integral part of the mid-piece of sperm and also has role in other parts of male reproductive system. Similarly, mitochondrial DNA has role in female reproductive system including ovulation, zygote activation, fertilization, oocyte maturation and embryo development. Mitochondrial defect are collectively named as "mystondria" (mysterious diseases of mitochondria) and may be corrected through mitochondrial replacement therapy, popularly known as three parent baby concept, since there are no other scope for cure or treatment. Two approaches for mitochondrial replacement therapy are pronuclear transfer and spindle transfer. The first three parent baby was developed in April 2016 through mitochondrial replacement therapy. The present review is aimed at functional relevance of three-parent baby concept in animal reproduction.
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7

Lenzi, Paola, Rosangela Ferese, Francesca Biagioni, Federica Fulceri, Carla L. Busceti, Alessandra Falleni, Stefano Gambardella, Alessandro Frati, and Francesco Fornai. "Rapamycin Ameliorates Defects in Mitochondrial Fission and Mitophagy in Glioblastoma Cells." International Journal of Molecular Sciences 22, no. 10 (May 20, 2021): 5379. http://dx.doi.org/10.3390/ijms22105379.

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Glioblastoma (GBM) cells feature mitochondrial alterations, which are documented and quantified in the present study, by using ultrastructural morphometry. Mitochondrial impairment, which roughly occurs in half of the organelles, is shown to be related to mTOR overexpression and autophagy suppression. The novelty of the present study consists of detailing an mTOR-dependent mitophagy occlusion, along with suppression of mitochondrial fission. These phenomena contribute to explain the increase in altered mitochondria reported here. Administration of the mTOR inhibitor rapamycin rescues mitochondrial alterations. In detail, rapamycin induces the expression of genes promoting mitophagy (PINK1, PARKIN, ULK1, AMBRA1) and mitochondrial fission (FIS1, DRP1). This occurs along with over-expression of VPS34, an early gene placed upstream in the autophagy pathway. The topographic stoichiometry of proteins coded by these genes within mitochondria indicates that, a remarkable polarization of proteins involved in fission and mitophagy within mitochondria including LC3 takes place. Co-localization of these proteins within mitochondria, persists for weeks following rapamycin, which produces long-lasting mitochondrial plasticity. Thus, rapamycin restores mitochondrial status in GBM cells. These findings add novel evidence about mitochondria and GBM, while fostering a novel therapeutic approach to restore healthy mitochondria through mTOR inhibition.
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Bakare, Ajibola B., Julienne Daniel, Joshua Stabach, Anapaula Rojas, Austin Bell, Brooke Henry, and Shilpa Iyer. "Quantifying Mitochondrial Dynamics in Patient Fibroblasts with Multiple Developmental Defects and Mitochondrial Disorders." International Journal of Molecular Sciences 22, no. 12 (June 10, 2021): 6263. http://dx.doi.org/10.3390/ijms22126263.

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Mitochondria are dynamic organelles that undergo rounds of fission and fusion and exhibit a wide range of morphologies that contribute to the regulation of different signaling pathways and various cellular functions. It is important to understand the differences between mitochondrial structure in health and disease so that therapies can be developed to maintain the homeostatic balance of mitochondrial dynamics. Mitochondrial disorders are multisystemic and characterized by complex and variable clinical pathologies. The dynamics of mitochondria in mitochondrial disorders is thus worthy of investigation. Therefore, in this study, we performed a comprehensive analysis of mitochondrial dynamics in ten patient-derived fibroblasts containing different mutations and deletions associated with various mitochondrial disorders. Our results suggest that the most predominant morphological signature for mitochondria in the diseased state is fragmentation, with eight out of the ten cell lines exhibiting characteristics consistent with fragmented mitochondria. To our knowledge, this is the first comprehensive study that quantifies mitochondrial dynamics in cell lines with a wide array of developmental and mitochondrial disorders. A more thorough analysis of the correlations between mitochondrial dynamics, mitochondrial genome perturbations, and bioenergetic dysfunction will aid in identifying unique morphological signatures of various mitochondrial disorders in the future.
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9

Murata, Daisuke, Kenta Arai, Miho Iijima, and Hiromi Sesaki. "Mitochondrial division, fusion and degradation." Journal of Biochemistry 167, no. 3 (December 4, 2019): 233–41. http://dx.doi.org/10.1093/jb/mvz106.

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Abstract The mitochondrion is an essential organelle for a wide range of cellular processes, including energy production, metabolism, signal transduction and cell death. To execute these functions, mitochondria regulate their size, number, morphology and distribution in cells via mitochondrial division and fusion. In addition, mitochondrial division and fusion control the autophagic degradation of dysfunctional mitochondria to maintain a healthy population. Defects in these dynamic membrane processes are linked to many human diseases that include metabolic syndrome, myopathy and neurodegenerative disorders. In the last several years, our fundamental understanding of mitochondrial fusion, division and degradation has been significantly advanced by high resolution structural analyses, protein-lipid biochemistry, super resolution microscopy and in vivo analyses using animal models. Here, we summarize and discuss this exciting recent progress in the mechanism and function of mitochondrial division and fusion.
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10

Sonn, Seong Keun, Seungwoon Seo, Jaemoon Yang, Ki Sook Oh, Hsiuchen Chen, David C. Chan, Kunsoo Rhee, Kyung S. Lee, Young Yang, and Goo Taeg Oh. "ER-associated CTRP1 regulates mitochondrial fission via interaction with DRP1." Experimental & Molecular Medicine 53, no. 11 (November 2021): 1769–80. http://dx.doi.org/10.1038/s12276-021-00701-z.

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AbstractC1q/TNF-related protein 1 (CTRP1) is a CTRP family member that has collagenous and globular C1q-like domains. The secreted form of CTRP1 is known to be associated with cardiovascular and metabolic diseases, but its cellular roles have not yet been elucidated. Here, we showed that cytosolic CTRP1 localizes to the endoplasmic reticulum (ER) membrane and that knockout or depletion of CTRP1 leads to mitochondrial fission defects, as demonstrated by mitochondrial elongation. Mitochondrial fission events are known to occur through an interaction between mitochondria and the ER, but we do not know whether the ER and/or its associated proteins participate directly in the entire mitochondrial fission event. Interestingly, we herein showed that ablation of CTRP1 suppresses the recruitment of DRP1 to mitochondria and provided evidence suggesting that the ER–mitochondrion interaction is required for the proper regulation of mitochondrial morphology. We further report that CTRP1 inactivation-induced mitochondrial fission defects induce apoptotic resistance and neuronal degeneration, which are also associated with ablation of DRP1. These results demonstrate for the first time that cytosolic CTRP1 is an ER transmembrane protein that acts as a key regulator of mitochondrial fission, providing new insight into the etiology of metabolic and neurodegenerative disorders.
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Дисертації з теми "Mitochondrial defects"

1

Bindoff, L. A. "Defects of mitochondrial oxidations." Thesis, University of Newcastle Upon Tyne, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.241373.

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2

Kollberg, Gittan. "Crisis in energy metabolism : mitochondrial defects and a new disease entity /." Göteborg : Department of Pathology, Institute of Biomedicine, The Sahlgrenska Academy at Göteborg University, 2007. http://hdl.handle.net/2077/779.

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3

Brierley, Elizabeth Jane. "Defects of mitochondrial DNA and mitochondrial energy production in ageing." Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.323477.

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4

Perry, Justin Bradley. "Novel approaches to treat mitochondrial complex-I mediated defects in disease." Diss., Virginia Tech, 2019. http://hdl.handle.net/10919/100602.

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Dysfunction within complex I (CI) of the mitochondrial electron transport system has been implicated in a number of disease states ranging from cardiovascular diseases to neuro-ophthalmic indications. Herein, we provide three novel approaches to model and study the impacts of injury on the function of CI. Cardiovascular ischemia/reperfusion (I/R) injury has long been recognized as a leading contributor to CI dysfunction. Aside from the physical injury that occurs in the tissue during the ischemic period, the production of high levels of reactive oxygen species (ROS) upon reperfusion, led by reverse electron transport (RET) from CI, causes significant damage to the cell. With over 700,000 people in the US set to experience an ischemic cardiac event annually, the need for a pharmacological intervention is paramount. Unfortunately, current pharmacological approaches to treat I/R related injury are limited and the ones that have shown efficacy have often done so with mixed results. Among the current approaches to treat I/R injury antioxidants have shown some promise to help preserve mitochondrial function and assuage tissue death. The studies described herein have provided new, more physiologically matched, methods for assessing the impact of potential therapeutic interventions in I/R injury. With these methods we evaluated the efficacy of the coenzyme-Q derivative idebenone, a proposed antioxidant. Surprisingly, in both chemically induced models of I/R and I/R in the intact heart, we see no antioxidant-based mechanism for rescue. The mechanistic insight we gained from these models of I/R injury directed us to further examine CI dysfunction in greater detail. Through the use of two cutting edge genetic engineering approaches, CRISPR/Cas9 and Artificial Site-specific RNA Endonucleases (ASRE), we have been able to directly edit the mitochondria to accurately model CI dysfunction in disease. The use of these genetic engineering technologies have provided first in class methods for modeling three unique mitochondrial diseases. The culmination of these projects has provided tremendous insight into the role of CI in disease and have taken a significant step towards elucidating potential therapeutic avenues for targeting decrements in mitochondrial function.
Doctor of Philosophy
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5

Fontes, Adriana Filipa da Silva. "Mitochondrial defects in proteasome and COP9 mutants." Master's thesis, Universidade de Aveiro, 2014. http://hdl.handle.net/10773/13273.

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Mestrado em Biotecnologia - Biotecnologia Molecular
The aim of this work is the study of phenotypic changes and mitochondrial morphology in Saccharomyces cerevisiae cells with specific mutations in genes involved in the ubiquitin-proteasome pathway. The protein turnover is important because it ensures organelles viability such as mitochondria, indispensable for cell survival. The COP9 complex is paralogous to the proteasome lid and eukaryotic translational initiator factor 3 (eIF3) complexes. The CSN5 subunit of the COP9 signalosome is responsible for the E3 ligase Cdc53/Cul1 activity through the removal of the ubiquitin-like protein, Rub1. Deletion of the Csn5 gene is lethal in high eukaryotes but not in yeast, this observation allow us to study the effects of this mutation in this organism (strain Δcsn5) together with other mutants or double mutants: rpn11-m1, Δrub1, rpn11-m1/Δcsn5 rpn11-m1/ Δrub1. Mutants and wildtype (W303-1A) were characterised regarding growth in different carbon sources and temperature as well as response to stress or DNA damage causing agents (methyl methanesulfonate and canavanin). The morphological results allowed us to investigate authophagy, and in particular mitophagy, through fluorescence microscopy (GFP-Atg8 and GFP-Atg32) and Western Blot analysis. We found a relation between deubiquitination undertaken by Rpn11 protein, from the 19S proteasome subunit, and the activation of rubylation/derubylation cycles by the CSN5 subunit of the CSN complex (COP9 signalosome). In fact, the rpn11-m1/ Δrub1 shows a semi-lethal phenotype and mitophagy in exponential phase in glucose rich medium. Also the Δcsn5 strain shows early mitophagy together with phenotypic changes, such as big vacuoles. In addition, it has been established a possible relationship between the CSN complex and the resilience to damage in the DNA caused by the methylating agent, methyl methanesulfonate (MMS).
O objectivo deste trabalho centrou-se no estudo das alterações fenotípicas e ao nível da morfologia mitocondrial em células de levedura Saccharomyces cerevisiae com mutações específicas em genes envolvidos na via de degradação proteica ubiquitinaproteasoma. O turnover proteíco é muito importante pois garante a viabilidade dos vários organelos celulares, de entre os quais, a mitochondria, cuja função principal é a produção de energia na forma de ATP. A subunidade Csn5 do COP9 signalosome, complexo com elevada similaridade com a lid proteasomal e com o factor 3 de iniciação translacional em eucariotas (eIF3), é responsável pela actividade da E3 ligase Cdc53/Cul1 através da remoção da proteina similar à ubiquitina, Rub1. A delação do gene que codifica para a subunidade Csn5 é letal em eucariotas superiores mas não em levedura o que nos permite estudar os seus efeitos juntamente com outros mutantes: rpn11-m1, Δrub1, rpn11-m1/Δcsn5 rpn11-m1/ Δrub1. Mutantes e wild-type (W303-1A) foram caracterizados a nível de crescimento em diferentes fontes de carbono e a diferentes temperaturas, assim como à resposta a factores causadores de dano ao nível do DNA e síntese proteica (sulfonato de metil metano e canavanina) juntamente com uma análise do potencial de membrana mitochondrial, autofagia/mitofagia através de microscopia de fluorescencia (GFP-Atg8 e GFP-Atg32) e Western Blot. Os resultados obtidos indicam que existe uma relação entre a acção de deubiquitinação da proteina Rpn11, da subunidade 19S do proteasome, e a activação dos ciclos de rubilação/ derubilação pela subunidade Csn5 do complex CSN (COP9 signalosome), sendo que o mutante rpn11-m1/Δrub1 apresenta um fenótipo semi-letal com instabilidade ao nível do DNA e alterações mitocôndriais que levam a um mitofagia em fase exponencial em meio rico em glucose. Por sua vez, o mutante rpn11-m1/Δcsn5 também revela mitofagia prematura em conjunto com alterações fenotípicas, como o aumento da dimensão celular (grande vacúolo), que ja é também evidente no mutante Δcsn5. Foi ainda estabelecida uma possível relação entre o complex CSN e a capacidade de resistência aos danos causados no DNA pelo agente metilante MMS.
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6

Yarham, John William. "Identification and characterisation of novel mitochondrial and nuclear mutations associated with mitochondrial translation defects." Thesis, University of Newcastle Upon Tyne, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613448.

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7

Almazan, Annabel Vivian P. "Overexpression of the human optic atrophy-associated OPA1 gene induces mitochondrial and cellular fitness defects in yeast." Wright State University / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=wright1590861295140841.

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8

Taylor, Claire Louise. "Biochemical investigations of defects of the mitochondrial respiratory chain." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.281706.

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9

Luca, Corneliu Constantin. "MTERFD3 is a Mitochondrial Protein that Modulates Oxidative Phosphorylation." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_dissertations/132.

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Mitochondrial function is critical for the survival of eukaryotes. Hence, mitochondrial dysfunctions are involved in numerous human diseases. An essential process for a normal mitochondrial function is mitochondrial gene expression which is tightly regulated in response to various physiological changes. The accurate control of mitochondrial gene expression is essential in order to provide the appropriate oxidative phosphorylation capacity for diverse metabolic demands. Recent findings in the basic mitochondrial replication and transcription regulation helped advance our understanding of organelle function and basic pathogenetic mechanisms of mitochondrial DNA mutations associated with oxidative phosphorylation defects. Mitochondrial transcription is regulated by the mitochondrial transcription termination factor (mTERF) both at the initiation and termination levels. A protein family containing highly conserved mTERF motifs has been identified recently and its members named generically as "terfins." In this work, one of these factors, mTERFD3, has been characterized in vitro and in vivo. The mTERFD3 protein is highly conserved throughout evolution. It is a mitochondrial protein localized to the matrix and is abundantly expressed in high energy demand tissues. We found that it contains 4 putative leucine zippers and is able to form dimers in vitro. We showed that mTERFD3 binds mtDNA at the transcription initiation site in the mtDNA regulatory region. These findings suggest that mTERFD3 may be involved in regulating mitochondrial gene expression at the transcriptional initiation level. In order to study the functional significance of mTERFD3 in vivo we developed a mouse deficient in mTERFD3 using a gene trapping strategy. The KO mice had a normal lifespan but showed decreased weight gain and decreased fat content in females. Fibroblasts isolated from KO mice displayed decreased growth rate when compared with WT in respiratory media, and had decreased complex IV activity. Consistent with the above findings, we found that muscle, one of the tissues with high energy demands, showed abnormal mitochondrial function, displaying features characteristic of mitochondrial myopathy such as decreased muscle strength and endurance. Muscle mitochondria of the KO mice showed a significant decrease in the complex II +III and complex IV activity. The decrease in OXPHOS complexes activity was associated with increased citrate synthase activity, suggesting mitochondrial proliferation, a feature typical for mitochondrial disorders. Another important finding was a decrease in the muscle mitochondrial transcripts in the KO animals associated with decreased steady state levels of OXPHOS subunits. Together these data suggest that mTERFD3 is a mitochondrial protein involved in the regulation of mtDNA transcription. mTERFD3 KO is not embryonic lethal suggesting that it is involved in the fine tuning of mitochondrial transcription. We conclude that mTERFD3 is a mitochondrial protein that modulates oxidative phosphorylation function, probably by directed interactions with the mtDNA regulatory region. This work shows the importance of mTERFD3, an mTERF family member, in the mitochondrial gene expression regulation.
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Lowerson, Shelagh Anne. "Defects of the mitochondrial respiratory chain : biochemical studies and mathematical modelling." Thesis, University of Newcastle Upon Tyne, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297572.

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Книги з теми "Mitochondrial defects"

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International Symposium on Glycolytic and Mitochondrial Defects in Muscle and Nerve (1995 Osaka, Japan). International Symposium on Glycolytic and Mitochondrial Defects in Muscle and Nerve, Osaka, Japan, July 7-8, 1994 ; Osaka Sun Palace (Expo Park Senti, Suita, Osaka. Edited by Tarui Seiichirō. New York: Wiley, 1995.

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2

Felberg, Mary A. Mitochondrial Disease and Anesthesia. Edited by Erin S. Williams, Olutoyin A. Olutoye, Catherine P. Seipel, and Titilopemi A. O. Aina. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190678333.003.0042.

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Mitochondrial disease is a genetically, biochemically, and clinically heterogeneous group of disorders that arise from defects in cellular oxidative phosphorylation, most commonly within the electron transport chain. All mitochondrial diseases involve disruption in energy production; clinical symptoms usually manifest in tissues with high energy demands although all organs may be affected. The extent of disease depends not only on the mitochondrial defect but on the numbers of dysfunctional mitochondria present in each tissue. Despite in vitro evidence that almost every anesthetic agent studied has been shown to decrease mitochondrial function, all anesthetic agents have been used safely. Discussion of the implications of mitochondrial disease for anesthetic management includes preoperative preparation, volatile and intravenous anesthetic agents, avoidance of succinylcholine, risk of malignant hyperthermia, perioperative fluids, and postoperative management.
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3

Mitochondrial Disorders: From Pathophysiology to Acquired Defects. Springer Paris, 2014.

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4

Desnuelle, Claude, and S. Di Mauro. Mitochondrial Disorders: From Pathophysiology to Acquired Defects. Springer London, Limited, 2013.

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5

Jou, J. Fay, Lori A. Aronson, and Jacqueline W. Morillo-Delerme. Mitochondrial Disorder for Muscle Biopsy. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199764495.003.0049.

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Mitochondrial disease (mtD) is a genetically, biochemically, and clinically heterogeneous group of disorders that arise most commonly from defects in the oxidative phosphorylation or electron transport chain involved in energy metabolism. These patients have an increased risk for cardiac, respiratory, neurologic, and metabolic complications from anesthesia. Consequently, there are several anesthetic considerations for patients with mtD.
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Duran, Marinus, and Isabel Tavares de Almeida. Interpretation of Acylcarnitine Analysis Results. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0085.

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The analysis of acylcarnitines in plasma or blood spot samples by tandem mass spectrometry will detect all 15 defects of mitochondrial fatty acid beta-oxidation, although false negative results may occur in well-fed, non-fasting patients. Moreover, more than 20 organic acidemias can be detected by this methodological approach. An acylcarnitine profile should be part of the work-up of patients presenting with rhabdomyolysis and/or hypoglycemia and adults with an unexplained leukoencephalopathy. Cases with abnormal acylcarnitines require an analysis of urine organic acids as well as enzyme activity evaluation and molecular investigations to confirm the inherited defect.
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Elliott, Perry, and Giuseppe Limongelli. Cardiac Aspects of INHERITED METABOLIC DISEASES. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0070.

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More than 40 inherited metabolic disorders cause heart disease, including fatty acid oxidation defects, glycogen storage disorders, lysosomal storage disorders, peroxisomal diseases, mitochondrial cytopathies, organic acidemias, aminoacidopathies, and congenital disorders of glycosylation. The pattern and severity of cardiac involvement varies between disorders but includes congenital heart diseases, heart muscle diseases, arrhythmias and sudden death, and heart failure. The majority of IMDs are multisystem diseases, but in a few cases cardiac disease is the predominant clinical feature and the main determinant of prognosis. For an increasing number of IEMs there are specific therapies designed to treat or ameliorate the effects of the underlying metabolic defect. In some cases, these therapies have an important effect on the progression of cardiac disease.
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Michels, Virginia V. Genetics. Oxford University Press, 2012. http://dx.doi.org/10.1093/med/9780199755691.003.0276.

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Genetic factors play a role in the development of many types of human disease. Genetic determinants may be chromosome abnormalities (Down syndrome, Kleinfelter syndrome, Turner syndrome), single gene defects (dilated and hypertrophic cardiomyopathies, Ehlers-Danlos syndrome, Marfan syndrome, neurofibromatosis, tuberous sclerosis, Gaucher disease, cystic fibrosis, sickle cell disease), mitochondrial mutations (MELAS, MERRF, Kearns-Sayre syndrome), or epigenetic or multifactorial factors. Genetics testing methods are also reviewed.
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Garcia-Pavia, Pablo, and Fernando Dominguez. Left ventricular non-compaction: genetics and embryology. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0362.

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Left ventricular non-compaction (LVNC) is a rare disorder that is considered an ‘unclassified cardiomyopathy’ by the European Society of Cardiology. Several different gene mutations related to LVNC have been identified, involving sarcomeric, cytoskeletal, Z-line, ion channel, mitochondrial, and signalling proteins. However, there is broad genetic overlap between LVNC and other inherited cardiac diseases such as dilated cardiomyopathy and hypertrophic cardiomyopathy. LVNC could also be part of multisystemic genetic entities such as Barth syndrome, or accompany congenital heart defects.
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Dionisi-Vici, Carlo, Diego Martinelli, Enrico Bertini, and Claude Bachmann. HHH Syndrome. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0020.

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Hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome is an autosomal recessive disorder of the urea cycle characterized by impaired transport of ornithine across the inner mitochondrial membrane. As seen in other urea cycle defects, in the acute phase the disease is characterized by intermittent episodes of hyperammonemia accompanied by vomiting, lethargy, and coma, with or without signs of acute liver failure. The disease course is characterized by a pyramidal tract dysfunction associated with myoclonic seizures and cerebellar symptoms. Most patients reaching adulthood manifest variable degrees of cognitive impairment and abnormal behavior. Long-term treatment consists of a low-protein diet supplemented with citrulline, arginine, or ornithine. Protein restriction may be combined with sodium benzoate. If plasma creatine levels are low, creatine supplementation should be instituted. Acute treatment is similar to other urea cycle defects.
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Частини книг з теми "Mitochondrial defects"

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Salviati, Leonardo. "Cytochrome c Defects in Human Disease." In Mitochondrial Diseases, 191–200. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-70147-5_7.

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Fernández-Moreno, Miguel A., Luis Vázquez-Fonseca, Sara Palacios Zambrano, and Rafael Garesse. "Mitochondrial DNA: Defects, Maintenance Genes and Depletion." In Mitochondrial Diseases, 69–94. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-70147-5_3.

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Oldfors, A. "Mitochondrial Defects in Myositis and Inclusion Body Myopathies." In Mitochondrial Disorders, 265–74. Paris: Springer Paris, 2002. http://dx.doi.org/10.1007/978-2-8178-0929-8_22.

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van der Knaap, Marjo S., and Jacob Valk. "Defects of Mitochondrial DNA." In Magnetic Resonance of Myelin, Myelination, and Myelin Disorders, 146–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-03078-3_21.

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Desnuelle, C., C. Richelme, and V. Paquis-Flucklinger. "Neurological Features of Genetic and Acquired Metabolic Mitochondrial Defects." In Mitochondrial Disorders, 193–210. Paris: Springer Paris, 2002. http://dx.doi.org/10.1007/978-2-8178-0929-8_16.

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Lenaz, Giorgio, Carla Bovina, Cinzia Castelluccio, Romana Fato, Gabriella Formiggini, Maria Luisa Genova, Mario Marchetti, et al. "Mitochondrial Complex I defects in aging." In Detection of Mitochondrial Diseases, 329–33. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-6111-8_50.

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Yu-Wai-Man, Patrick, Guy Lenaers, and Patrick F. Chinnery. "Defects in Mitochondrial Dynamics and Mitochondrial DNA Instability." In Mitochondrial Disorders Caused by Nuclear Genes, 141–61. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3722-2_9.

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Robinson, Brian H. "Nuclear Defects Affecting Mitochondrial Function." In Mitochondrial DNA Mutations in Aging, Disease and Cancer, 185–204. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-662-12509-0_10.

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Kunz, Wolfram S., Kirstin Winkler, Andrey V. Kuznetsov, Hartmut Lins, Elmar Kirches, and Claus W. Wallesch. "Detection of mitochondrial defects by laser fluorimetry." In Detection of Mitochondrial Diseases, 97–100. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-6111-8_15.

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Scaglia, Fernando. "Nuclear Gene Defects in Mitochondrial Disorders." In Methods in Molecular Biology, 17–34. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-504-6_2.

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Тези доповідей конференцій з теми "Mitochondrial defects"

1

Bölsterli, Bigna K., Eugen Boltshauser, Felix Distelmaier, Tobias Geis, Annick Klabunde-Cherwon, Raimund Kottke, Christine Makowski, et al. "Mitochondrial Transporter Defects: Successful Treatment with Ketogenic Diet Therapy." In Abstracts of the 46th Annual Meeting of the Society for Neuropediatrics. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1739697.

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Garcia-Carrizo, F., A. Jank, M. Ost, and T. Schulz. "Extracellular matrix dysfunction promotes mitochondrial defects and ectopic adipocyte infiltration in skeletal muscle." In Abstracts des Adipositas-Kongresses 2020 zur 36. Jahrestagung der Deutschen Adipositas Gesellschaft e.V. (DAG). © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1714460.

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Krželj, Vjekoslav, and Ivana Čulo Čagalj. "INHERITED METABOLIC DISORDERS AND HEART DISEASES." In Symposium with International Participation HEART AND … Akademija nauka i umjetnosti Bosne i Hercegovine, 2019. http://dx.doi.org/10.5644/pi2019.181.02.

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Анотація:
Inherited metabolic disorders can cause heart diseases, cardiomyopathy in particular, as well as cardiac arrhythmias, valvular and coronary diseases. More than 40 different inherited metabolic disorders can provoke cardiomyopathy, including lysosomal storage disorders, fatty acid oxidation defects, organic acidemias, amino acidopathies, glycogen storage diseases, congenital disorders of glycosylation as well as peroxisomal and mitochondrial disorders. If identified and diagnosed on time, some of congenital metabolic diseases could be successfully treated. It is important to assume them in cases when heart diseases are etiologically undefined. Rapid technological development has made it easier to establish the diagnosis of these diseases. This article will focus on common inherited metabolic disorders that cause heart diseases, as well as on diseases that might be possible to treat.
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Reimann, G., R. Gerlini, N. Spielmann, E. Heyne, M. Szibor, V. Gailus-Durner, T. Komlodi, et al. "Defect in Complex III of the Mitochondrial Electron Transfer System Affects Cardiac Insulin Sensitivity but Not Contractile Function." In 50th Annual Meeting of the German Society for Thoracic and Cardiovascular Surgery (DGTHG). Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1725679.

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Ashrafzadeh, Sepideh, Lauren D. Van Wassenhove, and Sofia D. Merajver. "Abstract 1695: Quantification of mitochondria in MCF-10A, MDA-MB-231, and SUM149 cells to understand potential defects in oxidative phosphorylation in cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1695.

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Звіти організацій з теми "Mitochondrial defects"

1

Shoffner, John M. Mechanisms of Mitochondrial Defects in Gulf War Syndrome. Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada612595.

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Shoffner, John M. Mechanisms of Mitochondrial Defects in Gulf War Syndrome. Fort Belvoir, VA: Defense Technical Information Center, August 2010. http://dx.doi.org/10.21236/ada536634.

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Shoffner, John M. Mechanisms of Mitochondrial Defects in Gulf War Syndrome. Fort Belvoir, VA: Defense Technical Information Center, August 2012. http://dx.doi.org/10.21236/ada567223.

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Shoffner, John. Mechanisms of Mitochondrial Defects in Gulf War Syndrome. Fort Belvoir, VA: Defense Technical Information Center, August 2011. http://dx.doi.org/10.21236/ada554016.

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