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Mitochondria in Health and Diseases
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Mitochondria are subcellular organelles evolved by the endosymbiosis of bacteria with eukaryotic cells. They are the main source of ATP in the cell and engaged in other aspects of cell metabolism and cell function, including the regulation of ion homeostasis, cell growth, redox status, and cell signaling. Due to their central role in cell life and death, mitochondria are also involved in the pathogenesis and progression of human diseases/conditions, including neurodegenerative and cardiovascular disorders, cancer, diabetes, inflammation, and aging. However, despite the increasing number of studies, precise mechanisms whereby mitochondria are involved in the regulation of basic physiological functions, as well as their role in the cell under pathophysiological conditions, remain unknown. A lack of in-depth knowledge of the regulatory mechanisms of mitochondrial metabolism and function, as well as interplay between the factors that transform the organelle from its role in pro-survival to pro-death, have hindered the development of new mitochondria-targeted pharmacological and conditional approaches for the treatment of human diseases. This book highlights the latest achievements in elucidating the role of mitochondria under physiological conditions, in various cell/animal models of human diseases, and in patients.

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Keywords

  • 2-oxoglutarate dehydrogenase
  • 4-HNE
  • adenine nucleotide translocase
  • ADP/ATP carrier
  • Aging
  • amino acid neurotransmitter
  • ancient mutation
  • antioxidant system
  • Antioxidants
  • Apoptosis
  • BAX
  • BCL-2
  • BKCa channels
  • cardiolipin
  • cardiomyocytes
  • cardioprotection
  • cerebellar amino acid metabolism
  • cholangiocellular carcinoma
  • colon
  • complex I (CI) deficiency
  • cyclosporin A
  • cytoskeletal proteins
  • DDE
  • dentate granule cell
  • Development
  • dextran
  • DRP1
  • dsRNA
  • electron and confocal microscopy
  • electron tunneling (ET)
  • Energy Metabolism
  • Epilepsy
  • Erk1/2
  • ETC complexes
  • fatty acid oxidation
  • ferritin
  • gemfibrozil
  • GW9662
  • H9c2 cardiomyoblasts
  • healthy cells
  • Heart
  • hepatic fibrogenesis
  • hepcidin
  • high-fat diet
  • Hippocampus
  • HtrA2/Omi
  • human amniotic membrane
  • human diseases
  • hyperforin
  • Hypoglycemia
  • hypoxia
  • Inflammation
  • innate immunity
  • inorganic phosphate
  • interferon response
  • intranuclear mitochondria
  • ion homeostasis
  • iron overload
  • ischemia reperfusion injury
  • JNK
  • KmADP
  • Langendorff
  • LHON
  • life span
  • lipid droplet
  • lipid handling
  • Liver
  • LONP1
  • medicine
  • metabolome and proteome profiling
  • Mitochondria
  • mitochondria bioenergetics
  • mitochondria calcium buffering
  • mitochondria permeability transition pore
  • mitochondria: energy metabolism
  • mitochondrial cell death
  • mitochondrial connexin 43
  • mitochondrial dynamics
  • Mitochondrial dysfunction
  • mitochondrial function
  • mitochondrial gene expression
  • mitochondrial homeostasis
  • mitochondrial interactions
  • mitochondrial permeability transition pores
  • mitochondrial UCP2
  • Morphology
  • mtDNA
  • mtDNA transcription
  • mtRNA
  • muscle aging
  • myocardial
  • neuron death
  • Neuroprotection
  • oxidative phosphorylation
  • Oxidative Stress
  • perilipin 5
  • physical performance
  • pilocarpine
  • pioglitazone
  • PKA
  • plectin
  • post-transcriptional mtRNA processing
  • potassium channel
  • pravastatin
  • protein phosphatases
  • pyruvate dehydrogenase
  • pyruvate dehydrogenase kinase
  • Reactive Oxygen Species
  • reactive oxygen species (ROS)
  • reactive oxygen species stress
  • redox state
  • Regeneration
  • respirasome assembly
  • respiratory supercomplexes
  • ROS
  • rosiglitazone
  • seizure
  • Siberian population
  • signaling
  • signaling pathways
  • siRNA
  • sodium dichloroacetate
  • specific genetic background
  • telomerase activity
  • telomere length
  • tensile strength
  • transferrin
  • tricarboxylic acid cycle
  • tubulin beta
  • TUNEL
  • TZD
  • Uncoupling
  • uncoupling protein
  • ZIP

Links

DOI: 10.3390/books978-3-03936-385-8

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