Abstract
The mitochondrion represents a unique organelle within the complex endomembrane systems that characterize any eukaryotic cell. It is realistic to state that complex life on earth has been made possible through the “acquisition” of mitochondria which provide an adequate supply of substrates for energy-expensive tasks. Higher multicellular organisms have indeed high-energy requirements necessary to carry out complex functions, such as muscle contraction, hormones and neurotransmitters synthesis and secretion, in addition to basal cellular metabolism (biomolecules synthesis and transformation, maintenance of ionic gradients across membrane, cell division). Mitochondria can fulfill this huge energy demand thanks to their extraordinary biosynthetic capacities: every day, mitochondria of a single human being can recycle up to 50 Kg of ATP. To further underline the relevance of these subcellular structures, one can also consider how these organelles have affected the physiology of the whole organism: lungs, heart, and circulatory system have evolved essentially to provide molecular oxygen to mitochondria, which consume about 98% of the total O2 we breathe. However, beyond the pivotal role they play in ATP production, a whole new mitochondrial biology has emerged in the last few decades: mitochondria have been shown to participate in many other aspects of cell physiology such as amino-acid synthesis, iron-sulphur clusters assembly, lipid metabolism, Ca2+ signaling, reactive oxygen species (ROS) production, and cell death regulation.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Dyall SD, Brown MT, Johnson PJ (2004) Ancient invasions: From endosymbionts to organelles. Science 304:253
Mokranjac D, Neupert W (2005) Protein import into mitochondria. Biochem Soc Trans 33:1019
Mannella CA (2006) Structure and dynamics of the mitochondrial inner membrane cristae. Biochim Biophys Acta 1763:542
Duchen MR (2004) Roles of mitochondria in health and disease. Diabetes 53:S96
Puigserver P, Wu Z, Park CW et al (1998) A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92:829
Liang H, Ward WF (2006) PGC-1alpha: A key regulator of energy metabolism. Adv Physiol Educ 30:145
Leone TC, Lehman JJ, Finck BN et al (2005) PGC-1alpha deficiency causes multisystem energy metabolic derangements: Muscle dysfunction, abnormal weight control and hepatic steatosis. PLoS Biol 3:e101
Lin J, Handschin C, Spiegelman BM (2005) Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab 1:361
Wu H, Kanatous SB, Thurmond FA et al (2002) Regulation of mitochondrial biogenesis in skeletal muscle by CaMK. Science 296:349
Handschin C, Rhee J, Lin J et al (2003) An autoregulatory loop controls peroxisome proliferator-activated receptor gamma coactivator lalpha expression in muscle. Proc Natl Acad Sci U S A 100:7111
Cadenas E, Davies KJ (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29:222
Harman D (1956) Aging: A theory based on free radical and radiation chemistry. J Gerontol 11:298
McCord JM, Fridovich I (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049
Balaban RS, Nemoto S, Finkel T (2005) Mitochondria, oxidants, and aging. Cell 120:483
Kang SW, Chae HZ, Seo MS et al (1998) Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 273:6297
Brand MD (2000) Uncoupling to survive? The role of mitochondrial inefficiency in ageing. Exp Gerontol 35:811
St-Pierre J, Drori S, Uldry M et al (2006) Suppression of reactive oxygen species and neurodegeneration by the PGC-1 transcriptional coactivators. Cell 127:397
Pelicci G, Lanfrancone L, Grignani F et al (1992) A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction. Cell 70:93
Pinton P, Rimessi A, Marchi S et al (2007) Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc. Science 315:659
Giorgio M, Migliaccio E, Orsini F et al (2005) Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 122:221
Marchenko ND, Zaika A, Moll UM (2000) Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J Biol Chem 275:16202
Frossi B, Tell G, Spessotto P et al (2002) H(2)O(2) induces translocation of APE/Ref-1 to mitochondria in the Raji B-cell line. J Cell Physiol 193:180
Majumder PK, Mishra NC, Sun X et al (2001) Targeting of protein kinase C delta to mitochondria in the oxidative stress response. Cell Growth Differ 12:465
Anesti V, Scorrano L (2006) The relationship between mitochondrial shape and function and the cytoskeleton. Biochim Biophys Acta 1757:692
Glater EE, Megeath LJ, Stowers RS, Schwarz TL (2006) Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J Cell Biol 173:545
Yi M, Weaver D, Hajnoczky G (2004) Control of mitochondrial motility and distribution by the calcium signal: A homeostatic circuit. J Cell Biol 167:661
Chan DC (2006) Mitochondrial fusion and fission in mammals. Annu Rev Cell Dev Biol 22:79
Chan DC (2006) Mitochondria: Dynamic organelles in disease, aging, and development. Cell 125:1241
Santel A (2006) Get the balance right: Mitofusins roles in health and disease. Biochim Biophys Acta 1763:490
Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239
Garrido C, Galluzzi L, Brunet M et al (2006) Mechanisms of cytochrome c release from mitochondria. Cell Death Differ 13:1423
Hill MM, Adrain C, Martin SJ (2003) Portrait of a killer: The mitochondrial apoptosome emerges from the shadows. Mol Interv 3:19
Ravagnan L, Roumier T, Kroemer G (2002) Mitochondria, the killer organelles and their weapons. J Cell Physiol 192:131
Danial NN, Korsmeyer SJ (2004) Cell death: Critical control points. Cell 116:205
Cipolat S, Martinsde BO, Dal ZB, Scorrano L (2004) OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc Natl Acad Sci U S A 101:15927
Frezza C, Cipolat S, Martins de BO et al (2006) OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126:177
Youle RJ, Karbowski M (2005) Mitochondrial fission in apoptosis. Nat Rev Mol Cell Biol 6:657
Szabadkai G, Simoni AM, Chami M et al (2004) Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+-mediated apoptosis. Mol Cell 16:59
Bernardi P, Krauskopf A, Basso E et al (2006) The mitochondrial permeability transition from in vitro artifact to disease target. FEBS J 273:2077
Basso E, Fante L, Fowlkes J et al (2005) Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D. J Biol Chem 280:18558
Nakagawa T, Shimizu S, Watanabe T et al (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434:652
Baines CP, Kaiser RA, Purcell NH et al (2005) Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434:658
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2007 Springer
About this chapter
Cite this chapter
De Stefani, D., Pinton, P., Rizzuto, R. (2007). Mitochondria in Cell Life and Death. In: Stocchi, V., De Feo, P., Hood, D.A. (eds) Role of Physical Exercise in Preventing Disease and Improving the Quality of Life. Springer, Milano. https://doi.org/10.1007/978-88-470-0376-7_9
Download citation
DOI: https://doi.org/10.1007/978-88-470-0376-7_9
Publisher Name: Springer, Milano
Print ISBN: 978-88-470-0375-0
Online ISBN: 978-88-470-0376-7
eBook Packages: MedicineMedicine (R0)