2009 Group 7 Project

From CellBiology

Mitochondria

Introduction

Mitochondria, commonly dubbed the 'powerhouses' of the cell, are cytoplasmic double-membraned organelles. The play key roles in respiration - the production of energy (ATP) and in apoptosis - a form of programmed cell death. Mitochondria have their own DNA, and mutations in this can lead to a wide variety of diseases, a prominent one being Alzheimer's Disease. [1]

History

Mitochondria Discovery Timeline
  • 1857 – Albert von Kolliker (1817-1905) reported mitochondria in muscle cells [2]
  • 1890 - Richard Altmann introduces the endosymbiotic theory and proposes that mitochondria are the evolutionary product of ingested bacteria. Named the structures ‘bioblasts’ [3]
  • 1898 - Carl Benda coins the term mitochondria from the greek ‘mitos’ meaning thread and ‘chondros’ meaning granule. [4]
  • 1925 – Keilin discovers the cytochrome system [5]
  • 1937 – Krebs formulates the citric acid cycle [6]
  • 1948 – First isolation of physically undamaged mitochondria by Hogeboom et al. [7]
  • 1952 – First high resolution electron micrographs of mitochondria published by Palade and Sjostrand [8]
  • 1953 – Slater proposes a chemical hypothesis for oxidative phosphorylation [9]
  • 1960 – Racker, Pullman, Penefsky & Datta isolate ATPase from beef heart submitochondrial particles [10]
  • 1963-64 – Nass and Nass discover mitochondrial DNA, along with Schatz et al., and Luck and Reich [11]
  • 1966-1969 – Levy et al, along with many other scientists, separate and characterise the inner and outer mitochondrial membranes [12]
  • 1975-76 – Molloy et al & Schweyen et al. produce a genetic map of yeast mitochondrial DNA [13]
  • 1979-1980 – Numerous scientists e.g. Hensgens et al produce evidence of the nucleotide sequence of mitochondrial genes. [14]
  • 1992 – Wallace provides evidence for a connection between mutations of mitochondrial DNA and disease [15]
  • 1998 – Complete sequence of yeast mtDNA is published [16][17]
  • 2000 - Establishment of the Mitochondria Research Society
Two main theories of mitochondria evolution

Evolution [18]

  • Main theory is the endosymbiont hypothesis
  • This theory is based on the idea that anaerobic organisms phagocytosed eubacteria-like organisms and utilised their oxidative phosophorylation for energy production.
  • Idea of a evolving from 'foreign' organisms is upheld as mitochondria have their own DNA separate from the cell
  • These phagocytosed organisms were then called ‘endosymbionts’
  • Believed to have happened around 1.5 x 10 x 9 years ago
  • Mitochondrial genome was transferred in to the host nucleus
  • Genome size range from just under 6kBp in Plasmodiumfalciparum (malaria parasite) to over 200kBp in plants

Structure

Structural Components of the Mitochondrion (starting top left and moving clockwise): Respiratory Chain Complexes, Porins, Cardiolipins and ATPases.

Mitochondria are mobile structures with high plasticity. They are made up of an outer membrane, inter membranous space, inner membrane, cristae and mitochondrial matrix. Purification and fractionation processes have allowed the analysis of the various components of this organelle[19]. It is often referred to as the ‘power house’ of the cell since one of the key functions of this organelle is to produce the body’s energy source; Adenosine Triphosphate (ATP).

Mitochondria are usually dispersed throughout the cytoplasm of a eukaryotic cell. Their location within the cell is based centrally upon the area which requires most energy, for example a higher concentration of mitochondria will be present in the flagella region of sperm as opposed to its head.


Outer Membrane

The outer membrane is filled with a transport protein called porin. The porins are made of B-strands which are arranged to form beta barrels throughout the outer mitochondrial membrane; research shows this structure of porins is very similar to that found in bacterial porins[20]

Porins allow the selective passage of molecules up to 5000D in size to pass through to the inter-membranous space. Other crucial proteins and enzymes are also present on the outer membrane. An example is 5 Aminolevulinic acid synthase which is the enzyme involved in heme biosynthesis[21] . Also, the ‘Bcl-2–associated X protein (BAX), which integrates into the outer mitochondrial membrane; it is important for cytochrome c release and hence apoptosis[22] .

Inner Membrane

The inner membrane acts as the ‘functional barrier’ to passage of small molecules from between the cytosol and the matrix. This high specificity is due to the composition of the lipid bi-layer which constitutes the inner membrane. The lipid bi-layer contain four fatty acids rather than two, these double phospholipids are called cardiolipin.

An important feature of the inner membrane is that it contains the electron transport chain. Energy for ATP synthesis is sequestered here. It is a very crucial structure of the mitochondria due to tis function; also because many diseases have been directly linked to malformations in the chain.

Cristae

These are the invaginations of the convoluted inner membrane into the matrix. Cristae greatly increase the surface area of the inner membrane which allows mitochondria to meet the metabolic demands of the cell. The amount of cristae in mitochondria varies depending on which cell the mitochondria are in. For example, in hepatic cells, the area of the inner membrane is five times the total area of the outer membrane. Also, a cardiac cell will have much higher cristae than a liver cell due to its higher demand for ATP[23].

Interestingly, research has shown that beta adrenoceptor agonists can increase the cristae to matrix ration as well as mitochondrial size. Hence the structure of mitochondria is dynamic and can be manipulated. Mitochondria are current targets for improving the low energy status of hearts in heart failure[24] .

Matrix

Mitochondria are the only organelles within the eukaryotic cell that contain their own set of DNA. For humans, this DNA, found in the matrix of the mitochondria, encodes for some mitochondrial proteins and encodes for 22 tRNAs as well as 16S and 12S rRNAs. The matrix also contains metabolic enzymes of the citric acid cycle[25].

Interestingly mitochondrial DNA plays a key role in ageing. Over time, humans collect a series of mutations in their mitochondrial DNA which result in decreased function of mitochondria. Hence eventually people have less efficiently working mitochondria which lead to an inevitable death in old age. It is believed that reducing reactive oxygen species, which are thought to cause a large portion of the damage, will slow the ageing process[26].

Function: Energy Production

As mentioned above, the structure of the mitochondria is fundamental to its function of energy production. Dynamic processes with multiple paths are involved in the production of energy rich ATP molecules and carbon dioxide from oxygen, pyruvate and fatty acids. The inner membrane and the components of the matrix of the mitochondria are the major components with which the reactants (pyruvate, fatty acids, acetylCoA and later NADH and FADH2) interact with to result in a final product (ATP), usable by the cell. The processes occur in the following order:

Glycolysis

The sugar molecule, Glucose, must first be broken down to pyruvate, ATP and NADH in the process of glycolysis. Glycolysis is a multi-step process which occurs in the cell cytosol independant of mitochondria and results in the net production of 2 pyruvate, 2 ATP and 2 NADH per molecule of glucose. Glycolysis can provide the cell with some energy but more importantly it provides the cell with the pyruvate molecules necessary for the much more efficient aerobic respiration which occurs within the mitochondria;[27][28][29]

Diagramatic representation of the Citric Acid Cycle in the mitochondrial matrix

Production of acetyl CoA

After glycolysis, pyruvate and fatty acids are translocated across the outer and inner membranes of the mitochondria to the matrix where they are converted to acetyl CoA. Pyruvate is converted to acetyl CoA by a multi-enzyme complex, pyruvate dehydrogenase, and CO2 and one molecule of NADH is yielded (Oxidation of pyruvate#1, Oxidation of pyruvate #2), while fatty acids must first be activated to form fatty-acylCoa and then undergo a repetitive break down cycle which yields two acetyl CoA molecules and one molecule each of NADH and FADH2 per cycle(Oxidation of Fatty Acids)[30][31][32].

Oxidative phosphorylation in the electron transport chain

Citric Acid Cycle

In the matrix, acetylCoA is oxidised in the citric acid cycle, or Krebs cycle, to CO2 and high-energy electrons carried in the molecules NADH and FADH2 as well as in GTP. This process also occurs in the matrix and involves a complex set of reactions which are facilitated by a set of mitochondrial enzymes. The end products of this cycle are then used in the electron transport chain.[33][34][35].

Electron Transport Chain

In the electron transport chain high-energy electrons are lost from NADH and FADH2 as well as from intermediates from the citric acid cycle. This occurs in the inner mitochondrial membrane where protein complexes embedded there transfer the electrons through the inner membrane, and reduce O2 to H20 whilst also pumping protons into the inter-membrane space. The proton gradient created across the inner membrane is then used as the driving force for the enzyme ATP synthase located on the inner membrane, resulting in the conversion of ADP + Pi → ATP[36][37][38].



Function: Apoptosis

All cells are programmed to die at a specific point in time so that the body, as a whole, can remain effective in its various processes. The mitochondria are main players in carrying out the apoptotic process.

Fas receptor activation and its consequences.

Death Signals

Apoptosis in cells is triggered either by increased uptake of Ca2+ by the cell or by cell reception of apoptotic signals[39] . A common apoptotic signal for cells is tumour necrosis factor (TNF)[40]. This binds to Fas receptors on the cell membrane.

Both increased intracellular Ca2+ and binding of TNF to Fas receptors have effects on the mitochondria of the cell which are intrinsic to the apoptotic process.

Structure of the Apoptosome.

Calcium Levels in the Cell

Ca2+ levels within a cell must be kept within a very specific range (typically around 100nM[41]) and, hence, a regulator and storage place for Ca2+ within the cell is essential. The endoplasmic reticulum is the organelle responsible for calcium storage while the mitochondrion is an important regulator of its levels[42] . The mitochondria are effective regulators of calcium levels for the following reasons:

  1. They are able to take up Ca2+ (if its levels are greater than 300 μM in the cytoplasm)[43] and
  2. They are relatively close to the endoplasmic reticulum, the storer of calcium.

Fas Receptor Activation

Fas receptor activation leads to procaspase-8 activation[44]. Like all procaspases, procaspase-8 is called caspase-8 in its active form. Caspases, which are proteases only significantly present in cells during apoptosis, break down the proteins essential for cell survival[45]. Caspase-8 specifically cleaves Bid, a Bcl-2 protein inducing apoptosis, which then moves into the mitochondrion for action[46].

Note: Bcl-2 proteins are proteins that either protect the mitochondrial membrane from damage or attack it; they can promote cell survival or cell death[47].

DNA Condensation induced by caspase 3 and DFF (bottom left).

Mitochondrial Cytochrome C Release

Cytochrome C release from the mitochondria through permeability transition pores[48] is encouraged by both high mitochondrial calcium levels and cleavage of Bid. Bid causes cytochrome C release by disrupting the inner mitochondrial membrane.

The release of cytochrome C into the cytoplasm is prominent in apoptosis because:

  1. the pro-caspase 9/APAF-1/cytochrome C complex (the apoptosome) becomes complete and pro-caspase 9 is converted into caspase-9[49][50]. Caspase-9 activation, like caspase-8 activation, will lead to the activation of the caspase cascade.
  2. cytochrome C can bind to IP3 receptors on the ER membrane to release calcium from it[51]. This causes even further cytochrome C release from the mitochondria due to the positive feedback mechanism present.

The Caspase Cascade

The caspase cascade is triggered by activated caspases. It leads to large numbers of nucleases and proteases being present in the cell which cleave DNA and the countless proteins necessary for cell survival (eg. nuclear lamins and cytosolic proteins)[52].

In research, caspase-3 and caspase-7 have been found to be important in the eventual cleavage of DNA. These two caspases cleave the inactivated form of DNA Fragmentation Factor (DFF), also known as Caspase-Activated DNase(CAD)[53] . DFF/CAD then begins to attack chromatin, a phenomenon which causes the observable chromatin condensation in the nuclei of affected cells.

Death

The high calcium, destroyed DNA and destroyed proteins from the above processes signal for apoptosis to continue within the cell.

Diseases

Mitochondrial proteins are of both nuclear and mitochondrial origins and the assembly of mitochondrial protein complexes also requires nuclear encoded factors. [54]. Therefore a large scope of mutations may contribute to mitochondrial dysfunction. On top of this, the electron transport chain involves the release of reactive oxygen species (ROS) which contribute to mitochondrial damage in a range of pathologies[55].

The United Mitochondrial Disease Foundation lists 43 groups of diseases associated with mitochondrial dysfunction. The OMIM database also lists over 700 entries for the mitochondria and known mendelian disorders.

Current Research

There is a huge amount of current research on mitochondria. Pubmed shows 1165 articles published on mitochondria in the past 3 months. UNSW has research projects in the School of Biotechnology and Biomolecular Sciences surrounding mitochondrial bioenergetics, aging and the link with Drosophilia

  • MFN2 and its functions relating to mitochondria beyond fusion
  • Mitochondria DNA mutation and the effect on aging[56]
  • Use of GFP to find localizations of Hepatitis C virus in mitochondria[57]
  • Connection between mitochondria function and Alzheimer's disease[58]
  • Connection between mitochondria and apoptosis in Parkinson's disease[59]
  • Use of mitochondria as a target for chemotherapy treatment[60][61]
  • Mitochondria and Reactive Oxygen species in aging[62]

Glossary of Terms

Apoptosis = a form of programmed cell death that most cells exhibit.

Apoptosome = the complex activating procaspase-9. It is composed of Apaf-1, cytochrome c, procaspase-9 and requires ATP.

ATP = adenosine triphosphate, the principal carrier molecule for energy used by cells.

Caspase = a protease activated during apoptosis.

Eubacteria = a large group of bacteria ('unicellular') having rigid cell walls.

Fractionation = a process that uses heat to separate a substance into its components.

GTP = guanosine triphosphate, a secondary energy carrier molecule used by cells with guanosine as opposed to adenine in ATP.

Oxidation = the loss of electrons.

Proton = in the instance of a proton gradient inside mitochondria, a proton refers to an oxidised hydrogen molecule, i.e. without any electons (H+).

Reduction = the gaining of electons.

References

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  3. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  4. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  5. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  6. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  7. From Microsomes to Ribosomes: ',Strategies" of "Representation" Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. PMID: 7033239
  8. From Microsomes to Ribosomes: ',Strategies" of "Representation" Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. PMID: 7033239
  9. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  10. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  11. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  12. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  13. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  14. Mitochondria: a historical review. Ernster L, Schatz G. J Cell Biol. 1981 Dec;91(3 Pt 2):227s-255s. Review.PMID: 7033239
  15. : Diseases of the mitochondrial DNA.Wallace DC.Annu Rev Biochem. 1992;61:1175-212. Review. PMID: 1497308
  16. The curious history of yeast mitochondrial DNA. Williamson D. Nat Rev Genet. 2002 Jun;3(6):475-81. Review. PMID: 12042774
  17. The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae.Foury F, Roganti T, Lecrenier N, Purnelle B.FEBS Lett. 1998 Dec 4;440(3):325-31.PMID: 9872396
  18. Mitochondrial genome evolution and the origin of eukaryotes. Lang BF, Gray MW, Burger G.Annu Rev Genet. 1999;33:351-97. Review. PMID: 10690412
  19. Molecular Biology of the Cell Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002 Bookshelf Link
  20. The evolutionary history of mitochondrial porins.Young MJ, Bay DC, Hausner G, Court DA.BMC Evol Biol. 2007 Feb 28;7:31. PMID: 17328803.
  21. Frederick J. Suchy, R. J. (2001). Liver Disease in Children. Lippincott Williams & Wilkins. Click here to see original work.
  22. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Eskes R, Desagher S, Antonsson B, Martinou JC. Mol Cell Biol. 2000 Feb;20(3):929-35.PMID: 10629050
  23. Molecular Cell Biology 4th ed., Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James E., New York: W. H. Freeman & Co., 1999. The Cell- A Molecular Approach Bookshelf Link
  24. Mitochondria in the human heart.Lemieux H, Hoppel CL.J Bioenerg Biomembr. 2009 Apr 8. [Epub ahead of print]PMID: 19353253
  25. The Cell - A Molecular Approach 2nd ed., Cooper, Geoffrey M., Sunderland (MA): Sinauer Associates, Inc., 2000. Bookshelf Link
  26. Mitochondrial DNA mutations in human disease.Taylor RW, Turnbull DM.Nat Rev Genet. 2005 May;65):389-402. Review.PMID: 15861210
  27. Molecular Biology of the Cell, Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002. Chapter 2, How Cells Obtain Energy From Food, & Molecular Biology of the Cell "The Mitochondrion"
  28. Molecular Cell Biology, Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James E. New York: W. H. Freeman & Co.; c1999. Chapter 16. Cellular Energetics: Glycolysis, Aerobic Oxidation, and Photosynthesis
  29. The Cell - A Molecular Approach, Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000, Chapter 2, Metabolic Energy, link
  30. Molecular Biology of the Cell, Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002. Chapter 2, How Cells Obtain Energy From Food, & Molecular Biology of the Cell "The Mitochondrion"
  31. Molecular Cell Biology, Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James E. New York: W. H. Freeman & Co.; c1999. Chapter 16. Cellular Energetics: Glycolysis, Aerobic Oxidation, and Photosynthesis
  32. The Cell - A Molecular Approach, Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000, Chapter 2, Metabolic Energy, link
  33. Molecular Biology of the Cell, Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002. Chapter 2, How Cells Obtain Energy From Food, & Molecular Biology of the Cell "The Mitochondrion"
  34. Molecular Cell Biology, Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James E. New York: W. H. Freeman & Co.; c1999. Chapter 16. Cellular Energetics: Glycolysis, Aerobic Oxidation, and Photosynthesis
  35. The Cell - A Molecular Approach, Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000, Chapter 2, Metabolic Energy, link
  36. Molecular Biology of the Cell, Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002. Chapter 2, How Cells Obtain Energy From Food, & Molecular Biology of the Cell "The Mitochondrion"
  37. Molecular Cell Biology, Lodish, Harvey; Berk, Arnold; Zipursky, S. Lawrence; Matsudaira, Paul; Baltimore, David; Darnell, James E. New York: W. H. Freeman & Co.; c1999. Chapter 16. Cellular Energetics: Glycolysis, Aerobic Oxidation, and Photosynthesis
  38. The Cell - A Molecular Approach, Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000, Chapter 2, Metabolic Energy, link
  39. Calcium orchestrates apoptosis. Mattson MP, Chan SL. Nat Cell Biol. 2003 Dec;5(12):1041-3. PMID: 14647298
  40. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000- IV. Cell Regulation Chapter 13. Cell Signaling
  41. Biochemistry - II. Transducing and Storing Energy 15.3 Calcium Ion Is a Ubiquitous Cytosolic Messenger, Berg, Jeremy M.; Tymoczko, John L.; and Stryer, Lubert. New York: W. H. Freeman and Co.; c2002
  42. Cell Metabolism Chapter taken from the Madame Curie Bioscience Database (formerly, Eurekah Bioscience Database) Eurekah.com and Landes Bioscience and Springer Science+Business Media; c2009 - ER Calcium and ER Chaperones: New Players in Apoptosis?
  43. Cell Metabolism Chapter taken from the Madame Curie Bioscience Database (formerly, Eurekah Bioscience Database) Eurekah.com and Landes Bioscience and Springer Science+Business Media; c2009 - ER Calcium and ER Chaperones: New Players in Apoptosis?
  44. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000 Cell death receptors
  45. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000- IV. Cell Regulation Chapter 13. Cell Signaling
  46. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000- IV. Cell Regulation Chapter 13. Cell Signaling
  47. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000- IV. Cell Regulation Chapter 13. Cell Signaling
  48. Hill, Mark (2009). 2009 Lecture 18 - Cellbiology. Retrieved May 30, 2009, from Cell Biology Wiki Web site: http://cellbiology.med.unsw.edu.au/cellbiology/index.php?title=2009_Lecture_18#Mitochondrial_Pathway
  49. Molecular Biology of the Cell Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002 Induction of apoptosis by either extracellular or intracellular stimuli
  50. The Cell- A Molecular Approach Cooper, Geoffrey M. Sunderland (MA): Sinauer Associates, Inc.; c2000 Regulators and effectors of apoptosis
  51. Calcium orchestrates apoptosis. Mattson MP, Chan SL. Nat Cell Biol. 2003 Dec;5(12):1041-3. PMID: 14647298
  52. Molecular Biology of the Cell Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walter, Peter New York and London: Garland Science; c2002 The caspase cascade involved in apoptosis
  53. Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G. Widlak P, Garrard WT. J Cell Biochem. 2005 Apr 15;94(6):1078-87. Review. PMID: 15723341
  54. Multiple defects in the respiratory chain lead to the repression of genes encoding components of the respiratory chain and TCA cycle enzymes. Bourges I, Mucchielli MH, Herbert CJ, Guiard B, Dujardin G, Meunier B. J Mol Biol. 2009 Apr 17;387(5):1081-91. Epub 2009 Feb 23. PMID: 19245817
  55. How mitochondria produce reactive oxygen species. Murphy MP. Biochem J. 2009 Jan 1;417(1):1-13. Review. PMID: 19061483
  56. Respiratory Function Decline and DNA Mutation in Mitochondria, Oxidative Stress and Altered Gene Expression during Aging. Wei YH, Wu SB, Ma YS, Lee HC. Chang Gung Med J. 2009 Mar-Apr;32(2):113-32. PMID: 19403001
  57. Subcellular localizations of the hepatitis C virus alternate reading frame proteins.Ratinier M, Boulant S, Crussard S, McLauchlan J, Lavergne JP.Virus Res. 2009 Jan;139(1):106-10. Epub 2008 Nov 28.PMID: 18996421
  58. An integrative view of the role of oxidative stress, mitochondria and insulin in Alzheimer's disease. Moreira PI, Duarte AI, Santos MS, Rego AC, Oliveira CR. J Alzheimers Dis. 2009 Apr;16(4):741-61. PMID: 19387110
  59. Endoplasmic reticulum and mitochondria interplay mediates apoptotic cell death: Relevance to Parkinson's disease. Arduíno DM, Esteves AR, Cardoso SM, Oliveira CR. Neurochem Int. 2009 Apr 16. [Epub ahead of print] PMID: 19375464
  60. Mitochondria as targets for cancer therapy. Ralph SJ, Neuzil J. Mol Nutr Food Res. 2009 Jan;53(1):9-28. PMID: 19123183
  61. Mitochondria as targets for cancer chemotherapy. Gogvadze V, Orrenius S, Zhivotovsky B. Semin Cancer Biol. 2009 Feb;19(1):57-66. Epub 2008 Dec 3. Review. PMID: 19101636
  62. Current thoughts on the role of mitochondria and free radicals in the biology of aging. Van Remmen H, Jones DP. J Gerontol A Biol Sci Med Sci. 2009 Feb;64(2):171-4. Epub 2009 Jan 30. Review. No abstract available. PMID: 19181714

Group Reflection

Overall, the group project was a great learning experience. We learnt a lot about mitochondria, their unique structure and the pivotal roles they play within the cell. We were also able to understand that abnormalities in mitochondria can cause quite detrimental effects on affected individuals and that current research is continuing to look into ways to reverse these effects.

With regards to the wiki writing and editing process, I think it's safe to say that everyone felt quite comfortable with it. During the earlier stages of making the project, we were a little unsure about some of the commands but by the end of it we were all competent with putting pictures, links and text up.

Reviewing peer wikis was definitely a good learning experience and we found that we had a lot to say to help our fellow groups out. We tried to put our criticism in positive, contructive terms - this was probably the hardest part to do. Overall, however, we think that peer reviewing is great because it definitely helped us to refine our site. It should definitely be kept a part of this project.

Below are the edits made up until 6:15pm, June 2.

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2009 Group Projects

Group 1 Meiosis | Group 2 Cell Death - Apoptosis | Group 3 Cell Division | Group 4 Trk Receptors | Group 5 The Cell Cycle | Group 6 Golgi Apparatus | Group 7 Mitochondria | Group 8 Cell Death - Necrosis | Group 9 Nucleus | Group 10 Cell Shape