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The Formation and Change of Cytochrome-c-oxidase in the Mitochondria of the Bovine Cardiac Muscle  

Kim, Soo-Jin (Department of Life Science, College of Natural Science, Hallym University)
Publication Information
Applied Microscopy / v.38, no.2, 2008 , pp. 125-133 More about this Journal
Abstract
Cytochrome-c-oxidase in mitochondria membrane is one of the most important factors for energy generation in the cell. As well as it is electron transfer enzyme, it is also heavily related to the apoptosis and other pathologic conditions. Meanwhile, porin is a protein located in inner and outer membranes of mitochondria, which is assumed to be functionally correlated with cytochrome-c-oxidase. It functions as forming electron transfer chain and conveying ATP. Therefore, using the immune-microscopy, It compared the distribution of cytochrome-c-oxidase and porin to figure out the formation and changes on cytochrome-c-oxidase in mitochondrial cristae. The sarcroplasm of cardic muscle tissue has many mitochondria. They are classified into two groups: the mitochondria with many cytochrome-c-oxidase and the mitochondria with only porins. The mitochondria with porins had few cytochrome-c-oxidases in their membrane; in contrast, the other mitochondria with rich cytochrome-c-oxidase had few porins in their walls. In addition, according to the location of the tissue in bovine heart, distribution of those kind of mitochondria had been clearly separated. As a result, it could be assumed that immature mitochondria has many porins to transfer the protein materials from sarcroplasm through the porins, and they made cytochrome-c-oxidase until it is enough, and then they decreased the porin and maintained minimum number of the porin.
Keywords
Cytochrom-c-oxidase; Porin protein; Bovine cardiac muscle tissue Immunogold labeling; Immuno-florescence labeling;
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1 Jamal JA: Involvement of porin N,N-dicyclohexylcarbodiimidereactive domain in hexokinase binding to the outer mitochondrial membrane. Protein J 24(1) : 1-8, 2005
2 Linden M, Gellerfors P, Nelson BD: Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane. Biochem J 208 : 77-82, 1982   DOI
3 Persichini T, Mazzonea V, Polticelli F, Morenoa S, Venturini G, Clementi E, Colasanti M: Mitochondrial type I nitric oxide synthase physically interacts with cytochrome c oxidase. Neuroscience Letters 384 : 254-259, 2005   DOI   ScienceOn
4 Rostovtseva T, Colombini M: VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J 72(5) :1954-1962, 1997   DOI   ScienceOn
5 Prabu SK, Anandatheerthavarada HK, Raza H, Srinivasan S, Spear JF, Avadhani NG : Protein kinase A-mediated phosphorylation modulates cytochrome c oxidase function and augments hypoxia and myocardial ischemia-related injury. The Journal of Biological Chemistry 281(4) : 2061-2070, 2006   DOI   ScienceOn
6 De Pinto V, Benz R, Caggese C, Palmieri F: Characterization of the mitochondrial porin from Drosophila melanogaster. Biochim Biophys Acta 987(1) : 1-7, 1989   DOI   ScienceOn
7 Sedlak E, Panda M, Dale MP, Weintraub ST, Robinson NC: Photolabeling of cardiolipin binding subunits within bovine Heart cytochrome c oxidase. Biochemistry 45 : 746-754, 2006   DOI   ScienceOn
8 Colombini M: A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279(5714) : 643-645, 1979   DOI   ScienceOn
9 Huttemann M, Schmidt TR, Grossman LI: A third isoform of cytochrome c oxidase subunit VIII is present in mammals. Gene 312 : 95-102, 2003   DOI   ScienceOn
10 Abrecht H, Wattiez R, Ruysschaert JM, Homble F: Purification and characterization of two voltage-dependent anion channel isoforms from plant seeds. Plant Physiol 124 : 1181-1190, 2000   DOI
11 Schein SJ, Colombini M, Finkelstein A: Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J Membr Biol 30(2) : 99-120, 1976   DOI
12 Shiva S, Oh JY, Landar AL, Ulasova E, Venkatraman A, Bailey SM, Darley-Usmar VM: Nitroxia: the pathological consequence of dysfunction in the nitric oxide-cytochrome c oxidase signaling pathway. Free Radic Biol Med 38(3) : 297-306, 2005   DOI   ScienceOn
13 Vik SB, Georgevich G, Capaldi RA: Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase. Biochemistry 78(3) : 1456-1460, 1981
14 Kim SJ, Lee KO, Takamiya S, Capaldi RA: Mitochondrial myopathy involving uviquinol-cytochrome-c-oxidoreductase (complex III) identified by immunoelectron microscopy. Biochem Biophys Acta 894 : 270-279, 1987   DOI   ScienceOn
15 Hanson BJ, Capaldi RA, Marusich MF, Sherwood SW: An immunocytochemical approach to detection of mitochondrial disorders. The Journal of Histochemistry & Cytochemistry 50(10) : 1281-1288, 2002   DOI   ScienceOn
16 Heins L, Mentzel H, Schmid A, Benz R, Schmitz UK: Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria. J Biol Chem 269(42) : 26402-26410, 1994
17 Piana GL, Marzullib M, GorgoglioneV, Lofrumento NE: Porin and cytochrome oxidase containing contact sites involved in the oxidation of cytosolic NADH. Archives of Biochemistry and Biophysics 436 : 91-100, 2005   DOI   ScienceOn
18 Kim SJ, Jung HS: Immunogold labeling of the enzyme in mitochondria inner membrane of beef and rat heart. Hallym Univ J 8 : 45-62, 1990
19 Konstantinova SA, Manneila CA, Skulachev VP, Zorov DB: Immunoelectron microscopic study of the distribution of porin on outer membranes of rat heart mitochondria. Journal of Bioenergetics and Biomembranes 27(1) : 93-99, 1995   DOI