Applied Microscopy

Korean Society of Microscopy (한국현미경학회)
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The Formation and Change of Cytochrome-c-oxidase in the Mitochondria of the Bovine Cardiac Muscle

우(牛)심근조직의 mitochondria에서 cytochrome-c-oxidase의 형성과 변화

  • Kim, Soo-Jin (Department of Life Science, College of Natural Science, Hallym University)
  • 김수진 (한림대학교 자연과학대학 생명과학과)
  • Published : 2008.06.30
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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.

Mitochondria 내막의 cytochrome-c-oxidase는 세포의 에너지 생합성에 중요한 요소이며, 세포자멸사와 각종세포의 병리학적 현상과 밀접한 연관성이 있는 전자전달계효소로 알려져 있다. Porin 단백은 mitochondria 내막과 외막에 분포하는 효소단백으로 전자전달계효소 형성과 ATP 운반에 관여하는 것으로 알려져 있다. 따라서 면역현미경법을 사용하여 cytochrome-c-oxidase의 분포와 porin 단백과의 연관성을 확인하여 mitochondria의 cristae에 분포하는 cytochrome-c-oxidase의 형성과 변화를 알아보고자 하였다. Cardiac muscle tissue의 sarcoplasm에는 많은 수의 mitochondria가 분포하며, cytochrome-c-oxidase가 풍부한 mitochondria와 porin 단백이 풍부한 mitochondria로 구별되었다. Cytochrome-c-oxidase가 풍부한 mitochondria는 porin 단백이 빈약하고 porin 단백이 풍부한 mitochondria는 cytochrome-c-oxidase가 소량 포함되어 있는 것으로 관찰되었다. 심근조직의 부위에 따라 근형질에 분포하는 mitochondria에 cytochrome-c-oxidase가 풍부한 mitochondria와 porin 단백이 풍부한 mitochondria가 각각 상이하게 분포하였다. 이상의 결과로 미성숙 mitochondria는 많은 양의 porin 단백을 함유하여 근형질로부터 단백질 소단위를 mitochondria 막내로 운반하여 cytochrome-c-oxidase를 형성시키고 mitochondria가 성숙하면서 ATP를 운반할 최소한 양의 porin 단백만을 남기고 소멸되는 것으로 추측된다.

Keywords

References

  1. 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 https://doi.org/10.1104/pp.124.3.1181
  2. Colombini M: A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279(5714) : 643-645, 1979 https://doi.org/10.1038/279643a0
  3. 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 https://doi.org/10.1016/0005-2736(89)90447-1
  4. 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 https://doi.org/10.1177/002215540205001001
  5. 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
  6. Huttemann M, Schmidt TR, Grossman LI: A third isoform of cytochrome c oxidase subunit VIII is present in mammals. Gene 312 : 95-102, 2003 https://doi.org/10.1016/S0378-1119(03)00604-8
  7. Jamal JA: Involvement of porin N,N-dicyclohexylcarbodiimidereactive domain in hexokinase binding to the outer mitochondrial membrane. Protein J 24(1) : 1-8, 2005
  8. 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
  9. 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 https://doi.org/10.1016/0005-2728(87)90196-4
  10. 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 https://doi.org/10.1007/BF02110336
  11. 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 https://doi.org/10.1042/bj2080077
  12. 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 https://doi.org/10.1016/j.neulet.2005.04.085
  13. 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 https://doi.org/10.1016/j.abb.2004.12.029
  14. 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 https://doi.org/10.1074/jbc.M507741200
  15. 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 https://doi.org/10.1016/S0006-3495(97)78841-6
  16. 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 https://doi.org/10.1007/BF01869662
  17. 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 https://doi.org/10.1021/bi050870z
  18. 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 https://doi.org/10.1016/j.freeradbiomed.2004.10.037
  19. Vik SB, Georgevich G, Capaldi RA: Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase. Biochemistry 78(3) : 1456-1460, 1981