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Homogeneity among mitochondria revealed by a constant proportion of their enzymes

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Summary

The homogeneity or heterogeneity at the enzyme level of mitochondria has not been directly demonstrated and is important for many studies. To clarify this point, carbamoyl phosphate synthase (ammonia), glutamate dehydrogenase and mitochondrial adenosine triphosphatase (F1) were located in rat liver by immunolabeling using protein A-gold. Measurements of the number of gold particles per square micron of cross sectional images of mitochondria permit to assess the relative molecular concentration of the three enzymes and, most interestingly, it presents the first evidence that different mitochondria in rat liver cells have the same relative proportion of the three enzymes. Since they have vastly different half-lives, bulk or unregulated autophagy as the main mechanism regulating the turnover of these enzymes seems unlikely.

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References

  • Arnold H, Maier KP (1971) Crystallization and some properties of glutamate dehydrogenase from rat liver. Biochim Biophys Acta 251:133–140

    Google Scholar 

  • Bendayan M, Shore GC (1982) Immunocytochemical localization of mitochondrial proteins in the rat hepatocyte. J Histochem Cytochem 30:139–147

    Google Scholar 

  • Bendayan M, Roth J, Perrelet A, Orci L (1980) Quantitative immunocytochemical localization of pancreatic secretory proteins in subcellular compartments of the rat acinar cell. J Histochem Cytochem 28:149–160

    Google Scholar 

  • Bosman FT (1983) Some recent developments in immunocytochemistry. Histochem J 15:189–200

    Google Scholar 

  • Clarke S (1976) A major polypeptide component of rat liver mitochondria: carbamyl phosphate synthetase. J Biol Chem 251:950–961

    Google Scholar 

  • Desautels M, Goldberg AL (1982) Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J Biol Chem 257:11673–11679

    Google Scholar 

  • Felipo V, Miralles V, Knecht E, Hernández-Yago J, Grisolía S (1983) The precursor of rat liver mitochondrial glutamate dehydrogenase has enzymatic activity. Eur J Biochem 133:641–644

    Google Scholar 

  • Grisolía S, Knecht E, Cervera J, Hernández J (1979) Mitochondrial protein degradation. In: Rapoport S, Schewe T (eds) Processing and turnover of proteins and organelles in the cell. Pergamon Press, New York, pp 143–153

    Google Scholar 

  • Grisolía S, Knecht E, Hernández-Yago J, Wallace R (1980) Turnover and degradation of mitochondria and their proteins. In: Protein degradation in health and disease (CIBA Found. Symp. 75). Elsevier, Amsterdam, pp 167–188

    Google Scholar 

  • Knecht E, Hernández J, Wallace R, Grisolía S (1979) Immunoferritin location of carbamoyl phosphate synthetase in rat liver. J Histochem Cytochem 27:975–981

    Google Scholar 

  • Knecht E, Hernández-Yago, J, Martinez-Ramón A, Grisolía S (1980) Fate of proteins synthesized in mitochondria of cultured mammalian cells revealed by electron microscope radioautography. Exp Cell Res 125:191–199

    Google Scholar 

  • Lehninger AL (1982) Principles of biochemistry. Worth Publishers, New York

    Google Scholar 

  • Nicoletti M, Guerri C, Grisolía S (1977) Turnover of carbamylphosphate synthase, of other mitochondrial enzymes and of rat tissues. Effect of diet and thyroidectomy. Eur J Biochem 75:583–592

    Google Scholar 

  • Pérez-Pastor E, Wallace R, Grisolía S (1982) Turnover of adenosine triphosphatase from rat liver mitochondria. Effect of high and low protein diets. Eur J Biochem 127:275–278

    Google Scholar 

  • Renau-Piqueras J, Knecht E, Hernández-Yago J (1981) Effects of different fixative solutions on labeling of coneanavalin-A receptor sites in human T-lymphocytes. Histochemistry 71:559–565

    Google Scholar 

  • Roth, J (1982) The protein A-gold (pAg) technique. A qualitative and quantitative approach for antigen localization on thin sections. In: Bullock GR, Petrusz P (eds) Techniques in immunocytochemistry. Academic Press, New York, pp 107–133

    Google Scholar 

  • Roth J, Bendayan M, Orci L (1978) Ultrastructural localization of intracellular antigens by the use of protein A-gold complex. J Histochem Cytochem 26:1074–1081

    Google Scholar 

  • Rubio V, Ramponi G, Grisolía S (1981) Carbamoyl phosphate synthetase I of human liver. Purification, some properties and immunological cross-reactivity with the rat liver enzyme. Biochim Biophys Acta 659:150–160

    Google Scholar 

  • Shore GC, Power F, Bendayan M, Carignan P (1981) Biogenesis of a 35-kilodalton protein associated with outer mitochondrial membrane in rat liver. J Biol Chem 256:8761–8766

    Google Scholar 

  • Swafford JR, Malloy PJ, Reeves HC (1983) Immunochemical localization of NADP-specific isocitrate dehydrogenase in Escherichia coli Science 221:295–296

    Google Scholar 

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Knecht, E., Hernández-Yago, J. & Grisolía, S. Homogeneity among mitochondria revealed by a constant proportion of their enzymes. Histochemistry 80, 359–362 (1984). https://doi.org/10.1007/BF00495417

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