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Gear 1970 Biochem J

From Bioblast
Publications in the MiPMap
Gear AR (1970) Inner- and outer-membrane enzymes of mitochondria during liver regeneration. Biochem J 120:577-87.

Β» PMID: 5499970 Open Access

Gear AR (1970) Biochem J

Abstract:

  1. Marker enzymes for the mitochondrial matrix, inner membrane, inter-membrane space and outer membrane were measured in mitochondria isolated from control and regenerating rat liver. The specific activity of these enzymes was then followed for up to 30 days after operation.
  2. The specific activity of marker enzymes for the matrix, inner membrane and inter-membrane space remained constant during liver regeneration.
  3. However, the specific activities of monoamine oxidase and kynurenine hydroxylase, both outer-membrane markers, fell by 67% and 49% respectively from their control values at 4 days after operation, and returned to normal by about 3 weeks.
  4. The repression of kynurenine hydroxylase activity was shown to be unrelated to any independent variation in tryptophan catabolism, based on tryptophan pyrrolase assays.
  5. These results are considered to indicate that enzymes of the inner and outer mitochondrial membranes are synthesized asynchronously during morphogenesis.
  6. The enzyme complement of purified outer membrane at 4 days after operation was about 50% of that of the appropriate control. Thus the composition of the outer membrane itself may vary dramatically, and supports the concept that constitutive enzymes may turn over independently of a membrane's existence.
  7. The behaviour of the rotenone-insensitive, NADH cytochrome c reductase did not parallel the other outer-membrane enzymes for intact mitochondria, but did so when assayed in highly purified fractions of outer membrane. This suggests a labile binding to the outer membrane during the early stages of morphogenesis.
  8. Electrophoresis of inner- and outer-membrane proteins revealed little difference between control and experimental mitochondria at 4 days, except for an increase in several, high-molecular-weight components of the outer membrane. These bands closely correspond to similar bands derived from smooth endoplasmic reticulum.
  9. The results are discussed in relation to the biogenesis and turnover of mitochondria, and are considered to provide evidence for turnover as a unit, at least for the matrix, inner membrane, inter-membrane space and possibly some form of primary outer membrane.


Labels: MiParea: mt-Biogenesis;mt-density, mt-Structure;fission;fusion, mt-Membrane 


Organism: Rat  Tissue;cell: Liver  Preparation: Isolated mitochondria  Enzyme: Complex I, Complex II;succinate dehydrogenase, Marker enzyme, TCA cycle and matrix dehydrogenases 

Coupling state: LEAK, OXPHOS 


Inner mt-membrane, Outer mt-membrane, Monoamine oxidase, Adenylate kinase, Malate dehydrogenase, Glutamate dehydrogenase 

217 mg protein/g Ww of liver.