Autophagy of mitochondria in rat liver assessed by immunogold proceduresE Knecht, A Martinez-Ramon and S Grisolia Instituto de Investigaciones Citologicas de la Caja de Ahorros de Valencia, Spain. Glutamate dehydrogenase and carbamoyl phosphate synthase-I were localized in rat liver by immunogold procedures, using monoclonal and polyclonal antibodies. As expected, there was extensive labeling in mitochondria. Label was also found in lysosomal autophagic vacuoles. When autophagy was stimulated by in vivo administration of the anti- microtubular agent vinblastine we found that: (a) carbamoyl phosphate synthase-I and glutamate dehydrogenase could be found in mitochondria within autophagic vacuoles; (b) the carbamoyl phosphate synthase-I and glutamate dehydrogenase content of the mitochondria sequestered into autophagic vacuoles is the same as that of the nearby "free" mitochondria; and (c) in the whole liver, autophagic vacuoles contain c. 1.5 times more glutamate dehydrogenase than carbamoyl phosphate synthase-I, in contrast to mitochondria which have c. three times more carbamoyl phosphate synthase-I than glutamate dehydrogenase. The latter finding could explain, at least partially, the difference in half-lives of these enzymes.
Volume 36,
Issue 11,
pp. 1433-1440,
11/01/1988
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Z.-H. Qin, Y. Wang, K. B. Kegel, A. Kazantsev, B. L. Apostol, L. M. Thompson, J. Yoder, N. Aronin, and M. DiFiglia Autophagy regulates the processing of amino terminal huntingtin fragments Hum. Mol. Genet., December 15, 2003; 12(24): 3231 - 3244. [Abstract] [Full Text] [PDF] |
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N. C. Chandra, M. J. Spiro, and R. G. Spiro Identification of a Glycoprotein from Rat Liver Mitochondrial Inner Membrane and Demonstration of Its Origin in the Endoplasmic Reticulum J. Biol. Chem., July 31, 1998; 273(31): 19715 - 19721. [Abstract] [Full Text] [PDF] |
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