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JBC, Vol. 251, Issue 10, 2891-2897, May, 1976
O. A. Scornik and V. Botbol
The significance of changes in rates of synthesis, export, and degradation
of proteins during liver regeneration was assessed. (a) Proteins were pulse
labeled by the intravenous injection of radioactive leucine and, 5 min
later, pactamycin (an inhibitor of the initiation of protein synthesis).
One-half of the protein radioactivity was lost from the normal liver within
3 hours. From the radioactivity of the plasma proteins at that time and a
study of the disappearance of these proteins from the circulation, it was
calculated that 28% of the newly synthesized proteins were exported. Serum
albumin accounted for a third of the exported proteins. Thirty-six hours
after partial hepatectomy the proportion of albumin to total protein
synthesis remained constant, while that of the other plasma proteins
increased by 50%. The fraction of the newly synthesized proteins retained
by the liver after 3 hours decreased by 20%. (b) During the first 36 hours
of liver regeneration the average rates of protein degradation slowed down
to one-half the normal values. This was determined either by the loss of
radioactivity from total protein (or the guanidino-C of protein-bound
arginine) in livers labeled with [14C]bicarbonate, or calculated as the
balance between protein synthesis and net protein gain. (c) From these
results, and those of our previous study of the protein synthetic machinery
of normal and regenerating livers (Scornik, O.A. (1974)J. Biol. Chem. 249,
3876-3883), we conclude that changes in the rate of protein degradation are
the single most important factor determining the increase in protein
content during liver compensatory growth.
Role of changes in protein degradation in the growth of regenerating livers
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O. A. Scornik, S. K. Howell, and V. Botbol Protein depletion and replenishment in mice: different roles of muscle and liver Am J Physiol Endocrinol Metab, December 1, 1997; 273(6): E1158 - E1167. [Abstract] [Full Text] [PDF] |
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