Protein turnover during metabolic arrest in turtle hepatocytes: role and energy dependence of proteolysis

Stephen C. Land, Peter W. Hochachka

Research output: Contribution to journalArticle

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Abstract

Hepatocytes from the western painted turtle (Chrysemys picta bellii) are capable of a coordinated metabolic suppression of 88% during 10 h of anoxia at 25°C. The energy dependence and role of proteolysis in this suppression were assessed in labile ([3H]Phe-labeled) and stable ([14C]Phe-labeled) protein pools. During anoxia, labile protein half-lives increased from 24.7 ± 3.3 to 34.4 ± 3.7 h, with stable protein half-lives increasing from 55.6 ± 3.4 to 109.6 ± 7.4 h. The total anoxic mean proteolytic suppression for both pools was 36%. On the basis of inhibition of O2 consumption and lactate production rates by cycloheximide and emetine, normoxic ATP-dependent proteolysis required 11.1 ± 1.7 μmol ATP · g-1 · h-1 accounting for 21.8 ± 1.4% of total cellular metabolism. Under anoxia this was suppressed by 93% to 0.73 ± 0.43 μmol ATP · g-1 · h-1. Summation of this with protein synthesis ATP turnover rates indicated that under anoxia 45% of total ATP turnover rate was directed toward protein turnover. Studies with inhibitors of energy metabolism indicated that the majority of energy dependence was found in the stable protein pool, with no significant inhibition occurring among the more labile proteins. We conclude that proteolysis is largely energy dependent under normoxia, whereas under anoxia there is a shift to a slower overall proteolytic rate that is largely energy independent and represents loss mostly from the labile protein pool.

Original languageEnglish
Pages (from-to)C1028-C1036
Number of pages9
JournalAmerican Journal of Physiology: Cell Physiology
Volume266
Issue number4
DOIs
Publication statusPublished - 1 Apr 1994

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Proteolysis
Turtles
Hepatocytes
Adenosine Triphosphate
Proteins
Emetine
Cycloheximide
Metabolism
Energy Metabolism
Lactic Acid
Hypoxia

Keywords

  • adenosine 5'-triphosphate turnover
  • anoxia
  • Chrysemys picta bellii
  • hypometabolism
  • minimum metabolic rate
  • protein half-life
  • protein stability
  • western painted turtle

Cite this

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abstract = "Hepatocytes from the western painted turtle (Chrysemys picta bellii) are capable of a coordinated metabolic suppression of 88{\%} during 10 h of anoxia at 25°C. The energy dependence and role of proteolysis in this suppression were assessed in labile ([3H]Phe-labeled) and stable ([14C]Phe-labeled) protein pools. During anoxia, labile protein half-lives increased from 24.7 ± 3.3 to 34.4 ± 3.7 h, with stable protein half-lives increasing from 55.6 ± 3.4 to 109.6 ± 7.4 h. The total anoxic mean proteolytic suppression for both pools was 36{\%}. On the basis of inhibition of O2 consumption and lactate production rates by cycloheximide and emetine, normoxic ATP-dependent proteolysis required 11.1 ± 1.7 μmol ATP · g-1 · h-1 accounting for 21.8 ± 1.4{\%} of total cellular metabolism. Under anoxia this was suppressed by 93{\%} to 0.73 ± 0.43 μmol ATP · g-1 · h-1. Summation of this with protein synthesis ATP turnover rates indicated that under anoxia 45{\%} of total ATP turnover rate was directed toward protein turnover. Studies with inhibitors of energy metabolism indicated that the majority of energy dependence was found in the stable protein pool, with no significant inhibition occurring among the more labile proteins. We conclude that proteolysis is largely energy dependent under normoxia, whereas under anoxia there is a shift to a slower overall proteolytic rate that is largely energy independent and represents loss mostly from the labile protein pool.",
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Protein turnover during metabolic arrest in turtle hepatocytes : role and energy dependence of proteolysis. / Land, Stephen C.; Hochachka, Peter W.

In: American Journal of Physiology: Cell Physiology, Vol. 266, No. 4 , 01.04.1994, p. C1028-C1036.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Protein turnover during metabolic arrest in turtle hepatocytes

T2 - role and energy dependence of proteolysis

AU - Land, Stephen C.

AU - Hochachka, Peter W.

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