Proteasome production in human muscle during nutritional inhibition of myofibrillar protein degradation

Irwin G. Brodsky, Dennis Suzara, Mikhail Furman, Paul Goldspink, G. Charles Ford, K. Sreekumaran Nair, Jayme Kukowski, Sheryl Bedno

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Protein undernutrition inhibits adenosine triphosphate (ATP)-dependent muscle protein degradation-a hallmark of the proteasome system. Here we report decreased myofibrillar protein degradation during dietary protein restriction without a concomitant decrease in proteasome gene expression, proteasome protein abundance, or proteasome in vivo fractional synthesis rate. Healthy human subjects consuming the average minimum adult protein requirement (0.71 g · kg-1 fat-free mass · d-1) exhibited substantially lower (68%) excretion of 3-methylhistidine, an indicator of myofibrillar protein breakdown, when compared with subjects consuming an ample, American-style protein intake (1.67 g · kg-1 fat-free mass · d-1). However, they displayed no difference in the expression of mRNA for proteasome subunits C2 or C3, in the content of C2 protein, or in the rate of incorporation of stable isotopically labeled L-[1-13C]-leucine into proteasome proteins. The results demonstrate that nutritional inhibition of myofibrillar protein degradation does not involve suppression in vivo of proteasome production in man. This suggests that other elements of the ubiquitin-proteasome system, such as ubiquitination pathways, are more important than proteasome abundance in the nutritional regulation of skeletal muscle mass.

Original languageEnglish (US)
Pages (from-to)340-347
Number of pages8
JournalMetabolism: Clinical and Experimental
Issue number3
StatePublished - Mar 2004

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Endocrinology


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