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Review Article
Mechanisms of Disease
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Volume 335:1897-1905 December 19, 1996 Number 25
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Mechanisms of Muscle Wasting — The Role of the Ubiquitin–Proteasome Pathway
William E. Mitch, M.D., and Alfred L. Goldberg, Ph.D.

Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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All proteins in mammalian cells are continually being degraded and replaced. In the cytosol, nucleus, and organelles, individual proteins are degraded at widely differing rates; some cytosolic enzymes have half-lives as short as 10 minutes, whereas others last for days. The average rate of protein turnover also varies among tissues; the majority of proteins in rat hepatocytes are replaced every few days, whereas those in muscle or brain cells are replaced every one to two weeks. The amount of intracellular protein turned over each day is quite large. In a normal 70-kg adult, about 280 g of protein is synthesized . . . [Full Text of this Article]

Intracellular Protein Degradation

Lysosomal Protein Degradation

The Ubiquitin–Proteasome Pathway

Muscle-Protein Degradation

The Ubiquitin–Proteasome Pathway in Catabolic States

Biochemical Adaptations That Activate Muscle Proteolysis

Cytokines and Hormones That Activate Muscle Proteolysis

Factors That Suppress Muscle Proteolysis

Future Treatment Prospects


Source Information

From the Renal Division, Emory University School of Medicine, Atlanta (W.E.M.), and the Department of Cell Biology, Harvard Medical School, Boston (A.L.G.).

Address reprint requests to Dr. Mitch at the Renal Division, Emory University, 1364 Clifton Rd., Atlanta, GA 30322.

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