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  • Ubiquitin, proteasomes and proteolytic mechanisms activated by kidney disease
  • Rajan V; Mitch WE
  • Biochim Biophys Acta 2008[Dec]; 1782 (12): 795-9
  • The ubiquitin-proteasome system (UPS) includes 3 enzymes that conjugate ubiquitin to intracellular proteins that are then recognized and degraded in the proteasome. The process participates in the regulation of cell metabolism. In the kidney, the UPS regulates the turnover of transporters and signaling proteins and its activity is down regulated in acidosis-induced proximal tubular cell hypertrophy. In chronic kidney disease (CKD), muscle wasting occurs because complications of CKD including acidosis, insulin resistance, inflammation, and increased angiotensin II levels stimulate the UPS to degrade muscle proteins. This response also includes caspase-3 and calpains which act to cleave muscle proteins to provide substrates for the UPS. For example, caspase-3 degrades actomyosin, leaving a 14 kDa fragment of actin in muscle. The 14 kDa actin fragment is increased in muscle of patient with kidney disease, burn injury and surgery. In addition, acidosis, insulin resistance, inflammation and angiotensin II stimulate glucocorticoid production. Glucocorticoids are also required for the muscle wasting that occurs in CKD. Thus, the UPS is involved in regulating kidney function and participates in highly organized responses that degrade muscle protein in response to loss of kidney function.
  • |Animals[MESH]
  • |Humans[MESH]
  • |Kidney Diseases/*metabolism[MESH]
  • |Proteasome Endopeptidase Complex/*metabolism[MESH]
  • |Ubiquitin/*metabolism[MESH]

  • *{{pmid18723090}}
    *<b>[ Ubiquitin, proteasomes and proteolytic mechanisms activated by kidney disease ]</b> Biochim Biophys Acta 2008; 1782(12) ; 795-9 Rajan V; Mitch WE


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    Biochim Biophys Acta

    795 12.1782 2008