Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures

Hong, Dezhi; Forsberg, Neil E.

doi:10.1016/0303-7207(95)03476-n

Cited by 82 publications

(64 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Increases in calpain gene transcription and calpain expression contribute to this regulation in a tissue-or a cell-specific manner (42)(43)(44)(45). Thus, our data imply that glucocorticoids could limit their own binding to GR by up-regulating calpain activity.…”

Section: Discussionmentioning

confidence: 67%

Somatostatin Increases Glucocorticoid Binding and Signaling in Macrophages by Blocking the Calpain-specific Cleavage of Hsp 90

Bellocq¹,

Doublier²,

Suberville³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 67%

Somatostatin Increases Glucocorticoid Binding and Signaling in Macrophages by Blocking the Calpain-specific Cleavage of Hsp 90

Bellocq¹,

Doublier²,

Suberville³

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…The catabolic effects of glucocorticoid on overall muscle protein metabolism are well known. For example, glucocorticoid increased overall protein degradation in rat L8 and L6 myotubes and enhanced the degradation of myofibrillar proteins in C2C12 myotubes (1)(2)(3). In response to fasting, muscles of adrenalectomized animals, unlike normals, are unable to increase protein breakdown, whereas complete restoration occurs after glucocorticoid administration.…”

mentioning

confidence: 98%

Glucocorticoids differentially regulate degradation of MyoD and Id1 by N-terminal ubiquitination to promote muscle protein catabolism

Sun

Trausch-Azar

Muglia

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Accelerated protein degradation via the ubiquitin-proteasome pathway is the principal cause of skeletal muscle wasting associated with common human disease states and pharmacological treatment with glucocorticoids. Although many protein regulatory factors essential for muscle development and regeneration are degraded via the ubiquitin system, little is known about the mechanisms and regulation of this pathway that promote wasting muscle. Here, we demonstrate that, in differentiated myotubes, glucocorticoid, via the glucocorticoid receptor, selectively induces a decrease in protein abundance of MyoD, a master switch for muscle development and regeneration, but not that of its negative regulator Id1. This decrease in MyoD protein results from accelerated degradation after glucocorticoid exposure. Using MyoD and Id1 mutants deficient in either N terminus-dependent or internal lysine-dependent ubiquitination, we further show that these ubiquitination pathways of MyoD degradation are regulated differently from those of Id1 degradation. Specifically, glucocorticoid activates the N-terminal ubiquitination pathway in MyoD degradation in myotubes, without concomitant effects on Id1 degradation. This effect of glucocorticoid on MyoD and Id1 protein degradation is associated with the distinct cellular compartments in which their degradation occurs. Taken together, these results support a key role for the N terminus-dependent ubiquitination pathway in the physiology of muscle protein degradation.ubiquitin ͉ proteolysis

show abstract

“…IGF-I stimulates hypertrophy in myotubes and skeletal muscle (Adams & McCue 1998, Rommel et al 2001, Sacheck et al 2004, while glucocorticoid conversely induces proteolysis in myotubes and skeletal muscle (Hong & Forsberg 1995, Kayali et al 1987, Sacheck et al 2004). However, the roles played by IGF-I and glucocorticoid in compensatory growth remain unclear.…”

Section: Compensatory Growth Of C2c12 Myotubes Induced By the Combinementioning

confidence: 99%

Mechanism of Compensatory Growth with Changing Levels of Dietary Lysine from Deficient to Sufficient in Pigs

Ishida

Nakashima

Kyoya

et al. 2015

JARQ

View full text Add to dashboard Cite

This review describes our studies on compensatory growth, specifically the growth that occurs after dietary lysine deficiency is changed to sufficiency. We found that dietary lysine sufficiency induced compensatory growth in pigs after dietary lysine deficiency. We also showed that compensatory growth of pigs induced by dietary lysine sufficiency was partly attributed to greater N retention. In a rat model, both suppression of proteolysis and increased protein synthesis in skeletal muscle contributed to their compensatory growth with lysine sufficiency. Finally, our in vitro studies with cultured skeletal muscle cells revealed that the compensatory growth in these cells was induced by increased lysine levels in combination with the modulation of insulin-like growth factor-I and glucocorticoid levels. This suggested that compensatory growth in pigs and rats with lysine sufficiency was due to both increased serum lysine levels and changes in the levels of hormones involved in protein synthesis and degradation.

show abstract

Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures

Cited by 82 publications

References 40 publications

Somatostatin Increases Glucocorticoid Binding and Signaling in Macrophages by Blocking the Calpain-specific Cleavage of Hsp 90

Somatostatin Increases Glucocorticoid Binding and Signaling in Macrophages by Blocking the Calpain-specific Cleavage of Hsp 90

Glucocorticoids differentially regulate degradation of MyoD and Id1 by N-terminal ubiquitination to promote muscle protein catabolism

Mechanism of Compensatory Growth with Changing Levels of Dietary Lysine from Deficient to Sufficient in Pigs

Contact Info

Product

Resources

About