Tumour necrosis factor blockade did not prevent the increase of muscular muscle RING finger-1 and muscle atrophy F-box in arthritic rats

Granado, Miriam; Martín, Ana Isabel; Priego, Teresa; López-Calderón, Asunción; Villanúa, María Ángeles

doi:10.1677/joe.1.06931

Cited by 26 publications

(21 citation statements)

References 49 publications

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“…However, this does not seem to be the cause, since with systemic anti-TNF-␣ administration, inflammation was also decreased in a similar way (21), but no modifications in IGFBP-5, MAFbx or MuRF1 mRNA, or gastrocnemius weight were observed (22). Taking into account that TNF-␣ is also an important trigger of muscular atrophy and it upregulates MAFbx and MuRF1 gene expression (31,35), the lack of effect of systemic anti-TNF-␣ in preventing muscular wasting was unexpected (22). A possible explanation can be that the "in vivo" anti-TNF-␣ therapy is not able to suppress COX activity in the muscle, as is the case of the synovial tissue from rheumatoid arthritis patients (33).…”

Section: Discussionmentioning

confidence: 94%

“…These data emphasize the importance of the COX pathway in the inflammatory cachexia. Another explanation could be that muscle proteolysis by the ubiquitin-proteasome pathway is activated by local TNF-␣ rather than by circulating TNF-␣, since systemic anti-TNF-␣ therapy is not able to prevent the increased gene expression of TNF-␣ in the gastrocnemius muscle (22). In the present data, normalization of MuRF1 and MAFbx is associated with a decrease in muscular TNF-␣, which means that there is a relationship between prostaglandin inhibition and TNF-␣ gene expression.…”

Section: Discussionmentioning

confidence: 99%

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Experimental arthritis inhibits the insulin-like growth factor-I axis and induces muscle wasting through cyclooxygenase-2 activation

Granado¹,

Martín²,

Villanúa³

et al. 2007

American Journal of Physiology-Endocrinology and Metabolism

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Chronic arthritis induces cachexia associated with an inhibition of the growth hormone (GH)-insulin-like growth factor-I (IGF-I) system and an activation of the E3 ubiquitin-ligating enzymes muscle atrophy F-box (MAFbx) and muscle Ring finger 1 (MuRF1) in the skeletal muscle. The aim of this work was to study the role of cyclooxygenase (COX)-2 in chronic arthritis-induced cachexia. Arthritis was induced in rats by Freund's adjuvant injection, and the effects of two COX inhibitors (indomethacin, a nonspecific inhibitor, and meloxicam, a selective COX-2 inhibitor on pituitary GH and on liver and serum IGF-I levels) were tested. Arthritis decreased body weight gain and GH and liver IGF-I gene expression. In the arthritic rats, both inhibitors, indomethacin and meloxicam, prevented the inhibitory effect of arthritis on body weight gain. Indomethacin and meloxicam administration to arthritic rats increased pituitary GH and liver IGF-I mRNA as well as serum levels of IGF-I. These data suggest that induction of COX-2 during chronic inflammation is involved in the inhibition of the GH-IGF-I axis and in the body weight loss. In the gastrocnemius muscle, arthritis increased the gene expression of tumor necrosis factor (TNF)-α, the E3 ubiquitin-ligating enzymes MAFbx and MuRF1, as well as of IGF-I and IGF-binding protein-5 (IGFBP-5). Inhibition of COX-2 by meloxicam administration increased gastrocnemius weight and decreased MAFbx, MuRF1, TNF-α, and IGFBP-5 gene expression. In summary, our data indicate that chronic arthritis-induced cachexia and muscle wasting are mediated by the COX-2 pathway resulting in a decreased GH-IGF-I secretion and increased expression of MAFbx and MuRF1 mRNA.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Experimental arthritis inhibits the insulin-like growth factor-I axis and induces muscle wasting through cyclooxygenase-2 activation

Granado¹,

Martín²,

Villanúa³

et al. 2007

American Journal of Physiology-Endocrinology and Metabolism

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“…6). However, there is accumulating evidence to suggest that the pathway(s) mediating muscle proteolysis is (are) more complex than anticipated because there are reports showing 1) that IGF-I downregulated the burn-induced elevation of MuRF1 and MAFbx genes independent of its effect on glucocorticoids (40); 2) that IGF-I could not prevent muscle atrophy induced by proinflammatory cytokines, despite inhibiting MAFbx (9); 3) that TNF-␣ blockade did not prevent the increase of muscle MuRF1 and MAFbx genes in arthritic rats (21); and 4) that MuRF1 and MAFbx genes could be regulated through multiple pathways including those involving AKT, NF-B, and p38 MAPK (34). Moreover, as discussed earlier, direct actions of ghrelin on muscle also could have contributed to attenuated expression of the E3 ligase genes and, hence, to reduced muscle proteolysis (10,20,45,51,67).…”

Section: Discussionmentioning

confidence: 99%

Ghrelin inhibits skeletal muscle protein breakdown in rats with thermal injury through normalizing elevated expression of E3 ubiquitin ligases MuRF1 and MAFbx

Balasubramaniam

Joshi²,

Su³

et al. 2009

American Journal of Physiology-Regulatory, Integrative and Comp

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Balasubramaniam A, Joshi R, Su C, Friend LA, Sheriff S, Kagan RJ, James JH. Ghrelin inhibits skeletal muscle protein breakdown in rats with thermal injury through normalizing elevated expression of E3 ubiquitin ligases MuRF1 and MAFbx. Am J Physiol Regul Integr Comp Physiol 296: R893-R901, 2009. First published February 11, 2009; doi:10.1152/ajpregu.00015.2008.-We previously determined that ghrelin synthesis was downregulated after burn injury and that exogenous ghrelin retained its ability both to stimulate food intake and to restore plasma growth hormone levels in burned rats. These observations and the finding that anabolic hormones can attenuate skeletal muscle catabolism led us to investigate whether ghrelin could attenuate burn-induced skeletal muscle protein breakdown in rats. These studies were performed in young rats (50 -60 g) 24 h after ϳ30% total body surface area burn injury. Burn injury increased total and myofibrillar protein breakdown in extensor digitorum longus (EDL) muscles assessed by in vitro tyrosine and 3-methyl-histidine release, respectively. Continuous 24-h administration of ghrelin (0.2 mg ⅐ kg Ϫ1 ⅐ h Ϫ1 ) significantly inhibited both total and myofibrillar protein breakdown in burned rats. Ghrelin significantly attenuated burninduced changes in mRNA expression of IGFBP-1 and IGFBP-3 in liver. In EDL, ghrelin attenuated the increases in mRNA expression of the binding proteins, but had no significant effect on reduced expression of IGF-I. Ghrelin markedly reduced the elevated mRNA expression of TNF-␣ and IL-6 in EDL muscle that occurred after burn. Moreover, ghrelin normalized plasma glucocorticoid levels, which were elevated after burn. Expression of the muscle-specific ubiquitinligating enzyme (E3) ubiquitin ligases MuRF1 and MAFbx were markedly elevated in both EDL and gastrocnemius and were normalized by ghrelin. These results suggest that ghrelin is a powerful anticatabolic compound that reduces skeletal muscle protein breakdown through attenuating multiple burn-induced abnormalities.

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“…Interestingly, Granado et al reported the opposite effect of sTNFR1 on arthritic rat. They observed that administration of polyethylene glycol linked-sTNFRI to arthritic rats does not alter the gastrocnemius muscle mass and MuRF1/MAFbx gene expression [125].…”

Section: Anti-tnfsmentioning

confidence: 99%

Skeletal muscle atrophy: Potential therapeutic agents and their mechanisms of action

Dutt

Gupta

Dabur

et al. 2015

Pharmacological Research

143

110

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Tumour necrosis factor blockade did not prevent the increase of muscular muscle RING finger-1 and muscle atrophy F-box in arthritic rats

Cited by 26 publications

References 49 publications

Experimental arthritis inhibits the insulin-like growth factor-I axis and induces muscle wasting through cyclooxygenase-2 activation

Experimental arthritis inhibits the insulin-like growth factor-I axis and induces muscle wasting through cyclooxygenase-2 activation

Ghrelin inhibits skeletal muscle protein breakdown in rats with thermal injury through normalizing elevated expression of E3 ubiquitin ligases MuRF1 and MAFbx

Skeletal muscle atrophy: Potential therapeutic agents and their mechanisms of action

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