Tumor necrosis factor-alpha inhibits myogenic differentiation through myod protein destabilization
Abstract
Tumor necrosis factor alpha (TNFalpha) has been implicated as a mediator of muscle wasting through nuclear factor kappa B (NF-kappaB) -dependent inhibition of myogenic differentiation. The aim of the present study was to identify the regulatory molecule(s) of myogenesis targeted by TNFalpha/NF-kappaB signaling. TNFalpha interfered with cell cycle exit and repressed the accumulation of transcripts encoding muscle-specific genes in differentiating C2C12 myoblasts. Overexpression of a p65 (RelA) mutant lacking the transcriptional activation domain attenuated the TNFalpha-mediated inhibition of muscle-specific gene transcription. The ability of muscle regulatory factor MyoD to induce muscle-specific transcription in 10T1/2 fibroblasts was also disrupted by wild-type p65, demonstrating that NF-kappaB transcriptional activity interferes with the function of MyoD. Inhibition of muscle-specific gene expression by TNFalpha was restored by overexpression of MyoD, whereas endogenous MyoD protein abundance and stability were reduced by TNFalpha through increased proteolysis of MyoD by the ubiquitin proteasome pathway. Last, the inhibitory effects of TNFalpha on myogenic differentiation were demonstrated in a mouse model of skeletal muscle regeneration, in which TNFalpha caused a delay in myoblast cell cycle exit. These results implicate that TNFalpha inhibits myogenic differentiation through destabilizing MyoD protein in a NF-kappaB-dependent manner, which interferes with skeletal muscle regeneration and may contribute to muscle wasting.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
TNF-α and IL-6 play an important role in early stages of muscle regeneration following injury by enhancing myoblast proliferation and inhibiting differentiation.
“Although being considered pro-inflammatory, TNF-α and IL-6 also appear to play important role in the early stages of muscle regeneration following injury by enhancing myoblast proliferation and inhibiting differentiation [73,74,75].”
From Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration (2018) · cites this paper as [75]
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521 · see citing works
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774 · see citing works
MyoD or Myf-5 is required for the formation of skeletal muscle
Rudnicki, M. A., Schnegelsberg, P. N. J., Stead, R. H., Braun, T. W., Arnold, H.-H., & Jaenisch, R. (1993) · Cell · doi:10.1016/0092-8674(93)90621-v · Cited by 1,731 · see citing works
Myogenic satellite cells: physiology to molecular biology
Hawke, T. J., & Garry, D. J. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.91.2.534 · Cited by 1,646 · see citing works
Wasting as independent risk factor for mortality in chronic heart failure
Anker, S. D., Ponikowski, P. P., Varney, S. J., Chua, T. P., Clark, A. L., Webb-Peploe, K., Harrington, D., Kox, W. J., Poole-Wilson, P. A., & Coats, A. J. S. (1997) · The Lancet · doi:10.1016/s0140-6736(96)07015-8 · Cited by 1,399 · see citing works
NF-κB Controls Cell Growth and Differentiation through Transcriptional Regulation of Cyclin D1
D, D. C. G., Albanese, C., Reuther, J. Y., Pestell, R. G., & Baldwin, A. S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5785 · Cited by 1,304 · see citing works
Correlation of Terminal Cell Cycle Arrest of Skeletal Muscle with Induction of p21 by MyoD
Halevy, O., Novitch, B. G., Spicer, D. B., Skapek, S. X., Rhee, J., Hannon, G. J., Beach, D., & Lassar, A. B. (1995) · Science · doi:10.1126/science.7863327 · Cited by 1,139 · see citing works
Weight Loss Is a Reversible Factor in the Prognosis of Chronic Obstructive Pulmonary Disease
Schols, A. M. W. J., Slangen, J. J. M., Volovics, L., & Wouters, E. F. �. (1998) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.157.6.9705017 · Cited by 1,084 · see citing works
Weintraub, H. M., Tapscott, S. J., Davis, R. L., Thayer, M. J., Adam, M. A., Lassar, A. B., & Miller, A. D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5434 · Cited by 985 · see citing works
NF-κB-Induced Loss of MyoD Messenger RNA: Possible Role in Muscle Decay and Cachexia
D, D. C. G., Mayo, M. W., Madrid, L. V., Wang, C., & Baldwin, A. S. (2000) · Science · doi:10.1126/science.289.5488.2363 · Cited by 922 · see citing works
MyoD1: A Nuclear Phosphoprotein Requiring a Myc Homology Region to Convert Fibroblasts to Myoblasts
Tapscott, S. J., Davis, R. L., Thayer, M. J., Cheng, P.-F., Weintraub, H. M., & Lassar, A. B. (1988) · Science · doi:10.1126/science.3175662 · Cited by 845 · see citing works
Magnitude of body-cell-mass depletion and the timing of death from wasting in AIDS
Kotler, D. P., Tierney, A. R., Wang, J., & Pierson, R. N. (1989) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/50.3.444 · Cited by 792 · see citing works
MyoD is required for myogenic stem cell function in adult skeletal muscle
Megeney, L. A., Kablar, B., Garrett, K., Anderson, J. E., & Rudnicki, M. A. (1996) · Genes & Development · doi:10.1101/gad.10.10.1173 · Cited by 724 · see citing works
Tumor Necrosis Factor-Alpha Levels and Weight Loss in Chronic Obstructive Pulmonary Disease
Di Francia, M., Barbier, D., Mège, J. L., & OREHEK, J. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.150.5.7952575 · Cited by 480 · see citing works
Positive autoregulation of the myogenic determination gene MyoD1
Thayer, M. J., Tapscott, S. J., Davis, R. L., Wright, W. E., Lassar, A. B., & Weintraub, H. M. (1989) · Cell · doi:10.1016/0092-8674(89)90838-6 · Cited by 471 · see citing works
Inflammatory cytokines inhibit myogenic differentiation through activation of nuclear factor‐κΒ
LANGEN, R. C. J., Schols, A. M. W. J., KELDERS, M. C. J. M., Wouters, E. F. �., & Janssen-Heininger, Y. M. W. (2001) · The FASEB Journal · doi:10.1096/fj.00-0463 · Cited by 423 · see citing works
Guo, K. Y., Wang, J., Andrés, V., Smith, R. C., & Walsh, K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3823 · Cited by 422 · see citing works
Buck, M., & Chojkier, M. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00524.x · Cited by 327 · see citing works
MyoD−/− Satellite Cells in Single-Fiber Culture Are Differentiation Defective and MRF4 Deficient
Cornelison, D., Olwin, B. B., Rudnicki, M. A., & Wold, B. J. (2000) · Developmental Biology · doi:10.1006/dbio.2000.9682 · Cited by 314 · see citing works
Puri, P., & Sartorelli, V. (2000) · Journal of Cellular Physiology · doi:10.1002/1097-4652(200011)185:2 · Cited by 290 · see citing works
Cachectin/TNF or IL-1 alpha induces cachexia with redistribution of body proteins
Fong, Y., Moldawer, L. L., Marano, M. A., Wei, H., Barber, A. E., Manogue, K., Tracey, K. J., Kuo, G., Fischman, D. A., Cerami, A., et al. (1989) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1989.256.3.r659 · Cited by 266 · see citing works
TNF-α is a mitogen in skeletal muscle
Li, Y.-P. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00453.2002 · Cited by 249 · see citing works
TNF‐α increases ubiquitin‐conjugating activity in skeletal muscle by up‐regulating UbcH2/E2 20k
LI, Y.-P., Lecker, S. H., Chen, Y., Waddell, I. D., Goldberg, A. L., & Reid, M. B. (2003) · The FASEB Journal · doi:10.1096/fj.02-0759com · Cited by 243 · see citing works
Patterns of histone variant synthesis can distinguish go from G1 cells
Wu, R. S., Tsai, S., & Bonner, W. M. (1982) · Cell · doi:10.1016/0092-8674(82)90130-1 · Cited by 228 · see citing works
Thaloor, D., Miller, K. J., Gephart, J., Mitchell, P. O., & Pavlath, G. K. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.277.2.c320 · Cited by 213 · see citing works
Phosphorylation of Nuclear MyoD Is Required for Its Rapid Degradation
Song, A., Wang, Q., Goebl, M. G., & Harrington, M. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.4994 · Cited by 165 · see citing works
A muscle precursor cell-dependent pathway contributes to muscle growth after atrophy
Mitchell, P. O., & Pavlath, G. K. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.5.c1706 · Cited by 164 · see citing works
Tumour necrosis factor‐α increases the ubiquitinization of rat skeletal muscle proteins
Garcia‐Martínez, C., Agell, N., Llovera, M., López-Soriano, F. J., & Argilés, J. M. A. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81341-v · Cited by 139 · see citing works
Ubiquitin gene expression is increased in skeletal muscle of tumour‐bearing rats
Llovera, M., Garcia‐Martínez, C., Agell, N., Marzábal, M., López-Soriano, F. J., & Argilés, J. M. A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80290-4 · Cited by 133 · see citing works
Tumor necrosis factor-α inhibits myogenesis through redox-dependent and -independent pathways
LANGEN, R. C. J., Schols, A. M. W. J., KELDERS, M. C. J. M., van der Velden, J. L. J., Wouters, E. F. �., & Janssen-Heininger, Y. M. W. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00418.2001 · Cited by 132 · see citing works
Association between tumor necrosis factor in serum and cachexia in patients with prostate cancer.
Nakashima, J., Tachibana, M., Ueno, M., Miyajima, A., Baba, S., & Murai, M. (1998) · PubMed · Cited by 128 · see citing works
Tumor Necrosis Factor Inhibits Human Myogenesis In Vitro
Miller, S. C., Ito, H., Blau, H. M., & Torti, F. M. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.6.2295-2301.1988 · Cited by 123 · see citing works
Hatoum, O. A., Gross-Mesilaty, S., Breitschopf, K., Hoffman, A., Gonen, H., Ciechanover, A. J., & Bengal, E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5670 · Cited by 119 · see citing works
Exercise-enhanced satellite cell proliferation and new myonuclear accretion in rat skeletal muscle
Smith, H. K., Maxwell, L., Rodgers, C. D., McKee, N. H., & Plyley, M. J. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.4.1407 · Cited by 106 · see citing works
Reynaud, E. G., Pelpel, K., Guillier, M., Leibovitch, M.-P., & Leibovitch, S. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7621 · Cited by 105 · see citing works
Szalay, K. S., Rázga, Z., & Duda, E. (1997) · PubMed · Cited by 105 · see citing works
Kami, K., & Senba, E. (2002) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540205001202 · Cited by 96 · see citing works
Elevated plasma levels of tumor necrosis factor in chronic heart failure with cachexia
Zhao, S., & Ling-hui, Z. (1997) · International Journal of Cardiology · doi:10.1016/s0167-5273(96)02873-2 · Cited by 71 · see citing works
Layne, M. D., & Farmer, S. R. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4465 · Cited by 71 · see citing works
Duguez, S., Bihan, M. L., Gouttefangeas, D., Féasson, L., & Freyssenet, D. G. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00331.2002 · Cited by 63 · see citing works
Application of neural networks in structure-activity relationships
K�vesdi, I., Dominguez‐Rodriguez, M. F., �rfi, L., N�ray-Szab�, G., Varró, A., Papp, J. G., & M�tyus, P. (1999) · Medicinal Research Reviews · doi:10.1002/(sici)1098-1128(199905)19:3 · Cited by 62 · see citing works
Determinants of Nuclear and Cytoplasmic Ubiquitin-mediated Degradation of MyoD
Lingbeck, J. M., Trausch‐Azar, J. S., Ciechanover, A. J., & Schwartz, A. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208815200 · Cited by 60 · see citing works
Yamazaki, T., YOKOYAMA, T., Akatsu, H., Tukiyama, T., & Tokiwa, T. (2003) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1290/1543-706x(2003)039 · Cited by 59 · see citing works
LANGEN, R. C. J., Schols, A. M. W. J., KELDERS, M. C. J. M., Wouters, E. F. �., & Janssen-Heininger, Y. M. W. (2003) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-003-0011-2 · Cited by 51 · see citing works
RIP2, a Checkpoint in Myogenic Differentiation
Munz, B., Hildt, E., Springer, M. L., & Blau, H. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5879-5886.2002 · Cited by 44 · see citing works
Activity‐induced fiber regeneration in rat soleus muscle
Wanek, L., & Snow, M. H. (2000) · The Anatomical Record · doi:10.1002/(sici)1097-0185(20000201)258:2 · Cited by 43 · see citing works
Isolation, Characterization, and Partial Purification of a Novel Ubiquitin-Protein Ligase, E3
Gonen, H., Stancovski, I., Shkedy, D., Hadari, T., Bercovich, B., Bengal, E., Mesilati, S., Hatoum, O. A., Schwartz, A. L., & Ciechanover, A. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.302 · Cited by 39 · see citing works
Wunsch, A. M., & Lough, J. (1987) · Developmental Biology · doi:10.1016/0012-1606(87)90210-7 · Cited by 37 · see citing works
SEPSIS INHIBITS SYNTHESIS OF MYOFIBRILLAR AND SARCOPLASMIC PROTEINS
Vary, T. C., Owens, E. L., Beers, J. K., Verner, K., & Cooney, R. N. (1996) · Shock · doi:10.1097/00024382-199607000-00004 · Cited by 34 · see citing works
B�lec, L., Meillet, D., Gr??senguet, G., & Gherardi, K. (1995) · Journal of Acquired Immune Deficiency Syndromes & Human Retrovirology · doi:10.1097/00042560-199502000-00015 · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Arnold, L., Henry, A., Poron, F., Baba-Amer, Y., van Rooijen, N., Plonquet, A., Gherardi, R. K., & Chazaud, B. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070075 · Cited by 2,002 · see citing works
“behavior: TNFα is mitogenic for myoblasts and inhibits their differentiation (71,72); IL-1β”
BackgroundRegulatory interactions between muscle and the immune system during muscle regeneration
Tidball, J. G., & Villalta, S. A. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00735.2009 · Cited by 1,105 · see citing works
Proinflammatory Cytokines, Aging, and Age-Related Diseases
Michaud, M., Balardy, L., Moulis, G., Gaudin, C., Peyrot, C., Vellas, B., Cesari, M., & Nourhashemi, F. (2013) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2013.05.009 · Cited by 1,094 · see citing works
Skeletal muscle performance and ageing
Tieland, M., Trouwborst, I., & Clark, B. C. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12238 · Cited by 904 · see citing works
“tion factors are involved in the transition from proliferation to differentiation of satellite cells.(188) Thus, in elderly people, the relatively high levels of inflammatory cytokines over”
The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756 · see citing works
“and altering transcriptional activity (Garcia-Martinez et al. 1994; Lang et al. 2002; Langen et al. 2004).”
BackgroundThe Role of Inflammation in Age-Related Sarcopenia
Dalle, S., Rossmeislova, L., & Koppo, K. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01045 · Cited by 668 · see citing works
“It was shown that TNFα, in particular, reduces the expression of MyoD and myogenin in myoblasts and destabilizes MyoD in regenerating mice muscles (Szalay et al., 1997; Langen et al., 2004).”
BackgroundOxidative Stress, Chronic Disease, and Muscle Wasting
Moylan, J. S., & Reid, M. B. (2007) · Muscle & Nerve · doi:10.1002/mus.20743 · Cited by 416 · see citing works
Pulmonary and Systemic Oxidant/Antioxidant Imbalance in Chronic Obstructive Pulmonary Disease
MacNee, W. (2005) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200411-056sf · Cited by 410 · see citing works
Mechanisms of Muscle Injury, Repair, and Regeneration
Tidball, J. G. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100092 · Cited by 439 · see citing works
Inflammation and Skeletal Muscle Wasting During Cachexia
Webster, J. M., Kempen, L. J. A. P., Hardy, R. S., & Langen, R. C. J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.597675 · Cited by 372 · see citing works
Self-citationApoptotic cell death in disease—Current understanding of the NCCD 2023
Vitale, I., Pietrocola, F., Guilbaud, E., Aaronson, S. A., Abrams, J., Adam, D., Agostini, M., Agostinis, P., Alnemri, E. S., Altucci, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01153-w · Cited by 359 · see citing works
Zanou, N., & Gailly, P. L. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1330-4 · Cited by 361 · see citing works
A Muscle Stem Cell Support Group: Coordinated Cellular Responses in Muscle Regeneration
Wosczyna, M. N., & Rando, T. A. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.06.018 · Cited by 353 · see citing works
Mourkioti, F., Kratsios, P., Luedde, T., Song, Y.-H., Delafontaine, P., Adami, R., Parente, V., Bottinelli, R., Pasparakis, M., & Rosenthal, N. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28721 · Cited by 315 · see citing works
Ilich, J. Z., Kelly, O. J., Inglis, J. E., Panton, L. B., Duque, G., & Ormsbee, M. J. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.02.007 · Cited by 282 · see citing works
Agustí, A. G. N., & Soriano, J. B. (2008) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1080/15412550801941349 · Cited by 280 · see citing works
“In patients with COPD, cytokines, particularly TNFα, can activate the NF-KB pathway (24), induce the expression of a variety of genes, such as the inducible form of the nitric oxide synthase (iNOS) (24), facilitate the degradation of myosin heavy chains through the ubiquitin-proteasome complex (25, 26) and contribute…”
BackgroundAutophagic Degradation Contributes to Muscle Wasting in Cancer Cachexia
Penna, F., Costamagna, D., Pin, F., Camperi, A., Fanzani, A., Chiarpotto, E., Cavallini, G., Bonelli, G., Baccino, F. M., & Costelli, P. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.12.023 · Cited by 270 · see citing works
Wang, H., Hertlein, E. K., Bakkar, N., Sun, H., Acharyya, S., Wang, J., Carathers, M., Davuluri, R. V., & D, D. C. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02020-06 · Cited by 259 · see citing works
“From the current work, it appears that NF- B silences myofibrillar gene expression through mutually exclusive mechanisms involving the positive regulation of YY1 and the negative regulation of MyoD (27, 37).”
BackgroundMaternal Obesity, Inflammation, and Fetal Skeletal Muscle Development1
Du, ., Yan, X., Tong, J. F., Zhao, J., & Zhu, M. J. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.109.077099 · Cited by 203 · see citing works
Inhibition of Atrogin-1/MAFbx Mediated MyoD Proteolysis Prevents Skeletal Muscle Atrophy In Vivo
Lagirand-Cantaloube, J., Cornille, K., Csibi, A., Batonnet‐Pichon, S., Leibovitch, M.-P., & Leibovitch, S. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004973 · Cited by 202 · see citing works
“Depending on the atrophic signaling pathway, MyoD expression seems to be inhibited both at the RNA and protein levels suggesting that in vivo, MyoD down-regulation is crucial for muscle loss [8,21,29].”
Rethinking Regenerative Medicine: A Macrophage-Centered Approach
Brown, B., Sicari, B. M., & Badylak, S. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00510 · Cited by 185 · see citing works
The role of systemic inflammation in age‐related muscle weakness and wasting
Degens, H. (2009) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2009.01018.x · Cited by 188 · see citing works
“It is possible that at least part of the destabilization of MyoD caused by TNFa (Langen et al., 2004) is due to an increased expression of Id proteins.”
BackgroundInfluentialThe central role of myostatin in skeletal muscle and whole body homeostasis
Elliott, B., Renshaw, D. W., Getting, S. J., & Mackenzie, R. (2012) · Acta Physiologica · doi:10.1111/j.1748-1716.2012.02423.x · Cited by 183 · see citing works
“Further, inflammatory mediators such as TNFa act in muscle to inhibit myogenic differentiation via NF-jB (Guttridge et al. 2000, Li & Reid 2000, Langen et al. 2001, 2004, Li & Schwartz 2001), upregulate atrogin and murf expression (Liu et al. 2003, Li et al. 2005), and inhibit the anabolic actions…”
Peake, J. M., Gatta, P. A. D., & Cameron‐Smith, D. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00467.2009 · Cited by 182 · see citing works
“In vivo, TNF- induces muscle wasting in healthy rodents (83, 93), and rodents with conditions, such as cancer cachexia (35, 63, 145), chronic pulmonary inflammation (82), and sepsis (81).”
BackgroundFactors contributing to muscle wasting and dysfunction in COPD patients.
Wüst, R. C. I., & Degens, H. (2007) · PubMed Central · Cited by 179 · see citing works
Inflammation and age-associated skeletal muscle deterioration (sarcopaenia)
Wang, J., Leung, K.-S., Chow, S. K.-H., & Cheung, W.-H. (2017) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2017.05.006 · Cited by 173 · see citing works
“Furthermore, a report showed that TNF-a inhibited myogenic differentiation through MyoD protein destabilisation [55].”
BackgroundEffect of pulmonary rehabilitation on muscle remodelling in cachectic patients with COPD
Vogiatzis, I., Simoes, D. C. M., Stratakos, G. K., Kourepini, E., Terzis, G. D., Manta, P., Athanasopoulos, D., Roussos, C., Wagner, P. D., & Zakynthinos, S. G. (2010) · European Respiratory Journal · doi:10.1183/09031936.00112909 · Cited by 173 · see citing works
“inconsistent, experimental data suggest that TNF-α can interfere with the hypertrophic action of muscle IGF-I [13] and inhibit myogenic differentiation by destabilizing MyoD protein [14].”
BackgroundInfluentialDivergent Roles of Inflammation in Skeletal Muscle Recovery From Injury
Howard, E. E., Pasiakos, S. M., Blesso, C. N., Fussell, M. A., & Rodriguez, N. R. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00087 · Cited by 176 · see citing works
“An overlap in expression of M1- and M2derived tumor necrosis factor-α (TNFα) and transforming growth factor beta 1 (TGF-β1), respectively, has been shown to reduce FAP apoptosis and increase ECM deposition (Lemos et al., 2015).”
BackgroundDogra, C., Changotra, H., Mohan, S., & Kumar, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511131200 · Cited by 158 · see citing works
Triggers and mechanisms of skeletal muscle wasting in chronic obstructive pulmonary disease
LANGEN, R. C. J., Gosker, H. R., Remels, A. H. V., & Schols, A. M. W. J. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.015 · Cited by 159 · see citing works
Whitman, S. A., Wacker, M. J., Richmond, S. R., & Godard, M. P. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1473-8 · Cited by 156 · see citing works
Skeletal muscle regeneration and impact of aging and nutrition
Domingues-Faria, C., Vasson, M.-P., Goncalves-Mendes, N., Boirie, Y., & Walrand, S. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2015.12.004 · Cited by 157 · see citing works
Diaphragm adaptations in patients with COPD
Ottenheijm, C. A. C., Heunks, L. M. A., & Dekhuijzen, R. P. N. (2008) · Respiratory Research · doi:10.1186/1465-9921-9-12 · Cited by 156 · see citing works
“Cytokines promote striated muscle injury, impair contractile protein function [105] and stimulate proteolysis through the ubiquitin-proteasome pathway in vitro [ 106- 108 ].”
Cellular Markers of Muscle Atrophy in Chronic Obstructive Pulmonary Disease
Plant, P. J., Brooks, D., Faughnan, M., Bayley, T., Bain, J., Singer, L., Correa, J., Pearce, D., Binnie, M., & Batt, J. (2010) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0382oc · Cited by 190 · see citing works
Therapeutic approaches for muscle wasting disorders
Lynch, G. S., Schertzer, J. D., & Ryall, J. G. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.11.004 · Cited by 152 · see citing works
Potential mechanisms underlying the role of chronic inflammation in age-related muscle wasting
Jo, E., Lee, S.-R., Park, B., & Kim, J. (2012) · Aging Clinical and Experimental Research · doi:10.1007/bf03654825 · Cited by 145 · see citing works
Burnham, J. M., Justine Shults, A., Semeao, E. J., Foster, B. J., Zemel, B. S., Stallings, V. A., & Leonard, M. B. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/82.2.413 · Cited by 140 · see citing works
Muscle Wasting and Impaired Muscle Regeneration in a Murine Model of Chronic Pulmonary Inflammation
LANGEN, R. C. J., Schols, A. M. W. J., KELDERS, M. C. J. M., van der Velden, J. L. J., Wouters, E. F. �., & Janssen-Heininger, Y. M. W. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0103oc · Cited by 137 · see citing works
Cytokine Profile in Quadriceps Muscles of Patients with Severe COPD
Barreiro, E., Schols, A. M. W. J., Polkey, M. I., Galdiz, J. B., Gosker, H. R., Swallow, E. B., Coronell, C., Gea, J., & on behalf of the ENIGMA in COPD project (2007) · Thorax · doi:10.1136/thx.2007.078030 · Cited by 175 · see citing works
NF-κB signaling in skeletal muscle: prospects for intervention in muscle diseases
Mourkioti, F., & Rosenthal, N. A. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0308-4 · Cited by 132 · see citing works
“Different research laboratories [48–58] have analyzed the effect of TNF-α in muscles.”
Interplay of skeletal muscle and adipose tissue: sarcopenic obesity.
Park, M., & Choi, K. M. (2023) · Metabolism: Clinical and Experimental · doi:10.1016/j.metabol.2023.155577 · Cited by 106 · see citing works
Dlk1 Is Necessary for Proper Skeletal Muscle Development and Regeneration
Waddell, J. N., Zhang, P., Wen, Y., Gupta, S. K., Yevtodiyenko, A., Schmidt, J. V., Bidwell, C. A., Kumar, A., & Kuang, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015055 · Cited by 129 · see citing works
“Increased levels of TNF-a have been shown to decrease nascent myofiber genesis [72,73] which along with IL-1b, activate the NF-kB signaling pathway [62,74,75].”
BackgroundRegenerative function of immune system: Modulation of muscle stem cells
Saini, J., McPhee, J. S., Al-Dabbagh, S., Stewart, C. E., & Al‐Shanti, N. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.03.006 · Cited by 129 · see citing works
“338 339 TNFα can also activate NF-κB within myoblasts, resulting in myoblast proliferation through the 340 up-regulation of cyclin D1 while suppressing differentiation, as well as inhibiting MyoD 341 expression, further suppressing differentiation (Langen et al., 2004).”
BackgroundHeightened muscle inflammation susceptibility may impair regenerative capacity in aging humans
Merritt, E. K., Stec, M. J., Thalacker-Mercer, A., Windham, S. T., Cross, J. M., Shelley, D. P., Craig Tuggle, S., Kosek, D. J., Kim, J.-S., & Bamman, M. M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00019.2013 · Cited by 127 · see citing works
“Both the greater basal TNF- receptor content and reduced basal I B protein content in AGE64 cells likely drive increased NF- B activation and reduced myogenesis in AGE64 cells at higher doses of TNF- , as the overall increased NF- B signaling can reduce myoblast differentiation via reduced expression (18) and destabil…”
BackgroundMesquita‐Ferrari, R. A., Martins, M. D., Silva, J. A., da Silva, T. D., Piovesan, R. F., Pavesi, V. C. S., Bussadori, S. K., & Fernandes, K. P. S. (2010) · Lasers in Medical Science · doi:10.1007/s10103-010-0850-5 · Cited by 126 · see citing works
“Langen et al. [21] found that the administration of TNF-α induces muscle atrophy, demonstrating a causal role for this cytokine in inflammationassociated muscle wasting and demonstrated that myoblast differentiation and fusion are inhibited in response to inflammatory stimuli, including TNF-α [ 22 ].”
BackgroundAssis, L., Moretti, A. I. S., Abrahão, T. B., Cury, V., de Souza, H. P., Hamblin, M. R., & Parizotto, N. A. (2012) · Lasers in Surgery and Medicine · doi:10.1002/lsm.22077 · Cited by 126 · see citing works
“Excessive production of these mediators can be harmful for muscle repair, as it intensifies inflammation and can inhibit differentiation and fusion of myoblasts, impairing the regeneration of muscle tissue [11,12].”
BackgroundThe epigenetic network regulating muscle development and regeneration
Palacios, D., & Puri, P. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20489 · Cited by 124 · see citing works
“…on the observation that in myoblasts high levels of the serum-inducible inhibitor of differentiation (Id) proteins sequestrate the heterodimeric partners of MyoD, the products of the E2A gene (E12 and E47), thereby preventing MyoD from binding the DNA (Benezra et al., 1990; Lassar et al., 1991).”
BackgroundCellular Players in Skeletal Muscle Regeneration
Ceafalan, L. C., Popescu, B. O., & Hinescu, M. E. (2014) · BioMed Research International · doi:10.1155/2014/957014 · Cited by 122 · see citing works
Tumor necrosis factor-α gene transfer induces cachexia and inhibits muscle regeneration
Coletti, D., Moresi, V., Adamo, S., Molinaro, M., & Sassoon, D. A. (2005) · genesis · doi:10.1002/gene.20160 · Cited by 124 · see citing works
“Our studies and those from other groups have elucidated several molecular pathways through which TNFa may inhibit the myogenic program (Coletti et al., 2002; Foulstone et al., 2004; Langen et al., 2004).”
Muscle cachexia is regulated by a p53–PW1/Peg3-dependent pathwayPreprint
Schwarzkopf, M., Coletti, D., Sassoon, D. A., & Marazzi, G. (2006) · Genes & Development · doi:10.1101/gad.412606 · Cited by 123 · see citing works
“(**) p < 0.01 by Student’s t-test 3442 GENES & DEVELOPMENT To address this concern, we used C2C12 myogenic cells that also express p53 (Latella et al. 2004; data not shown) and assayed differentiation in the presence or absence of the p53 inhibitor Pifithrin (Komarov et al. 1999) in combination…”
BackgroundMethodInfluentialNF-κB Signaling in Skeletal Muscle Health and Disease
Peterson, J. M., Bakkar, N., & D, D. C. G. (2011) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-385940-2.00004-8 · Cited by 118 · see citing works
Strle, K., Broussard, S. R., McCusker, R. H., Shen, W. H., Johnson, R. W., Freund, G. G., Dantzer, R., & Kelley, K. W. (2004) · Endocrinology · doi:10.1210/en.2003-1749 · Cited by 115 · see citing works
“Both HS and FBS contain numerous growth-promoting factors, including IGF-I.”
MethodInfluentialImmune system and sarcopenia: Presented relationship and future perspective
Zhang, X., Li, H., He, M., Wang, J., Wu, Y., & Li, Y. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111823 · Cited by 112 · see citing works
Age-related sarcopenia and its pathophysiological bases
Ogawa, S., Yakabe, M., & Akishita, M. (2016) · Inflammation and Regeneration · doi:10.1186/s41232-016-0022-5 · Cited by 109 · see citing works
“Exposure of myoblasts to TNF-α causes inhibition of myogenic differentiation through increased proteolysis of MyoD by the ubiquitin-proteasome pathway in vitro [45].”
BackgroundMagee, P., Pearson, S., & Allen, J. (2008) · Lipids in Health and Disease · doi:10.1186/1476-511x-7-24 · Cited by 105 · see citing works
Age-related skeletal muscle dysfunction: causes and mechanisms.
Degens, H. (2007) · PubMed · Cited by 103 · see citing works
Nicastro, H., da Luz, C. R., Chaves, D. F. S., Bechara, L. R. G., Voltarelli, V. A., Rogero, M. M., & Lancha, A. H. (2012) · Journal of Nutrition and Metabolism · doi:10.1155/2012/136937 · Cited by 105 · see citing works
“The release of ROS induced by TNF-α induces degradation of the inhibitor-κB (IκB), which allows the nuclear factorkappaB (NF-κB) to translocate to the nucleus and to activate the transcription of several κB-dependent genes such as those encoding proinflammatory cytokines, and breakdown of MyoD and myogenin (regulators…”
Backgroundvan der Velden, J. L. J., LANGEN, R. C. J., KELDERS, M. C. J. M., Wouters, E. F. �., Janssen-Heininger, Y. M. W., & Schols, A. M. W. J. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00068.2005 · Cited by 105 · see citing works
Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration
Tachtsis, B., Camera, D., & Lacham-Kaplan, O. (2018) · Nutrients · doi:10.3390/nu10030309 · Cited by 104 · see citing works
Vogiatzis, I., Stratakos, G., Simoes, D. C. M., Terzis, G., Georgiadou, O., Roussos, C., & Zakynthinos, S. (2007) · Thorax · doi:10.1136/thx.2006.069310 · Cited by 122 · see citing works
“9 39 Study limitations The invasive nature of the muscle biopsies precluded a parallel, aged-matched, healthy control training group which would allow comparisons in training-induced changes in local muscle inflammatory and growth factors between healthy subjects and patients with COPD.”
Antioxidant Levels Represent a Major Determinant in the Regenerative Capacity of Muscle Stem Cells
Urish, K. L., Vella, J. B., Okada, M., Deasy, B. M., Tobita, K., Keller, B. B., Cao, B., Piganelli, J. D., & Huard, J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0274 · Cited by 103 · see citing works
“Vol. 20, January 1, 2009 517 factor kappa B (NF-B) pathway (Guttridge et al., 1999; Langen et al., 2004 ).”
Sishi, B., & Engelbrecht, A. (2011) · Cytokine · doi:10.1016/j.cyto.2011.01.009 · Cited by 99 · see citing works
Skeletal muscle dysfunction in COPD: clinical and laboratory observations
Man, W. D., Kemp, P. R., Moxham, J., & Polkey, M. I. (2009) · Clinical Science · doi:10.1042/cs20080659 · Cited by 98 · see citing works
Liao, P., Zhou, J.-P., Ji, L. L., & Zhang, Y. (2010) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00480.2009 · Cited by 103 · see citing works
Inducible nitric oxide synthase (iNOS) in muscle wasting syndrome, sarcopenia, and cachexia
Hall, D. T., Ma, J. F., Marco, S. D., & Gallouzi, I. (2011) · Aging · doi:10.18632/aging.100358 · Cited by 95 · see citing works
“Loss of MyoD is known to prevent the differentiation of myoblasts (undifferentiated muscle cells) [73, 88, 89], leading to a reduction in the repair and regeneration capacity of muscle fibers.”
BackgroundDogra, C., Hall, S. L., Wedhas, N., Linkhart, T. A., & Kumar, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608668200 · Cited by 94 · see citing works
Bhatnagar, S., Panguluri, S. K., Gupta, S. K., Dahiya, S., Lundy, R. F., & Kumar, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013262 · Cited by 94 · see citing works
“Furthermore, the inhibitory effect of TNF-a on myogenesis is mediated through the activation of NF-kB which downregulates the levels of myogenic regulatory factor MyoD in myoblasts through distinct mechanisms [18,19,20].”
BackgroundPhilippou, A., Maridaki, M., Theos, A., & Koutsilieris, M. (2012) · Advances in Clinical Chemistry · doi:10.1016/b978-0-12-394383-5.00010-2 · Cited by 91 · see citing works
NF-κB Activation Is Required for the Transition of Pulmonary Inflammation to Muscle Atrophy
LANGEN, R. C. J., Haegens, A., Vernooy, J. H. J., Wouters, E. F. �., de Winther, M. P. J., Carlsen, H., Steele, C. H., Shoelson, S. E., & Schols, A. M. W. J. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0119oc · Cited by 89 · see citing works
“C2C12 murine myoblasts were cultured and differentiated into myotubes, as previously described (21).”
MethodTGF-β's delay skeletal muscle progenitor cell differentiation in an isoform-independent manner
Schabort, E. J., van der Merwe, M., Loos, B., Moore, F. P., & Niesler, C. U. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.037 · Cited by 88 · see citing works
Atrophy and hypertrophy signalling in the diaphragm of patients with COPD
Testelmans, D., Crul, T., Maes, K., Agten, A., Crombach, M., Decramer, M., & Gayan‐Ramirez, G. (2009) · European Respiratory Journal · doi:10.1183/09031936.00091108 · Cited by 87 · see citing works
TWEAK and cIAP1 Regulate Myoblast Fusion Through the Noncanonical NF-κB Signaling Pathway
Enwere, E. K., Holbrook, J., Mrad, R. L., Vineham, J., Timusk, K., Sivaraj, B., Isaac, M. B., Uehling, D., Al‐awar, R., LaCasse, E. C., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2003086 · Cited by 85 · see citing works
Photobiomodulation and different macrophages phenotypes during muscle tissue repair
Souza, N. H. C., Mesquita‐Ferrari, R. A., Rodrigues, M. F. S. D., da Silva, D. D. F. T., Ribeiro, B. G., Alves, A. N., Garcia, M. P., Nunes, F. D., da Silva, E. M., França, C. M., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13757 · Cited by 84 · see citing works
“infiltration as well as the proliferation and differentiation of myogenic precursor cells.(3,27,28) Here, IL-6 up‐regulation could be responsible for the increased number of immature muscle fibres found in the group treated with PBM at 780 nm.”
BackgroundAlami-Durante, H., Bazin, D., Cluzeaud, M., Fontagné-Dicharry, S., Kaushik, S., & Geurden, I. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2017.10.030 · Cited by 83 · see citing works
Duchesne, É., Dufresne, S. S., & Dumont, N. A. (2017) · Physical Therapy · doi:10.1093/ptj/pzx056 · Cited by 81 · see citing works
Wang, Y., Welc, S. S., Wehling‐Henricks, M., & Tidball, J. G. (2018) · Aging Cell · doi:10.1111/acel.12828 · Cited by 80 · see citing works
Franch, H. A., Raissi, S., Wang, X., Zheng, B., Bailey, J. L., & Price, S. R. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00440.2003 · Cited by 80 · see citing works
Differential Cytokine Gene Expression in the Diaphragm in Response to Strenuous Resistive Breathing
Vassilakopoulos, T., Divangahi, M., Rallis, G., Kishta, O. A., Petrof, B. J., Comtois, A. S., & Hussain, S. N. A. (2004) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200308-1071oc · Cited by 79 · see citing works
Álvarez, Á. M., DeOcesano-Pereira, C., Teixeira, C., & Moreira, V. (2020) · Cells · doi:10.3390/cells9092005 · Cited by 78 · see citing works
Pharmacological blockade of TNFα prevents sarcopenia and prolongs survival in aging mice
Sciorati, C., Gamberale, R., Monno, A., Citterio, L., Lanzani, C., De Lorenzo, R., Ramirez, G. A., Esposito, A., Manunta, P., Manfredi, A. A., et al. (2020) · Aging · doi:10.18632/aging.202200 · Cited by 79 · see citing works
“TNFα also down-regulates the expression of anabolic hormones and growth factors [33], reduces the expression of MyoD and myogenin in regenerating muscles and increases MyoD degradation through the ubiquitin proteasome pathway in myoblasts [12, 34].”
BackgroundAlter, J., Rozentzweig, D., & Bengal, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801379200 · Cited by 77 · see citing works
Stem Cell and Macrophage Roles in Skeletal Muscle Regenerative Medicine
Scala, P., Rehak, L., Giudice, V., Ciaglia, E., Puca, A. A., Selleri, C., Porta, G. D., & Maffulli, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910867 · Cited by 76 · see citing works
“Mice HS/RL TNF-α Soleus Gastrocnemius Decrease of Myog expression [85]”
BackgroundMoresi, V., Pristerà, A., Scicchitano, B. M., Molinaro, M., Teodori, L., Sassoon, D. A., Adamo, S., & Coletti, D. (2008) · Stem Cells · doi:10.1634/stemcells.2007-0493 · Cited by 76 · see citing works
Oh, J., Sinha, I., Tan, K. Y., ROSNER, B. A., Dreyfuss, J. M., Gjata, O., Tran, P. H., Shoelson, S. E., & Wagers, A. J. (2016) · Aging · doi:10.18632/aging.101098 · Cited by 77 · see citing works
“Canonical NFκB signaling is activated in proliferating myoblasts and appears to repress myoblast differentiation, in part by inhibiting expression of the myogenic transcription factor MyoD [11,12].”
Backgroundvan der Velden, J. L. J., Schols, A. M. W. J., Willems, J., KELDERS, M. C. J. M., & LANGEN, R. C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707812200 · Cited by 72 · see citing works
Reductive stress impairs myogenic differentiation
Rajasekaran, N. S., Shelar, S. B., Jones, D. P., & Hoidal, J. R. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101492 · Cited by 70 · see citing works
Tidball, J. G., Flores, I., Welc, S. S., Wehling-Henricks, M., & Ochi, E. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2020.111200 · Cited by 66 · see citing works
Impaired regeneration: A role for the muscle microenvironment in cancer cachexia
Talbert, E. E., & D, D. C. G. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.09.009 · Cited by 67 · see citing works
Kotelnikova, E. A., Shkrob, M., Pyatnitskiy, M. A., Ferlini, A., & Daraselia, N. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002365 · Cited by 66 · see citing works
“. MyoD impaired activity in dystrophin-deficient muscle can be caused by activation of NFkB and IFNG pathways that result in MyoD destabilization”
BackgroundMuscle-specific GSK-3β ablation accelerates regeneration of disuse-atrophied skeletal muscle
Pansters, N. A. M., Schols, A. M. W. J., Verhees, K. J. P., de Theije, C. C., Snepvangers, F. J. M., KELDERS, M. C. J. M., Ubags, N. D. J., Haegens, A., & LANGEN, R. C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.006 · Cited by 66 · see citing works
Haren, M. T., Malmstrom, T. K., Miller, D. K., Patrick, P., Perry, H. M., Herning, M. M., Banks, W. A., & Morley, J. E. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp148 · Cited by 65 · see citing works
Sharples, A. P., Al‐Shanti, N., & Stewart, C. E. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22252 · Cited by 63 · see citing works
“It has been previously reported that TNF-a (10 ng ml 1) induced reduction of myogenin and myoD protein levels in C2C12 cells as a consequence of myoD destabilisation by nuclear factor kappa beta (NF-kb) (Langen et al., 2004).”
BackgroundThe Cytokine Basis of Cachexia and its Treatment: Are They Ready for Prime Time?
Yeh, S., Blackwood, K., & Schuster, M. W. (2008) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2008.01.003 · Cited by 63 · see citing works
Physical activity and body composition in patients with ankylosing spondylitis
Plasqui, G., Boonen, A. E. R. C. H., Geusens, P., Kroot, E.-J. J. A., Starmans, M., & van der Linden, S. (2011) · Arthritis Care & Research · doi:10.1002/acr.20566 · Cited by 62 · see citing works
“The importance of TNF in the pathophysiology of AS (1) but also in muscle loss is well known (8,30,31).”
BackgroundInactivation of glycogen synthase kinase-3β (GSK-3β) enhances skeletal muscle oxidative metabolism
Theeuwes, W. F., Gosker, H. R., LANGEN, R. C. J., Verhees, K. J. P., Pansters, N., Schols, A. M. W. J., & Remels, A. H. V. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.018 · Cited by 62 · see citing works
Remels, A. H. V., Gosker, H. R., van der Velden, J. L. J., LANGEN, R. C. J., & Schols, A. M. W. J. (2007) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2007.06.003 · Cited by 62 · see citing works
Kang, M. S., Kang, J. I., Thi, P. L., Park, K. M., Hong, S. W., Choi, Y. S., Han, D., & Park, K. D. (2021) · ACS Macro Letters · doi:10.1021/acsmacrolett.0c00845 · Cited by 61 · see citing works
Mechanisms of Muscle Injury, Repair, and Regeneration
Tidball, J. (2011) · Comprehensive Physiology · doi:10.1002/j.2040-4603.2011.tb00387.x · Cited by 401 · see citing works
Genetic Ablation of TWEAK Augments Regeneration and Post-Injury Growth of Skeletal Muscle in Mice
Mittal, A., Bhatnagar, S., Kumar, A., Paul, P. K., Kuang, S., & Kumar, A. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100335 · Cited by 61 · see citing works
A novel autosomal recessive limb-girdle muscular dystrophy with quadriceps atrophy maps to 11p13-p12
Jarry, J., Rioux, M., Bolduc, V., Robitaille, Y., Khoury, V., Thiffault, I., Tétreault, M., Loisel, L., Bouchard, J. P., & Brais, B. (2006) · Brain · doi:10.1093/brain/awl270 · Cited by 60 · see citing works
“…to the development of skeletal muscles, since it has been reported that TNFa inhibits myogenic differentiation through the NFkB-dependent destabilization of the MyoD protein activity, which interferes with skeletal muscle regeneration and may contribute to muscle wasting (Langen et al., 2004).”
Background
- Authors
- Langen, R. C. J., van der Velden, J. L. J., Schols, A. M. W. J., Kelders, M. C. J. M., Wouters, E. F. M., & Janssen‐Heininger, Y. M. W.
- Affiliations
- Maastricht University (NL)
- Department of Respiratory Medicine Maastricht University Maastricht The Netherlands
- Department of Pathology University of Vermont Burlington Vermont USA
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2004-02
- Volume
- 18
- Issue
- 2
- Pages
- 227-237
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2057070304
- Cited by
- 319
- References
- 51
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 11 · 2023: 11 · 2022: 10 · 2021: 16 · 2020: 21 · 2019: 7 · 2018: 14 · 2017: 15 · 2016: 14 · 2015: 12 · 2014: 13 · 2013: 19 · 2012: 19
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Research Publications (Maastricht University) (publishedVersion)
- Research Publications (Maastricht University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- TNF-α, myogenesis, MyoD, NF-κB, RelA/p65, protein destabilization, ubiquitin-proteasome system, muscle atrophy, skeletal muscle regeneration, C2C12 myoblasts, cell cycle exit
- MeSH terms
- Animals, Cell Cycle, Cell Differentiation, Cell Line, Cysteine Endopeptidases, Half-Life, Male, Mice, Inbred C57BL, Multienzyme Complexes, Regeneration, Tumor Necrosis Factor-alpha, Transcriptional Activation, NF-kappa B, MyoD Protein, Muscle, Skeletal, Muscle Development, Ubiquitin, Myoblasts, Proteasome Endopeptidase Complex, Mice, Transcription Factor RelA
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
