Effect of Branched-Chain Amino Acids on Muscle Atrophy in Cancer Cachexia
Open accessAbstract
In the present study, the BCAAs (branched-chain amino acids) leucine and valine caused a significant suppression in the loss of body weight in mice bearing a cachexia-inducing tumour (MAC16), producing a significant increase in skeletal muscle wet weight, through an increase in protein synthesis and a decrease in degradation. Leucine attenuated the increased phosphorylation of PKR (double-stranded-RNA-dependent protein kinase) and eIF2alpha (eukaryotic initiation factor 2alpha) in skeletal muscle of mice bearing the MAC16 tumour, due to an increased expression of PP1 (protein phosphatase 1). Weight loss in mice bearing the MAC16 tumour was associated with an increased amount of eIF4E bound to its binding protein 4E-BP1 (eIF4E-binding protein 1), and a progressive decrease in the active eIF4G-eIF4E complex due to hypophosphorylation of 4E-BP1. This may be due to a reduction in the phosphorylation of mTOR (mammalian target of rapamycin), which may also be responsible for the decreased phosphorylation of p70(S6k) (70 kDa ribosomal S6 kinase). There was also a 5-fold increase in the phosphorylation of eEF2 (eukaryotic elongation factor 2), which would also decrease protein synthesis through a decrease in translation elongation. Treatment with leucine increased phosphorylation of mTOR and p70(S6k), caused hyperphosphorylation of 4E-BP1, reduced the amount of 4E-BP1 associated with eIF4E and caused an increase in the eIF4G-eIF4E complex, together with a reduction in phosphorylation of eEF2. These changes would be expected to increase protein synthesis, whereas a reduction in the activation of PKR would be expected to attenuate the increased protein degradation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In cachexia-inducing tumor NMRI mice, leucine or valine increase protein synthesis and attenuate increased protein degradation.
“In cachexia-inducing tumor Naval Medical Research Institute mice with a significant suppression in the loss of body weight, leucine or valine could increase protein synthesis and attenuate the increased protein degradation [26].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [26]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
A Selective Inhibitor of eIF2α Dephosphorylation Protects Cells from ER Stress
Boyce, M., Bryant, K. F., Jousse, C., Long, K., Harding, H. P., Scheuner, D. L., Kaufman, R. J., Ma, D., Coen, D. M., Ron, D., et al. (2005) · Science · doi:10.1126/science.1101902 · Cited by 1,403 · see citing works
Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,370 · see citing works
A fluorometric method for the estimation of tyrosine in plasma and tissues.
Waalkes, T. P., & Udenfriend, S. (1957) · PubMed · Cited by 971 · see citing works
Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase
Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works
Anthony, J. C., Yoshizawa, F., Anthony, T. G., Vary, T. C., Jefferson, L. S., & Kimball, S. R. (2000) · Journal of Nutrition · doi:10.1093/jn/130.10.2413 · Cited by 804 · see citing works
Initiation of Protein Synthesis in Eukaryotic Cells
Pain, V. M. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00747.x · Cited by 712 · see citing works
Ribosomal S6 Kinase Signaling and the Control of Translation
Dufner, A., & Thomas, G. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4683 · Cited by 676 · see citing works
(1998) · British Journal of Cancer · doi:10.1038/bjc.1998.1 · Cited by 650 · see citing works
Trends in cancer incidence and mortality in Scotland: description and possible explanations
Swerdlow, A. J., Silva, I. D. S., Reid, A., Qiao, Z., Brewster, D., & Arrundale, J. (1998) · British Journal of Cancer · doi:10.1038/bjc.1998.424 · Cited by 531 · see citing works
Duncan, R., Milburn, S. C., & Hershey, J. W. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75938-9 · Cited by 483 · see citing works
Anthony, J. C., Anthony, T. G., Kimball, S. R., Vary, T. C., & Jefferson, L. S. (2000) · Journal of Nutrition · doi:10.1093/jn/130.2.139 · Cited by 469 · see citing works
TSC2: filling the GAP in the mTOR signaling pathway
Li, Y. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.11.007 · Cited by 418 · see citing works
Rieu, I., Balage, M., Sornet, C., Giraudet, C., Pujos, E., Grizard, J., Mosoni, L., & Dardevet, D. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.110742 · Cited by 410 · see citing works
Rowlands, A., Panniers, R., & Henshaw, E. C. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60596-4 · Cited by 335 · see citing works
Functional properties of phosphorylated elongation factor 2
CARLBERG, U., NILSSON, A., & Nygârd, O. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19169.x · Cited by 287 · see citing works
Minich, W. B., Balasta, M. L., Goss, D. J., & Rhoads, R. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7668 · Cited by 286 · see citing works
Whitehouse, A., Smith, H. J., Drake, J. L., & Tisdale, M. J. (2001) · PubMed · Cited by 226 · see citing works
Self-citationAnthony, J. C., Lang, C. H., Crozier, S. J., Anthony, T. G., MacLean, D. A., Kimball, S. R., & Jefferson, L. S. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00208.2001 · Cited by 219 · see citing works
Small molecule inhibitors of the RNA-dependent protein kinase
Jammi, N. V., Whitby, L. R., & Beal, P. A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01318-4 · Cited by 205 · see citing works
Regulation of protein synthesis by branched-chain amino acids in vivo
Yoshizawa, F. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.07.013 · Cited by 193 · see citing works
Anthony, J. C., Reiter, A. K., Anthony, T. G., Crozier, S. J., Lang, C. H., MacLean, D. A., Kimball, S. R., & Jefferson, L. S. (2002) · Diabetes · doi:10.2337/diabetes.51.4.928 · Cited by 177 · see citing works
Effects of preparatory patient education for radiation oncology patients
Rainey, L. C. (1985) · Cancer · doi:10.1002/1097-0142(19850901)56:5 · Cited by 174 · see citing works
Skeletal Muscle Atrophy, a Link between Depression of Protein Synthesis and Increase in Degradation
Eley, H. L., & Tisdale, M. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610378200 · Cited by 151 · see citing works
Self-citationIncreased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss.
Khal, J., Hine, A., Fearon, K., Dejong, C., & Tisdale, M. (2005) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2004.10.017 · Cited by 150 · see citing works
Self-citationSmith, K., & Tisdale, M. (1993) · British Journal of Cancer · doi:10.1038/bjc.1993.126 · Cited by 149 · see citing works
Self-citationWhitehouse, A., & Tisdale, M. J. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6601132 · Cited by 136 · see citing works
Self-citationBibby, M. C., Double, J. A., Ali, S. A., Fearon, K. C. H., Brennan, R. A., & Tisdale, M. J. (1987) · PubMed · Cited by 114 · see citing works
Self-citationRiazi, R., Wykes, L., Ball, R. O., & Pencharz, P. B. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1383 · Cited by 105 · see citing works
Russell, S. T., Eley, H. L., & Tisdale, M. J. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.003 · Cited by 90 · see citing works
Self-citationInduction of muscle protein degradation and weight loss by a tumor product.
Todorov, P., McDevitt, T., Cariuk, P., Coles, B., Deacon, M. M., & Tisdale, M. J. (1996) · PubMed · Cited by 84 · see citing works
Self-citationStimulation of protein phosphatase activity by insulin and growth factors in 3T3 cells.
Chan, C. P., McNall, S. J., Krebs, E. G., & Fischer, E. H. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6257 · Cited by 82 · see citing works
Shen, W., Boyle, D. W., Wisniowski, P., Bade, A., & Liechty, E. A. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.06080 · Cited by 63 · see citing works
Nitrogen excretion in cancer cachexia and its modification by a high fat diet in mice.
Beck, S., & Tisdale, M. J. (1989) · PubMed · Cited by 62 · see citing works
Self-citationBranched‐chain amino acids: A role in skeletal muscle proteolysis in catabolic states?
Busquets, S., Alvarez, B., López-Soriano, F. J., & Argilés, J. M. A. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10097 · Cited by 48 · see citing works
Tan, S., Tareen, S. U., Melville, M. W., Blakely, C. M., & Katze, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205109200 · Cited by 47 · see citing works
Eley, H. L., Russell, S. T., & Tisdale, M. J. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603704 · Cited by 46 · see citing works
Self-citationTalvas, J., Obled, A., Fafournoux, P., & Mordier, S. B. (2006) · Journal of Nutrition · doi:10.1093/jn/136.6.1466 · Cited by 43 · see citing works
Ventrucci, G., de Mello, M. A. R., & Gomes‐Marcondes, M. C. C. (2007) · BMC Cancer · doi:10.1186/1471-2407-7-42 · Cited by 42 · see citing works
Fraser, C. S. A., Pain, V. M., & Morley, S. (1999) · Biochemical Journal · doi:10.1042/bj3420519 · Cited by 30 · see citing works
Russell, S. T., Eley, H. L., & Tisdale, M. J. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.02.005 · Cited by 15 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Tisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,192 · see citing works
Self-citationLenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 492 · see citing works
Molecular and cellular mechanisms of skeletal muscle atrophy: an update
Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 372 · see citing works
Dickinson, J. M., Fry, C. S., Drummond, M. J., Gundermann, D. M., Walker, D. K., Glynn, E. L., Timmerman, K. L., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2011) · The Journal of Nutrition · doi:10.3945/jn.111.139485 · Cited by 282 · see citing works
Cancer cachexia—pathophysiology and management
Suzuki, H., Asakawa, A., Amitani, H., Nakamura, N., & Inui, A. (2013) · Journal of gastroenterology · doi:10.1007/s00535-013-0787-0 · Cited by 268 · see citing works
White, J. P., Baynes, J. W., Welle, S. L., Kostek, M. C., Matesic, L. E., Sato, S., & Carson, J. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024650 · Cited by 260 · see citing works
“The phosphorylation of mTOR target substrates, p70S6K and 4EBP1, corresponded with the reduction in myofibrillar protein synthesis throughout the progression of cachexia and are consistent with observations in other models of cancer cachexia [14,15].”
Eukaryotic elongation factor‐2 (eEF2): its regulation and peptide chain elongation
Kaul, G., Pattan, G., & Rafeequi, T. (2011) · Cell Biochemistry and Function · doi:10.1002/cbf.1740 · Cited by 216 · see citing works
Cancer-induced muscle wasting: latest findings in prevention and treatment
Aversa, Z., Costelli, P., & Muscaritoli, M. (2017) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834017698643 · Cited by 212 · see citing works
Regulation of Muscle Protein Synthesis and the Effects of Catabolic States
Gordon, B. S., Kelleher, A., & Kimball, S. (2013) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2013.05.039 · Cited by 195 · see citing works
Branched-chain amino acids, mitochondrial biogenesis, and healthspan: an evolutionary perspective
Valerio, A., D'Antona, G., & Nisoli, E. (2011) · Aging · doi:10.18632/aging.100322 · Cited by 196 · see citing works
Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
Kenney, J. W., Moore, C. E., Xuemin, W., & Proud, C. G. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.04.003 · Cited by 182 · see citing works
The Complex Role of Branched Chain Amino Acids in Diabetes and Cancer
O’Connell, T. M. (2013) · Metabolites · doi:10.3390/metabo3040931 · Cited by 130 · see citing works
Herningtyas, E. H., Okimura, Y., Handayaningsih, A. E., Yamamoto, D., Maki, T., Iida, K., Takahashi, Y., Kaji, H., & Chihara, K. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.004 · Cited by 113 · see citing works
Inflammatory burden and amino acid metabolism in cancer cachexia
Durham, W. J., Dillon, E. L., & Sheffield‐Moore, M. (2008) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32831cef61 · Cited by 110 · see citing works
Dukes, A., Davis, C., Refaey, M. E., Upadhyay, S. K., Mork, S., Arounleut, P., Johnson, M. H., Hill, W., Isales, C. M., & Hamrick, M. W. (2015) · Nutrition · doi:10.1016/j.nut.2015.02.011 · Cited by 106 · see citing works
Muscle atrophy in experimental cancer cachexia: Is the IGF‐1 signaling pathway involved?
Penna, F., Bonetto, A., Muscaritoli, M., Costamagna, D., Minero, V. G., Bonelli, G., Fanelli, F., Baccino, F., & Costelli, P. (2010) · International Journal of Cancer · doi:10.1002/ijc.25146 · Cited by 111 · see citing works
Eley, H. L., Russell, S. T., & Tisdale, M. J. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90567.2008 · Cited by 100 · see citing works
Self-citationResistance exercise and nutrition to counteract muscle wasting
Little, J. P., & Phillips, S. M. (2009) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h09-093 · Cited by 100 · see citing works
Eley, H. L., Russell, S. T., & Tisdale, M. J. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90530.2008 · Cited by 100 · see citing works
Self-citationAl‐Majid, S., & Waters, H. F. (2008) · Biological Research For Nursing · doi:10.1177/1099800408317345 · Cited by 99 · see citing works
Cachexia and pancreatic cancer: are there treatment options?
Mueller, T., Burmeister, M.-A., Bachmann, J., & Martignoni, M. E. (2014) · PubMed Central · doi:10.3748/wjg.v20.i28.9361 · Cited by 96 · see citing works
Mueller, T. C., Bachmann, J., Prokopchuk, O., Friess, H., & Martignoni, M. E. (2016) · BMC Cancer · doi:10.1186/s12885-016-2121-8 · Cited by 95 · see citing works
Kovařík, M., Muthný, T., Šišpera, L., & Holeček, M. (2010) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-010-0037-3 · Cited by 93 · see citing works
Leucine as a treatment for muscle wasting: a critical review.
Ham, D. J., Caldow, M., Lynch, G., & Koopman, R. (2014) · Clinical Nutrition · doi:10.1016/j.clnu.2014.09.016 · Cited by 90 · see citing works
Exercise as an Anti-inflammatory Therapy for Cancer Cachexia: A Focus on Interleukin-6 Regulation.
Daou, H. (2019) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00147.2019 · Cited by 74 · see citing works
Molecular and neuroendocrine mechanisms of cancer cachexia
Mendes, M. C. S., Pimentel, G. D., Costa, F. O., & Carvalheira, J. B. C. (2015) · Journal of Endocrinology · doi:10.1530/joe-15-0170 · Cited by 87 · see citing works
Nutritional Interventions in Cancer Cachexia: Evidence and Perspectives From Experimental Models
van de Worp, W. R. P. H., Schols, A. M. W. J., Theys, J., van Helvoort, A., & LANGEN, R. C. J. (2020) · Frontiers in Nutrition · doi:10.3389/fnut.2020.601329 · Cited by 92 · see citing works
Immunomodulatory role of branched-chain amino acids
Bonvini, A., Coqueiro, A. Y., Tirapegui, J., Calder, P. C., & Rogero, M. M. (2018) · Nutrition Reviews · doi:10.1093/nutrit/nuy037 · Cited by 84 · see citing works
Cancer cachexia: medical management
Mantovani, G., & Madeddu, C. (2009) · Supportive Care in Cancer · doi:10.1007/s00520-009-0722-3 · Cited by 81 · see citing works
Branched-chain amino acids ameliorate heart failure with cardiac cachexia in rats
Tanada, Y., Shioi, T., Kato, T., Kawamoto, A., Okuda, J., & Kimura, T. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.06.021 · Cited by 80 · see citing works
Pancreatic cancer cachexia: three dimensions of a complex syndrome
Kordes, M., Larsson, L., Engstrand, L., & Löhr, M. J. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01301-4 · Cited by 78 · see citing works
Fuller, J. C., Sharp, R. L., Angus, H. F., Baier, S. M., & Rathmacher, J. A. (2011) · British Journal of Nutrition · doi:10.1017/s0007114510003582 · Cited by 75 · see citing works
Bai, G.-H., Tsai, M.-C., Tsai, H.-W., Chang, C., & Hou, W. (2021) · European Journal of Nutrition · doi:10.1007/s00394-021-02710-0 · Cited by 74 · see citing works
Potential antiproteolytic effects of L-leucine: observations of in vitro and in vivo studies
Zanchi, N. E., Nicastro, H., & Lancha, A. H. (2008) · Nutrition & Metabolism · doi:10.1186/1743-7075-5-20 · Cited by 73 · see citing works
Wilson, J. M., Kim, J., Lee, S., Rathmacher, J. A., Dalmau, B., Kingsley, J. D., Koch, H., Manninen, A. H., Saadat, R., & Panton, L. B. (2009) · Nutrition & Metabolism · doi:10.1186/1743-7075-6-6 · Cited by 72 · see citing works
Role of specific dietary amino acids in clinical conditions
Jonker, R., Engelen, M., & Deutz, N. (2012) · British Journal of Nutrition · doi:10.1017/s0007114512002358 · Cited by 65 · see citing works
Curcumin and muscle wasting—A new role for an old drug?
Alamdari, N., O’Neal, P., & Hasselgren, P.-O. (2008) · Nutrition · doi:10.1016/j.nut.2008.09.002 · Cited by 70 · see citing works
Leucine and mTOR-Dependent Activation of Muscle Protein Synthesis in Aging
de Bandt, J. (2016) · Journal of Nutrition · doi:10.3945/jn.116.234518 · Cited by 49 · see citing works
Bifari, F., Ruocco, C., Decimo, I., Fumagalli, G. F., Valerio, A., & Nisoli, E. (2017) · Genes & Nutrition · doi:10.1186/s12263-017-0582-2 · Cited by 68 · see citing works
Girón, M. D., Vílchez, J. D., Salto, R., Manzano, M., Sevillano, N., Campos, N., Argilés, J. M. A., Rueda, R., & López-Pedrosa, J. M. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12032 · 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
Yoshiji, H., Noguchi, R., Kitade, M., Kaji, K., Ikenaka, Y., Namisaki, T., Yoshii, J., Yanase, K., Yamazaki, M., Tsujimoto, T., et al. (2009) · Journal of Gastroenterology · doi:10.1007/s00535-009-0031-0 · Cited by 64 · see citing works
Are Tumoral Factors Responsible for Host Tissue Wasting in Cancer Cachexia?
Tisdale, M. J. (2010) · Future Oncology · doi:10.2217/fon.10.20 · Cited by 62 · see citing works
Self-citationMoreira‐Pais, A., Ferreira, R. M., & da Costa, R. M. G. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.07.010 · Cited by 63 · see citing works
Soares, J. D. P., Howell, S. L., Teixeira, F. J., & Pimentel, G. D. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200218100420 · Cited by 61 · see citing works
Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy
Wang, Y., Liu, Q., Quan, H., Kang, S.-G., Huang, K., & Tong, T. (2021) · Nutrients · doi:10.3390/nu13061914 · Cited by 61 · see citing works
Inhibition of SNAT2 by Metabolic Acidosis Enhances Proteolysis in Skeletal Muscle
Evans, K., Nasim, Z., Brown, J. R. G., Clapp, E. L., Amin, A., Yang, B., Herbert, T. P., & Bevington, A. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2007101108 · Cited by 59 · see citing works
Sun, M., Liu, S., Tang, J., Wang, Z., Gong, X., Sun, C., & Greenaway, F. (2009) · PROTEOMICS · doi:10.1002/pmic.200701002 · Cited by 58 · see citing works
Time course of cigarette smoke-induced changes of systemic inflammation and muscle structure
Krüger, K., Dischereit, G., Seimetz, M., Wilhelm, J., Weißmann, N., & Mooren, F. C. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00074.2015 · Cited by 56 · see citing works
Cancer‐ and Chemotherapy‐Induced Musculoskeletal Degradation
Sturgeon, K. M., Mathis, K. M., Rogers, C. J., Schmitz, K. H., & Waning, D. L. (2019) · JBMR Plus · doi:10.1002/jbm4.10187 · Cited by 53 · see citing works
Linking Cancer Cachexia‐Induced Anabolic Resistance to Skeletal Muscle Oxidative Metabolism
Hardee, J. P., Montalvo, R. N., & Carson, J. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8018197 · Cited by 53 · see citing works
Salomão, E. M., Toneto, A. T., Silva, G. O., & Gomes‐Marcondes, M. C. C. (2010) · Nutrition and Cancer · doi:10.1080/01635581.2010.492082 · Cited by 53 · see citing works
Metabolic Changes During Cancer Cachexia Pathogenesis
Shyh‐Chang, N. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6020-5_11 · Cited by 52 · see citing works
Treatment of cachexia in oncology
Tazi, E. H., & Errihani, H. H. (2010) · Indian Journal of Palliative Care · doi:10.4103/0973-1075.73644 · Cited by 50 · see citing works
Bajotto, G., Sato, Y., Kitaura, Y., & Shimomura, Y. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1825-8 · Cited by 50 · see citing works
Modulating Metabolism to Improve Cancer‐Induced Muscle Wasting
Penna, F., Ballarò, R., Beltrà, M., Lucia, S. D., & Costelli, P. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7153610 · Cited by 46 · see citing works
Nutrient interaction for optimal protein anabolism in resistance exercise
Breen, L., & Phillips, S. M. (2012) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e3283516850 · Cited by 45 · see citing works
Chen, M.-C., Chen, Y.-L., Lee, C.-F., Hung, C.-H., & Chou, T.-C. (2015) · PLOS ONE · doi:10.1371/journal.pone.0143594 · Cited by 45 · see citing works
Nutritional leucine supplementation attenuates cardiac failure in tumour‐bearing cachectic animals
Toneto, A. T., Ramos, L., Salomão, E. M., Tomasin, R., Áreas, M. A., & Gomes‐Marcondes, M. C. C. (2016) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12100 · Cited by 45 · see citing works
Nutritional Interventions to Improve Cachexia Outcomes in Cancer—A Systematic Review
Braha, A., Albai, A., Timar, B., Negru, S. M., Săftescu, S., Roman, D., & Popovici, D. I. (2022) · Medicina · doi:10.3390/medicina58070966 · Cited by 44 · see citing works
Mirza, K. A., Pereira, S. L., Voss, A. C., & Tisdale, M. J. (2013) · Nutrition · doi:10.1016/j.nut.2013.11.012 · Cited by 44 · see citing works
Self-citationPancreatic Cancer Cachexia: The Role of Nutritional Interventions
Mitchell, T., Clarke, L., Goldberg, A., & Bishop, K. S. (2019) · Healthcare · doi:10.3390/healthcare7030089 · Cited by 43 · see citing works
Chen, W., Zu, Y., Huang, Q., Chen, F., Wang, G., Lan, W., Bai, C., Lu, S., Yue, Y., & Deng, F. (2011) · Magnetic Resonance in Medicine · doi:10.1002/mrm.22957 · Cited by 41 · see citing works
Cancer cachexia update in head and neck cancer: Pathophysiology and treatment
Couch, M. E., Dittus, K. L., Toth, M. J., Willis, M. S., D, D. C. G., George, J. R., Chang, E. Y., Gourin, C. G., & Der‐Torossian, H. (2014) · Head & Neck · doi:10.1002/hed.23696 · Cited by 39 · see citing works
Advances in pharmacologic strategies for cancer cachexia
Madeddu, C., Mantovani, G., Gramignano, G., & Macciò, A. (2015) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2015.1079621 · Cited by 38 · see citing works
An overview of amines as nutritional supplements to counteract cancer cachexia
de Campos‐Ferraz, P. L., de Andrade, I. T., das Neves, W., Hangai, I., Alves, C. R. R., & Lancha, A. H. (2014) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-014-0138-x · Cited by 38 · see citing works
Metabolomics workflow for lung cancer: Discovery of biomarkers
Tang, Y., Li, Z., Lazar, L., Fang, Z., Tang, C., & Zhao, J. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.05.012 · Cited by 37 · see citing works
Zhao, Q., Cao, Y., Wang, Y., Hu, C., Hu, A., Ruan, L., Bo, Q., Liu, Q., Chen, W., Tao, F., et al. (2014) · PubMed · doi:10.6133/apjcn.2014.23.3.13 · Cited by 36 · see citing works
Alsolmei, F. A., Li, H., Pereira, S. L., Krishnan, P., Johns, P. W., & Siddiqui, R. A. (2019) · Nutrients · doi:10.3390/nu11051077 · Cited by 36 · see citing works
Cancer Cachexia Pathophysiology and Translational Aspect of Herbal Medicine
Suzuki, H., Asakawa, A., Amitani, H., Fujitsuka, N., Nakamura, N., & Inui, A. (2013) · Japanese Journal of Clinical Oncology · doi:10.1093/jjco/hyt075 · Cited by 36 · see citing works
Dalmazi, G. D., Quinkler, M. O., Deutschbein, T., Prehn, C. P., Rayes, N., Kroiß, M., Berr, C., Stalla, G. K., Faßnacht, M., Adamski, J., et al. (2017) · European Journal of Endocrinology · doi:10.1530/eje-17-0109 · Cited by 36 · see citing works
Cancer cachexia and diabetes: similarities in metabolic alterations and possible treatment,
Chevalier, S., & Farsijani, S. (2013) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2013-0369 · Cited by 34 · see citing works
Resistance Exercise’s Ability to Reverse Cancer-Induced Anabolic Resistance
Montalvo, R. N., Hardee, J. P., VanderVeen, B. N., & Carson, J. A. (2018) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000159 · Cited by 34 · see citing works
Rodent Model of Muscular Atrophy for Sarcopenia Study
Baek, K., Jung, Y., Kim, J., Park, J. S., Hah, Y., Kim, S.-J., & Yoo, J. (2020) · Journal of Bone Metabolism · doi:10.11005/jbm.2020.27.2.97 · Cited by 34 · see citing works
Cancer-Related Fatigue and Muscle Quality in Hodgkin’s Lymphoma Survivors
de Lima, F. D., Bottaro, M., Valeriano, R. D. O., Cruz, L., Battaglini, C. L., Vieira, C. A., & de Oliveira, R. J. (2017) · Integrative Cancer Therapies · doi:10.1177/1534735417712009 · Cited by 28 · see citing works
Attenuation of skeletal muscle atrophy in cancer cachexia by d-myo-inositol 1,2,6-triphosphate
Russell, S., Siren, P. M., Sirén, M., & Tisdale, M. J. (2009) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-008-0899-z · Cited by 30 · see citing works
Self-citationSystemic IL-6 regulation of eccentric contraction-induced muscle protein synthesis.
Hardee, J., Fix, D. K., Wang, X.-W., Goldsmith, E., Koh, H.-J., & Carson, J. (2018) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00063.2018 · Cited by 26 · see citing works
An update on promising agents for the treatment of cancer cachexia
Madeddu, C., & Mantovani, G. (2009) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3283311c6f · Cited by 26 · see citing works
Branched-Chain Amino Acid Supplementation Ameliorates Angiotensin II-Induced Skeletal Muscle Atrophy
Yamanashi, K., Kinugawa, S., Fukushima, A., Kakutani, N., Takada, S., Obata, Y., Nakano, I., Yokota, T., Kitaura, Y., Shimomura, Y., et al. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117593 · Cited by 25 · see citing works
Cancer cachexia’s metabolic signature in a murine model confirms a distinct entity
Der‐Torossian, H., Asher, S. A., Winnike, J. H., Wysong, A. S., Yin, X., Willis, M. S., O’Connell, T. M., & Couch, M. E. (2012) · Metabolomics · doi:10.1007/s11306-012-0485-6 · Cited by 25 · see citing works
Duan, Y., Li, F., Guo, Q., Wang, W., Zhang, L., Wen, C., Chen, X., & Yin, Y. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b04841 · Cited by 25 · see citing works
Metabolomic Profiles of Mouse Tissues Reveal an Interplay between Aging and Energy Metabolism
Zhou, Q., Kerbl-Knapp, J., Zhang, F., Korbelius, M., Kuentzel, K. B., Vujić, N., Akhmetshina, A., Hörl, G., Paar, M., Steyrer, E., et al. (2021) · Metabolites · doi:10.3390/metabo12010017 · Cited by 25 · see citing works
Li, H., Zhang, Q., Hao, Q., Li, Q., Yang, L., Yang, X., Wang, K., Teng, J., Gong, Z., & Jia, Y. (2024) · BMC Geriatrics · doi:10.1186/s12877-024-05144-5 · Cited by 23 · see citing works
Chevalier, S., & Winter, A. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000047 · Cited by 23 · see citing works
Smith, H. K., Matthews, K. G., Oldham, J. M., Jeanplong, F., Falconer, S. J., Bass, J. J., Salerno, M. S., Bracegirdle, J., & McMahon, C. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094356 · Cited by 22 · see citing works
Taylor, K. (2010) · Alternatives to Laboratory Animals · doi:10.1177/026119291003800613 · Cited by 22 · see citing works
The complex liaison between cachexia and tumor burden (Review)
Barbaro, A. D. L. (2015) · Oncology Reports · doi:10.3892/or.2015.4164 · Cited by 22 · see citing works
Physiological characterization of a mouse model of cachexia in colorectal liver metastases.
Murphy, K., Struk, A., Malcontenti‐Wilson, C., Christophi, C., & Lynch, G. (2013) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00057.2013 · Cited by 18 · see citing works
Metabolic Remodeling in Skeletal Muscle Atrophy as a Therapeutic Target
Renzini, A., Riera, C. S., Minic, I., D’Ercole, C., Lozanoska‐Ochser, B., Cedola, A., Gigli, G., Moresi, V., & Madaro, L. (2021) · Metabolites · doi:10.3390/metabo11080517 · Cited by 20 · see citing works
Hur, H., Kim, H.-J., Lee, D., & Jo, C. (2024) · Food & Function · doi:10.1039/d3fo03911k · Cited by 20 · see citing works
Influence of Amino Acids and Exercise on Muscle Protein Turnover, Particularly in Cancer Cachexia
Pradhan, R., Dieterich, W., Natarajan, A., Schwappacher, R., Reljic, D., Herrmann, H. J., Neurath, M. F., & Zopf, Y. (2024) · Cancers · doi:10.3390/cancers16101921 · Cited by 18 · see citing works
Chen, W., Lu, S., Ou, J., Wang, G., Zu, Y., Chen, F., & Bai, C. (2016) · Cancer Biomarkers · doi:10.3233/cbm-160607 · Cited by 18 · see citing works
Cachexia in chronic heart failure: endocrine determinants and treatment perspectives
Mangner, N., Matsuo, Y., Schuler, G. C., & Adams, V. (2012) · Endocrine · doi:10.1007/s12020-012-9767-z · Cited by 17 · see citing works
Liu, Z., Huang, C., Liu, Y., Lin, D., & Zhao, Y. (2018) · RSC Advances · doi:10.1039/c8ra00819a · Cited by 16 · see citing works
Cancer Cachexia: Underlying Mechanisms and Potential Therapeutic Interventions
Directo, D., & Lee, S.-R. (2023) · Metabolites · doi:10.3390/metabo13091024 · Cited by 12 · see citing works
Soares, J. D. P., Siqueira, J. M., Oliveira, I. C. L., Laviano, A., & Pimentel, G. D. (2019) · Nutrition · doi:10.1016/j.nut.2019.110698 · Cited by 14 · see citing works
Chen, S.-H., Li, P., Chan, Y., Cheng, Y., Lin, H.-Y., Lee, S.-C., Lu, W., Ma, Y.-X., Li, M.-Y., & Song, T. (2023) · Agriculture · doi:10.3390/agriculture13010209 · Cited by 13 · see citing works
Colardo, M., Martella, N., Varone, M., Pensabene, D., Caretti, G., Bianchini, G., Aramini, A., & Segatto, M. (2025) · Acta Physiologica · doi:10.1111/apha.70067 · Cited by 13 · see citing works
Nakamura, K., Sasayama, A., Takahashi, T., & Yamaji, T. (2015) · Nutrition and Cancer · doi:10.1080/01635581.2015.1053495 · Cited by 13 · see citing works
Li, C., Yang, Q., & Zhang, L. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2023.2290458 · Cited by 12 · see citing works
- Authors
- Eley, H. L., Russell, S. T., & Tisdale, M. J.
- Affiliations
- Aston University (GB)
- ORCID
- Russell, Steven T.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-09-12
- Volume
- 407
- Issue
- 1
- Pages
- 113-120
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2267397
- OpenAlex
- W2112898640
- Cited by
- 184
- References
- 40
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 8 · 2023: 13 · 2022: 6 · 2021: 9 · 2020: 13 · 2019: 10 · 2018: 10 · 2017: 12 · 2016: 7 · 2015: 11 · 2014: 11 · 2013: 11 · 2012: 10
- FWCI
- 4.69
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Keywords
- branched-chain amino acids, leucine, valine, cancer cachexia, muscle atrophy, skeletal muscle protein synthesis, protein degradation, eIF2α, protein phosphatase 1, 4E-BP1, eIF4E, mTOR, p70S6K, elongation factor 2, weight loss
- MeSH terms
- Amino Acids, Branched-Chain, Animals, Cachexia, Carrier Proteins, Cells, Cultured, Leucine, Mice, Inbred Strains, Muscular Atrophy, Neoplasms, Phosphoproteins, Phosphorylation, Protein Kinases, Proteoglycans, Time Factors, Valine, Cell Cycle Proteins, Myoblasts, Eukaryotic Initiation Factor-4E, Eukaryotic Initiation Factor-4G, Eukaryotic Initiation Factors, Adaptor Proteins, Signal Transducing, Mice
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
