Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice.
Open accessAbstract
The muscles of IL-6 transgenic mice suffer from atrophy. Experiments were carried out on these transgenic mice to elucidate activation of proteolytic systems in the gastrocnemius muscles and blockage of this activation by treatment with the anti-mouse IL-6 receptor (mIL-6R) antibody. Muscle atrophy observed in 16-wk-old transgenic mice was completely blocked by treatment with the mIL-6R antibody. In association with muscle atrophy, enzymatic activities and mRNA levels of cathepsins (B and L) and mRNA levels of ubiquitins (poly- and mono-ubiquitins) increased, whereas the mRNA level of muscle-specific calpain (calpain 3) decreased. All these changes were completely eliminated by treatment with the mIL-6R antibody. This IL-6 receptor antibody could, therefore, be effective against muscle wasting in sepsis and cancer cachexia, where IL-6 plays an important role.
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?
Transgenic mice chronically overexpressing IL-6 exhibit marked muscle atrophy, but knockout of IL-6 was not sufficient to prevent sarcopenia in a sepsis mouse model.
“the pilot study of Tsujinaka and colleagues showed that transgenic mice chronically overexpressing IL-6 exhibit a marked muscle atrophy [47]; however, the knockout of IL-6 was not sufficient to prevent sarcopenia in a sepsis mouse model [48].”
From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [47]
Proinflammatory cytokines may inhibit muscle progenitor cell differentiation, and reactive oxygen species (nitric oxide) from M1 cells can be cytotoxic in sufficient quantities, requiring resolution of the proinflammatory response for muscle recovery.
“However, it has also been shown that proinflammatory cytokines may inhibit muscle progenitor cell differentiation and that the reactive oxygen species that are produced by M1 cells (nitric oxide) can be cytotoxic if present in sufficient quantities, demonstrating the need for resolution of the proinflammatory response for muscle recovery to proceed beyond this initial stage [120–122].”
From Macrophage polarization: an opportunity for improved outcomes in biomaterials and regenerative medicine (2012) · cites this paper as [122]
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
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
Chirgwin, J. M., Przybyla, A., MacDonald, R. J., & Rutter, W. J. (1979) · Biochemistry · doi:10.1021/bi00591a005 · Cited by 21,725 · see citing works
[41] Cathepsin B, cathepsin H, and cathepsin L
Barrett, A. J., & Kirschke, H. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)80043-2 · Cited by 1,698 · see citing works
THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION
Hershko, A., & Ciechanover, A. J. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003553 · Cited by 1,419 · see citing works
Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
Richard, I., Broux, O., Allamand, V., Fougerousse, F., Chiannilkulchai, N., Bourg, N., Brenguier, L., Devaud, C., Pasturaud, P., Roudaut, C., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90368-2 · Cited by 998 · see citing works
Soluble interleukin-6 receptor triggers osteoclast formation by interleukin 6.
Tamura, T., Udagawa, N., Takahashi, N., Miyaura, C., Tanaka, S., Yamada, Y., Koishihara, Y., Ohsugi, Y., Kumaki, K., & Taga, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.11924 · Cited by 826 · see citing works
Self-citationEvidence for the involvement of interleukin 6 in experimental cancer cachexia.
Strassmann, G., Fong, M., Kenney, J. S., & Jacob, C. O. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115767 · Cited by 660 · see citing works
IgG1 plasmacytosis in interleukin 6 transgenic mice
Suematsu, S., Matsuda, T., Aozasa, K., Akira, S., Nakano, N., Ohno, S., Miyazaki, J., Yamamura, K., Hirano, T., & Kishimoto, T. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7547 · Cited by 586 · see citing works
Mitch, W. E., Medina, R., Grieber, S., May, R. C., England, B. K., Price, S. R., Bailey, J. L., & Goldberg, A. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117208 · Cited by 405 · see citing works
Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and μ-types
Sorimachi, H., Imajoh‐Ohmi, S., Emori, Y., Kawasaki, H., Ohno, S., Minami, Y., & Suzuki, K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47225-6 · Cited by 381 · see citing works
Self-citationWing, S. S., & Goldberg, A. L. (1993) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1993.264.4.e668 · Cited by 345 · see citing works
Matsuda, T., Hirano, T., & Kishimoto, T. (1988) · European Journal of Immunology · doi:10.1002/eji.1830180618 · Cited by 304 · see citing works
Furuno, K., Goodman, M. N., & Goldberg, A. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38923-9 · Cited by 300 · see citing works
Interleukin-6 Induces Skeletal Muscle Protein Breakdown in Rats
Goodman, M. N. (1994) · Experimental Biology and Medicine · doi:10.3181/00379727-205-43695 · Cited by 296 · see citing works
Medina, R., Wing, S. S., & Goldberg, A. L. (1995) · Biochemical Journal · doi:10.1042/bj3070631 · Cited by 294 · see citing works
Baracos, V., DeVivo, C., Hoyle, D., & Goldberg, A. (1995) · American Journal of Physiology · doi:10.1152/ajpendo.1995.268.5.e996 · Cited by 275 · see citing works
Reshaping a human antibody to inhibit the interleukin 6-dependent tumor cell growth.
Sato, K., Tsuchiya, M., Saldanha, J. W., Koishihara, Y., Ohsugi, Y., Kishimoto, T., & Bendig, M. M. (1993) · PubMed · Cited by 274 · see citing works
Self-citationCytokine receptors and signal transduction
Taga, T., & Kishimoto, T. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.15.1334470 · Cited by 267 · 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
Natural substrates of the Ubiquitin proteolytic pathway
RECHSTEINER, M. C. (1991) · Cell · doi:10.1016/0092-8674(91)90104-7 · Cited by 236 · see citing works
The Acute Metabolic Effects of Tumor Necrosis Factor Administration in Humans
Warren, R. S. (1987) · Archives of Surgery · doi:10.1001/archsurg.1987.01400240042007 · Cited by 233 · see citing works
Suematsu, S., Matsusaka, T., Matsuda, T., Ohno, S., Miyazaki, J., Yamamura, K., Hirano, T., & Kishimoto, T. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.232 · Cited by 227 · see citing works
Lowell, B. B., Ruderman, N. B., & Goodman, M. N. (1986) · Biochemical Journal · doi:10.1042/bj2340237 · Cited by 222 · see citing works
Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats.
Temparis, S., Asensi, M., Taillandier, D., AUROUSSEAU, E., Larbaud, D., Obled, A., Béchet, D., Ferrara, M., Estrela, J. M., & Attaix, D. (1994) · PubMed · Cited by 214 · see citing works
Interleukin 1 and tumor necrosis factor do not regulate protein balance in skeletal muscle
Moldawer, L. L., Svaninger, G., Gélin, J., & Lundholm, K. (1987) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1987.253.6.c766 · Cited by 196 · see citing works
Sorimachi, H., Saido, T. C., & Suzuki, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80595-4 · Cited by 183 · see citing works
Self-citationDistribution of Cathepsins B and H in Rat Tissues and Peripheral Blood Cells1
Kominami, E., Tsukahara, T., Bando, Y., & Katunuma, N. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135277 · Cited by 182 · see citing works
Self-citationSkeletal muscle metabolism in patients with malignant tumor
Lundholm, K., Bylund, A., Holm, J., & Scherstén, T. (1976) · European Journal of Cancer (1965) · doi:10.1016/0014-2964(76)90036-0 · Cited by 180 · see citing works
Characterization of IL-6 receptor expression by monoclonal and polyclonal antibodies.
Hirata, Y., Taga, T., Hibi, M., Nakano, N., Hirano, T., & Kishimoto, T. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.9.2900 · Cited by 175 · see citing works
Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family
Dubiel, W., Ferrell, K., Pratt, G., & Rechsteiner, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50002-8 · Cited by 167 · see citing works
Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells.
Kanayama, H., Tanaka, K., Aki, M., Kagawa, S., Miyaji, H., Satoh, M., Okada, F., Sato, S., Shimbara, N., & Ichihara, A. (1991) · PubMed · Cited by 163 · see citing works
Self-citationGarc�a-Mart�nez, C., López-Soriano, F. J., & Argilés, J. M. A. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf00926829 · Cited by 160 · see citing works
Tsujinaka, T., Ebisui, C., Fujita, J., Kishibuchi, M., Morimoto, T., Ogawa, A., Katsume, A., Ohsugi, Y., Kominami, E., & Monden, M. (1995) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.1995.1168 · Cited by 159 · see citing works
Self-citationEbisui, C., Tsujinaka, T., Morimoto, T., Kan, K., Iijima, S., Yano, M., Kominami, E., Tanaka, K., & Monden, M. (1995) · Clinical Science · doi:10.1042/cs0890431 · Cited by 157 · see citing works
Self-citationRegulation of the acute phase and immune responses: interleukin-6.
Sehgal, P. B. (1989) · PubMed · Cited by 152 · 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
Purification and Tissue Distribution of Rat Cathepsin L1
Bando, Y., Kominami, E., & Katunuma, N. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a121703 · Cited by 133 · see citing works
Self-citationStrassmann, G., Fong, M., Freter, C. E., Windsor, S., D'Alessandro, F., & Nordan, R. P. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116816 · Cited by 131 · see citing works
Skeletal muscle and liver contain a soluble ATP + ubiquitin-dependent proteolytic system
Fagan, J. M., Waxman, L., & Goldberg, A. L. (1987) · Biochemical Journal · doi:10.1042/bj2430335 · Cited by 131 · see citing works
Molecular cloning and sequencing of cDNA for rat cathepsin L
Ishidoh, K., Towatari, T., Imajoh, S., Kawasaki, H., Kominami, E., Katunuma, N., & Suzuki, K. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80511-2 · Cited by 114 · see citing works
Self-citationKettelhut, Í. D. C., & Goldberg, A. L. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113467 · Cited by 110 · see citing works
The Ubiquitin System for Protein Degradation
Hershko, A. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.61.1.761 · Cited by 97 · see citing works
Anti‐human interleukin‐6 receptor antibody inhibits human myeloma growth in vivo
Suzuki, H., Yasukawa, K., Saito, T., Goitsuka, R., Hasegawa, A., Ohsugi, Y., Taga, T., & Kishimoto, T. (1992) · European Journal of Immunology · doi:10.1002/eji.1830220806 · Cited by 93 · see citing works
Self-citationJohnson, P. (1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90284-a · Cited by 90 · see citing works
Dubiel, W., Ferrell, K., & Rechsteiner, M. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81356-5 · Cited by 84 · see citing works
Tamura, T., Lee, D. H., Osaka, F., Fujiwara, T., Shin, S., Chung, C. H., Tanaka, K., & Ichihara, A. (1991) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(91)90090-9 · Cited by 82 · see citing works
Self-citationUbiquitin Gene Expression in Skeletal Muscle Is Increased by Tumor Necrosis Factor-α
Garcia‐Martínez, C., Llovera, M., Agell, N., López-Soriano, F. J., & Argilés, J. M. A. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1754 · Cited by 81 · see citing works
Induction of interleukin 6 by human and murine recombinant interleukin 1 in mice
Libert, C., Brouckaert, P., SHAW, A. R., & Fiers, W. (1990) · European Journal of Immunology · doi:10.1002/eji.1830200333 · Cited by 75 · see citing works
Interleukin 6 in Infection and Cancer
Sehgal, P. B. (1990) · Experimental Biology and Medicine · doi:10.3181/00379727-195-43129d · Cited by 71 · see citing works
Purification and characterization of the 26 S proteasome from spinach leaves.
Fujinami, K., Tanahashi, N., Tanaka, K., Ichihara, A., Cejka, Z., Baumeister, W. P., Miyawaki, M., Sato, T., & Nakagawa, H. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47331-0 · Cited by 58 · see citing works
Self-citation2 Cytokine receptors and signal transduction
Ihle, J. N., Witthuhn, B. A., Tang, B., Yi, T., & Quelle, F. W. (1994) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(05)80005-8 · Cited by 51 · see citing works
Introduction of Human γ1 Immunoglobulin Genes into Fertilized Mouse Eggs1
Yamamura, K., Kikutani, H., Takahashi, N., Taga, T., Akira, S., Kawai, K., Fukuchi, K., Kumahara, Y., Honjo, T., & Kishimoto, T. (1984) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a134845 · Cited by 50 · see citing works
Activation of the intramyofibral autophagic-lysosomal system in muscular dystrophy.
Kominami, E., Kunio, I., & Katunuma, N. (1987) · PubMed Central · Cited by 40 · see citing works
Self-citationHall-Angerås, M., Hasselgren, P.-O. J., Dimlich, R. V. W., & Fischer, J. E. (1991) · Metabolism · doi:10.1016/0026-0495(91)90114-c · Cited by 35 · see citing works
Human B-Cell Stimulatory Factor-2 Expressed in Escherichia Coli
Asagoe, Y., Yasukawa, K., Saito, T., MARUO, N., Miyata, K., Kono, T., Miyake, T., Kato, T., Kakidani, H., & Mitani, M. (1988) · Nature Biotechnology · doi:10.1038/nbt0788-806 · Cited by 29 · see citing works
Receptor-mediated uptake of horseradish peroxidase in innervated and denervated skeletal muscle
Tågerud, S., & Libelius, R. (1985) · Experimental Cell Research · doi:10.1016/0014-4827(85)90239-3 · Cited by 13 · see citing works
Flagged first, then by citations
1 of the 57 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Tisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,192 · see citing works
Brown, B. N., Ratner, B. D., Goodman, S. B., Amar, S., & Badylak, S. F. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.02.034 · Cited by 926 · see citing works
Stenvinkel, P., Ketteler, M., Johnson, R. J., Lindholm, B., Pecoits‐Filho, R., RIELLA, M. C., Heimbürger, O., Cederholm, T., & Girndt, M. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00200.x · Cited by 933 · see citing works
C-reactive protein predicts all-cause and cardiovascular mortality in hemodialysis patients
Yeun, J. Y., Levine, R. A., Mantadilok, V., & Kaysen, G. A. (2000) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(00)70200-9 · Cited by 885 · see citing works
Interleukin‐6 myokine signaling in skeletal muscle: a double‐edged sword?
Muñoz‐Cánoves, P., Scheele, C., Pedersen, B. K., & Serrano, A. L. (2013) · The FEBS Journal · doi:10.1111/febs.12338 · Cited by 774 · see citing works
Structure and physiological function of calpains
Sorimachi, H., Ishiura, S., & Suzuki, K. (1997) · Biochemical Journal · doi:10.1042/bj3280721 · Cited by 706 · see citing works
Self-citationEffects of Aging on Muscle Fibre Type and Size
Deschenes, M. R. (2004) · Sports Medicine · doi:10.2165/00007256-200434120-00002 · Cited by 671 · see citing works
Muscle‐derived interleukin‐6: possible biological effects
Pedersen, B. K., Steensberg, A., & Schjerling, P. (2001) · The Journal of Physiology · doi:10.1111/j.1469-7793.2001.0329c.xd · Cited by 599 · see citing works
Tsutamoto, T., 久永, 智., Wada, A., Maeda, K., Ohnishi, M., 深井, 大., Mabuchi, N., Sawaki, M., & Kinoshita, M. (1998) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(97)00494-4 · Cited by 563 · see citing works
Interleukin-6 predicts hypoalbuminemia, hypocholesterolemia, and mortality in hemodialysis patients
Bologa, R. M., Levine, D., Ts, P., Cheigh, J. S., Serur, D. S., Kh, S., & Rubin, A. L. (1998) · American Journal of Kidney Diseases · doi:10.1053/ajkd.1998.v32.pm9669431 · Cited by 551 · see citing works
Lenk, 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
Chronic Exposure to Interleukin-6 Causes Hepatic Insulin Resistance in Mice
Klover, P. J., Zimmers, T. A., Koniaris, L. G., & Mooney, R. A. (2003) · Diabetes · doi:10.2337/diabetes.52.11.2784 · Cited by 488 · see citing works
Tisdale, M. J. (1997) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/89.23.1763 · Cited by 489 · see citing works
Bonetto, A., Aydogdu, T., Jin, X., Zhang, Z., Zhan, R., Puzis, L., Koniaris, L. G., & Zimmers, T. A. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00039.2012 · Cited by 463 · see citing works
Skeletal Muscle as Potential Central Link between Sarcopenia and Immune Senescence
Nelke, C., Dziewas, R., Minnerup, J., Meuth, S. G., & Ruck, T. (2019) · eBioMedicine · doi:10.1016/j.ebiom.2019.10.034 · Cited by 437 · see citing works
Bowen, T. S., Schuler, G. C., & Adams, V. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12043 · Cited by 429 · see citing works
Monocyte Cytokine Production in an Elderly Population: Effect of Age and Inflammation
Roubenoff, R., Harris, T. B., Abad, L. W., Wilson, P. W. F., Dallal, G. E., & Dinarello, C. A. (1998) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/53a.1.m20 · Cited by 418 · see citing works
Cellular and molecular mechanisms underlying age-related skeletal muscle wasting and weakness
Ryall, J. G., Schertzer, J. D., & Lynch, G. S. (2008) · Biogerontology · doi:10.1007/s10522-008-9131-0 · Cited by 423 · see citing works
The Sick and the Weak: Neuropathies/Myopathies in the Critically Ill
Friedrich, O., Reid, M. B., den Berghe, G. V., Vanhorebeek, I., Hermans, G., Rich, M. M., & Larsson, L. (2015) · Physiological Reviews · doi:10.1152/physrev.00028.2014 · Cited by 394 · see citing works
Roubenoff, R., Parise, H., Payette, H., Abad, L. W., D’Agostino, R. B., Jacques, P. F., Wilson, P. W. F., Dinarello, C. A., & Harris, T. B. (2003) · The American Journal of Medicine · doi:10.1016/j.amjmed.2003.05.001 · Cited by 397 · see citing works
Kotler, D. P. (2000) · Annals of Internal Medicine · doi:10.7326/0003-4819-133-8-200010170-00015 · Cited by 385 · see citing works
Interleukin‐6 is a significant predictor of radiographic knee osteoarthritis: The Chingford study
Livshits, G., Zhai, G., Hart, D. J., Kato, B. S., Wang, H., Williams, F. M. K., & Spector, T. D. (2009) · Arthritis & Rheumatism · doi:10.1002/art.24598 · Cited by 383 · see citing works
Inflammatory Response and Body Composition in Chronic Obstructive Pulmonary Disease
Eid, A. A., Ionescu, A., Nixon, L. S., LEWIS-JENKINS, V., Matthews, S. B., Griffiths, T. L., & Shale, D. J. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.164.8.2008109 · Cited by 370 · 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
Tournadre, A., Vial, G., Capel, F., Soubrier, M., & Boirie, Y. (2019) · Joint Bone Spine · doi:10.1016/j.jbspin.2018.08.001 · Cited by 375 · see citing works
Bonetto, A., Aydogdu, T., Kunzevitzky, N., Guttridge, D. C., Khuri, S., Koniaris, L. G., & Zimmers, T. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022538 · Cited by 348 · see citing works
NF-kB and Inflammatory Cytokine Signalling: Role in Skeletal Muscle Atrophy
Thoma, A., & Lightfoot, A. P. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_12 · Cited by 320 · see citing works
Stehle, G., Sinn, H., Wunder, A., Schrenk, H. H., Stewart, J. C. M., Hartung, G., Maier-Borst, W., & Heene, D. L. (1997) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(97)00015-2 · Cited by 305 · see citing works
Müller, S., Martin, S., Koenig, W., Hanifi-Moghaddam, P., Rathmann, W., Haastert, B., Giani, G., Illig, T., Thorand, B., & Kolb, H. (2002) · Diabetologia · doi:10.1007/s00125-002-0829-2 · Cited by 311 · see citing works
Buford, T. W., Anton, S. D., Judge, A. R., Marzetti, E., Wohlgemuth, S. E., Carter, C. S., Leeuwenburgh, C., Pahor, M., & Manini, T. M. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.04.004 · Cited by 295 · see citing works
Pro- versus anti-inflammatory cytokines: myth or reality.
Cavaillon, J. (2001) · PubMed · Cited by 301 · see citing works
Regeneration of skeletal muscle
Turner, N., & Badylak, S. (2011) · Cell and Tissue Research · doi:10.1007/s00441-011-1185-7 · Cited by 308 · see citing works
The syndrome of cardiac cachexia
Anker, S. D., & Sharma, R. (2002) · International Journal of Cardiology · doi:10.1016/s0167-5273(02)00233-4 · Cited by 292 · see citing works
Amirouche, A., Durieux, A., Banzet, S., Koulmann, N., Bonnefoy, R., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2008) · Endocrinology · doi:10.1210/en.2008-0959 · Cited by 282 · see citing works
Interleukin-6 and cachexia in ApcMin/+ mice.
Baltgalvis, K. A., Berger, F. G., Peña, M., Davis, J. M., Muga, S., & Carson, J. A. (2008) · American Journal of Physiology. Regulatory Integrative and Comparative Physiology · doi:10.1152/ajpregu.00716.2007 · Cited by 281 · see citing works
Inflammation induced loss of skeletal muscle
Londhe, P., & Guttridge, D. C. (2015) · Bone · doi:10.1016/j.bone.2015.03.015 · Cited by 276 · see citing works
The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
Murton, A. J., Constantin, D., & Greenhaff, P. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.011 · Cited by 265 · 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
“Transgenic mice over-expressing IL-6 have muscle atrophy associated with increased expression of lysosomal and ubiquitin-related mRNA and proteins [34,35].”
Muscle contractions induce interleukin‐6 mRNA production in rat skeletal muscles
Jonsdottir, I. H., Schjerling, P., Ostrowski, S. R., Asp, S., Richter, E. A., & Pedersen, B. K. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00157.x · Cited by 251 · see citing works
Bilski, J., Pierzchalski, P., Szczepanik, M., Bonior, J., & Zoladz, J. A. (2022) · Cells · doi:10.3390/cells11010160 · Cited by 262 · see citing works
Skeletal Muscle Wasting and Renewal: A Pivotal Role of Myokine IL-6
Belizário, J. E., Fontes-Oliveira, C. C., Borges, J. P., Kashiabara, J. A., & Vannier, E. (2016) · SpringerPlus · doi:10.1186/s40064-016-2197-2 · Cited by 244 · see citing works
Lysosomal proteolysis in skeletal muscle
Béchet, D., Tassa, A., Taillandier, D., Combaret, L., & Attaix, D. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.02.029 · Cited by 241 · see citing works
IL-6 and Serum Amyloid A Synergy Mediates Angiotensin II–Induced Muscle Wasting
Zhang, L., Du, J., Hu, Z., Han, G., Delafontaine, P., García, G., & Mitch, W. E. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008060628 · Cited by 241 · see citing works
Solerte, S. B., Gazzaruso, C., Bonacasa, R., Rondanelli, M., Zamboni, M., Basso, C., Locatelli, E., Schifino, N., Giustina, A., & Fioravanti, M. (2008) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2008.03.004 · Cited by 235 · see citing works
Role of Interleukin-6 in Mortality from and Physiologic Response to Sepsis
Remick, D. G., Bolgos, G. L., Copeland, S., & Siddiqui, J. (2005) · Infection and Immunity · doi:10.1128/iai.73.5.2751-2757.2005 · Cited by 230 · see citing works
Peripheral Muscle Wasting in Chronic Obstructive Pulmonary Disease
Debigaré, R., Côt́e, C. H., & Maltais, F. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.164.9.2104035 · Cited by 230 · see citing works
Silva, K. A. S., Dong, J., Dong, Y., Dong, Y., Schor, N., Tweardy, D. J., Zhang, L., & Mitch, W. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641514 · Cited by 229 · see citing works
Féasson, L., Stockholm, D., Freyssenet, D. G., Richard, I., Duguez, S., Beckmann, J. S., & Denis, C. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.018689 · Cited by 224 · see citing works
Rupert, J. E., Narasimhan, A., Jengelley, D. H. A., Jiang, Y., Liu, J., Au, E. D., Silverman, L. M., Sandusky, G. E., Bonetto, A., Cao, S., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20190450 · Cited by 221 · see citing works
Origins and Clinical Relevance of Sarcopenia
Roubenoff, R. (2001) · Canadian Journal of Applied Physiology · doi:10.1139/h01-006 · Cited by 219 · see citing works
White, J. P., Puppa, M. J., Sato, S., Gao, S., Price, R., Baynes, J., Kostek, M., Matesic, L., & Carson, J. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-14 · Cited by 217 · see citing works
Circulating Interleukin-6 in Severe Heart Failure
MacGowan, G. A., Mann, D. L., Kormos, R. L., Feldman, A. M., & Murali, S. (1997) · The American Journal of Cardiology · doi:10.1016/s0002-9149(96)00063-x · Cited by 214 · see citing works
Molecular Pathways Leading to Cancer Cachexia
Tisdale, M. J. (2005) · Physiology · doi:10.1152/physiol.00019.2005 · Cited by 213 · see citing works
Kaysen, G. A., Chertow, G. M., Adhikarla, R., Young, B. S., Ronco, C., & Levin, N. W. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.00804.x · Cited by 209 · see citing works
Interleukin-6 Causes Myocardial Failure and Skeletal Muscle Atrophy in Rats
Janssen, S. P. M., Gayan‐Ramirez, G., den Bergh, A. V., Herijgers, P., Maes, K., Verbeken, E. K., & Decramer, M. (2005) · Circulation · doi:10.1161/01.cir.0000156469.96135.0d · Cited by 208 · see citing works
Mortality, malnutrition, and atherosclerosis in ESRD: What is the role of interleukin-6?
Stenvinkel, P., Barany, P. F., Heimbürger, O., Pecoits‐Filho, R., & Lindholm, B. (2002) · Kidney International · doi:10.1046/j.1523-1755.61.s80.19.x · Cited by 208 · see citing works
Matthys, P., & Billiau, A. (1997) · Nutrition · doi:10.1016/s0899-9007(97)00185-8 · Cited by 201 · see citing works
Truncal fat mass as a contributor to inflammation in end-stage renal disease
Axelsson, J., Qureshi, A. R., Suliman, M. E., Honda, H., Pecoits‐Filho, R., Heimbürger, O., Lindholm, B., Cederholm, T., & Stenvinkel, P. (2004) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/80.5.1222 · Cited by 199 · see citing works
Bartoli, M., & Richard, I. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.12.012 · Cited by 198 · see citing works
Cancer anorexia-cachexia syndrome: cytokines and neuropeptides
Ramos, E. J., Suzuki, S., Marks, D. L., Inui, A., Asakawa, A., & Meguid, M. M. (2004) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000134363.53782.cb · Cited by 196 · see citing works
Stenvinkel, P., Heimbürger, O., & Jogestrand, T. (2002) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2002.30546 · Cited by 192 · see citing works
Kasembeli, M. M., Bharadwaj, U., Robinson, P., & Tweardy, D. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082299 · Cited by 199 · see citing works
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
Production of Interleukin-6 by Skeletal Myotubes
Kosmidou, I., Vassilakopoulos, T., Xagorari, A., Zakynthinos, S. G., Papapetropoulos, A., & Roussos, C. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.5.4598 · Cited by 182 · see citing works
The Role of Cytokines in Regulating Protein Metabolism and Muscle Function
Zoico, E., & Roubenoff, R. (2002) · Nutrition Reviews · doi:10.1301/00296640260085949 · Cited by 181 · see citing works
Inflammatory signals associated with hemodialysis
Çağlar, K., Peng, Y., Pupim, L. B., Flakoll, P. J., Levenhagen, D. K., Hakim, R. M., & Ikizler, T. A. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00556.x · Cited by 179 · see citing works
Benedetti, F. D., Meazza, C., Oliveri, M., Pignatti, P., Vivarelli, M., Alonzi, T., Fattori, E., Garrone, S., Barreca, A., & Martini, A. (2001) · Endocrinology · doi:10.1210/endo.142.11.8511 · Cited by 171 · see citing works
Bone Density, Body Composition, and Inflammatory Status in Cystic Fibrosis
Ionescu, A., Nixon, L. S., EVANS, W. D., STONE, M. D., LEWIS-JENKINS, V., Chatham, K., & Shale, D. J. (2000) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.162.3.9910118 · Cited by 170 · see citing works
The role of cytokines in the catabolic consequences of infection and injury.
Chang, H. R., & Bistrian, B. (1998) · JPEN - Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607198022003156 · Cited by 183 · see citing works
Elevation of cytokine levels in cachectic patients with prostate carcinoma
Pfitzenmaier, J., Vessella, R. L., Higano, C. S., Noteboom, J. L., Wallace, D., & Corey, E. (2003) · Cancer · doi:10.1002/cncr.11178 · Cited by 167 · see citing works
Association between inflammatory mediators and muscle mass in long-term hemodialysis patients
Kaizu, Y., Ohkawa, S., Odamaki, M., Ikegaya, N., Hibi, I., Miyaji, K., & Kumagai, H. (2003) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(03)00654-1 · Cited by 165 · see citing works
Ono, Y., Maejima, Y., Saito, M., Sakamoto, K., Horita, S., Shimomura, K., Inoue, S., & Kotani, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-57714-3 · Cited by 167 · 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
Catabolism in chronic heart failure
Berry, C. (2000) · European Heart Journal · doi:10.1053/euhj.1999.1882 · Cited by 159 · see citing works
N UTRITIONAL M ANAGEMENT OF M AINTENANCE D IALYSIS P ATIENTS : Why Aren't We Doing Better?
Mehrotra, R., & Kopple, J. D. (2001) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.21.1.343 · Cited by 158 · see citing works
Interleukin-6 may mediate malnutrition in chronic hemodialysis patients
Kaizu, Y., Kimura, M., Yoneyama, T., Miyaji, K., Hibi, I., & Kumagai, H. (1998) · American Journal of Kidney Diseases · doi:10.1053/ajkd.1998.v31.pm9428458 · Cited by 158 · see citing works
Inflammation Based Regulation of Cancer Cachexia
Onesti, J. K., & D, D. C. G. (2014) · BioMed Research International · doi:10.1155/2014/168407 · Cited by 157 · see citing works
Interleukin-6: A Novel Target for Cardio-Cerebrovascular Diseases
Su, J.-H., Luo, M.-Y., Liang, N., Gong, S.-X., Chen, W., Huang, W., Tian, Y., & Wang, A. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.745061 · Cited by 160 · see citing works
Simons, J., Schols, A. M. W. J., Buurman, W. A., & Wouters, E. F. �. (1999) · Clinical Science · doi:10.1042/cs0970215 · Cited by 156 · see citing works
Moran, M. T., Schofield, J. P., Hayman, A. R., Shi, G., Young, E. P., & Cox, T. M. (2000) · Blood · doi:10.1182/blood.v96.5.1969 · Cited by 153 · see citing works
Hamada, K., Vannier, E. G., Sacheck, J. M., Witsell, A. L., & Roubenoff, R. (2004) · The FASEB Journal · doi:10.1096/fj.03-1286fje · Cited by 149 · see citing works
Exercise Training as a Treatment for Chronic Inflammation in the Elderly
Nicklas, B. J., & Brinkley, T. E. (2009) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3181b7b3d9 · Cited by 148 · see citing works
Stenvinkel, P. (2000) · Blood Purification · doi:10.1159/000046932 · Cited by 147 · see citing works
The JAK/STAT Pathway in Skeletal Muscle Pathophysiology
Moresi, V., Adamo, S., & Berghella, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00500 · Cited by 141 · see citing works
Yoshida, T., Tabony, A. M., Galvez, S., Mitch, W. E., Higashi, Y., Sukhanov, S., & Delafontaine, P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.035 · Cited by 142 · see citing works
Keller, G., Grimm, V., Vogelsang, H., Bischoff, P., Mueller, J., Siewert, J. R., & Höfler, H. (1996) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19961127)68:5 · Cited by 76 · see citing works
Self-citationERK2 is required for efficient terminal differentiation of skeletal myoblasts
Li, J., & Johnson, S. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.051 · Cited by 137 · see citing works
Calpain 3: a key regulator of the sarcomere?
Duguez, S., Bartoli, M., & Richard, I. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05351.x · Cited by 137 · see citing works
Transcriptional pathways associated with skeletal muscle disuse atrophy in humans
Chen, Y., Gregory, C. M., Scarborough, M. T., Shi, R., Walter, G. A., & Vandenborne, K. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00115.2006 · Cited by 134 · see citing works
Katsume, A., Saito, H., Yamada, Y., Yorozu, K., Ueda, O., Akamatsu, K.-I., Nishimoto, N., Kishimoto, T., Yoshizaki, K., & Ohsugi, Y. (2002) · Cytokine · doi:10.1006/cyto.2002.2012 · Cited by 134 · see citing works
Self-citationBouchard, J. J., Truong, J. K., Bouchard, K. E., Dunkelberger, D. L., Desrayaud, S., Moussaoui, S. M., Tabrizi, S. J., Stella, N., & Muchowski, P. J. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4008-12.2012 · Cited by 133 · see citing works
Genetic Influences in Sport and Physical Performance
Puthucheary, Z., Skipworth, J. R. A., Rawal, J., Loosemore, M., van Someren, K. A., & Montgomery, H. (2011) · Sports Medicine · doi:10.2165/11593200-000000000-00000 · Cited by 129 · see citing works
Anker, S. D., Steinborn, W., & Strassburg, S. (2004) · Annals of Medicine · doi:10.1080/07853890410017467 · Cited by 129 · see citing works
Adipose tissue and its relation to inflammation: The role of adipokines
Axelsson, J., Heimbürger, O., Lindholm, B., & Stenvinkel, P. (2005) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2004.09.034 · Cited by 127 · see citing works
Muscle wasting and interleukin-6-induced atrogin-I expression in the cachectic Apc Min/+ mouse
Baltgalvis, K. A., Berger, F. G., Peña, M. M. O., Davis, J. M., White, J. P., & Carson, J. A. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-008-0574-6 · Cited by 125 · see citing works
Siddiqui, J. A., Pothuraju, R., Jain, M., Batra, S. K., & Nasser, M. W. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188359 · Cited by 123 · see citing works
Arthur, S. T., & Cooley, I. D. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4262 · Cited by 119 · see citing works
A Perspective on Immunomodulation and Tissue Repair
Mokarram, N., & Bellamkonda, R. V. (2013) · Annals of Biomedical Engineering · doi:10.1007/s10439-013-0941-0 · Cited by 114 · see citing works
van Hall, G., Steensberg, A., Fischer, C., Keller, C., Møller, K., Moseley, P., & Pedersen, B. (2008) · Journal of Clinical Endocrinology and Metabolism · doi:10.1210/jc.2007-2223 · Cited by 116 · see citing works
Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.
Attaix, D., Aurousseau, E., Combaret, L., Kee, A., Larbaud, D., Rallière, C., Souweine, B., Taillandier, D., & Tilignac, T. (1998) · Reproduction Nutrition Development · doi:10.1051/rnd:19980202 · Cited by 109 · see citing works
- Authors
- Tsujinaka, T., Fujita, J., Ebisui, C., Yano, M., Kominami, E., Suzuki, K., Tanaka, K., Katsume, A., Ohsugi, Y., Shiozaki, H., & Monden, M.
- Affiliations
- Osaka University Hospital (JP)
- The University of Osaka (JP)
- Juntendo University (JP)
- Institute for Quantitative Biosciences, The University of Tokyo (JP)
- Chugai Pharmaceutical Co., Ltd. (Japan) (JP)
- Venue
- Journal of Clinical Investigation
- Published
- 1996-01-01
- Volume
- 97
- Issue
- 1
- Pages
- 244-249
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC507086
- OpenAlex
- W2060757943
- Cited by
- 421
- References
- 57
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 16 · 2023: 10 · 2022: 22 · 2021: 16 · 2020: 13 · 2019: 9 · 2018: 14 · 2017: 11 · 2016: 9 · 2015: 17 · 2014: 9 · 2013: 14 · 2012: 18
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- interleukin-6, IL-6 receptor antibody, muscle atrophy, proteolytic system, cathepsin B, cathepsin L, ubiquitin, CAPN3, gastrocnemius, cancer cachexia, sepsis
- MeSH terms
- Animals, Antibodies, Monoclonal, Body Weight, Calpain, Cathepsin B, Cathepsins, Cysteine Endopeptidases, Humans, Mice, Inbred C57BL, Mice, Transgenic, Multienzyme Complexes, Muscular Atrophy, Organ Size, Endopeptidases, RNA, Messenger, Ubiquitins, Antigens, CD, Interleukin-6, Gene Expression, Rats, Wistar, Receptors, Interleukin, Muscle, Skeletal, Receptors, Interleukin-6, Proteasome Endopeptidase Complex, Mice, Rats, Cathepsin L
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
