메뉴 건너뛰기




Volumn 170, Issue , 2017, Pages 56-63

TNF-α and cancer cachexia: Molecular insights and clinical implications

Author keywords

Acute phase response; Cancer cachexia; Metabolic abnormalities; Skeletal muscle wasting; Tumor necrosis factor alpha (TNF )

Indexed keywords

GLYCOGEN; INSULIN; INTERLEUKIN 1; LIPID; TUMOR NECROSIS FACTOR; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 3; CARBOHYDRATE; INTERLEUKIN 6; PROTEASOME; UBIQUITIN; UCP2 PROTEIN, HUMAN; UCP3 PROTEIN, HUMAN;

EID: 85008601729     PISSN: 00243205     EISSN: 18790631     Source Type: Journal    
DOI: 10.1016/j.lfs.2016.11.033     Document Type: Review
Times cited : (256)

References (101)
  • 1
    • 79955399340 scopus 로고    scopus 로고
    • Definition and classification of cancer cachexia: an international consensus
    • [1] Fearon, K., Strasser, F., Anker, S.D., et al. Definition and classification of cancer cachexia: an international consensus. Oncology 12 (2011), 489–495.
    • (2011) Oncology , vol.12 , pp. 489-495
    • Fearon, K.1    Strasser, F.2    Anker, S.D.3
  • 3
    • 34447541405 scopus 로고    scopus 로고
    • Pathophysiology of cancer cachexia: much more than host-tumour interaction?
    • [3] Skipworth, R.J., Stewart, G.D., Dejong, C.H., et al. Pathophysiology of cancer cachexia: much more than host-tumour interaction?. Clin. Nutr. 26 (2007), 667–676.
    • (2007) Clin. Nutr. , vol.26 , pp. 667-676
    • Skipworth, R.J.1    Stewart, G.D.2    Dejong, C.H.3
  • 4
    • 0027441379 scopus 로고
    • Humoral mediation for cachexia in tumor bearing rats
    • [4] Tessitore, L., Costelli, P., Baccino, F.M., Humoral mediation for cachexia in tumor bearing rats. Br. J. Cancer 67 (1993), 15–23.
    • (1993) Br. J. Cancer , vol.67 , pp. 15-23
    • Tessitore, L.1    Costelli, P.2    Baccino, F.M.3
  • 6
    • 84905434882 scopus 로고    scopus 로고
    • Molecular targets of cancer cachexia: opportunities for pharma nutritional approaches
    • [6] Sharma, M., Kambadur, R., Sriram, S., et al. Molecular targets of cancer cachexia: opportunities for pharma nutritional approaches. Pharma. Nutrition 2 (2014), 126–128.
    • (2014) Pharma. Nutrition , vol.2 , pp. 126-128
    • Sharma, M.1    Kambadur, R.2    Sriram, S.3
  • 7
    • 85008682523 scopus 로고    scopus 로고
    • The role of tumor necrosis factor- α in muscle wasting disorders
    • [7] Argiles, J.M., Martinez, C.G., Llovera, M., et al. The role of tumor necrosis factor- α in muscle wasting disorders. Basic Appl. Myol. 8 (1998), 371–380.
    • (1998) Basic Appl. Myol. , vol.8 , pp. 371-380
    • Argiles, J.M.1    Martinez, C.G.2    Llovera, M.3
  • 8
    • 0034254453 scopus 로고    scopus 로고
    • TNF- alpha and the TNF receptor superfamily: structure – unction relationship(s)
    • [8] Idriss, H.T., Naismith, J.H., TNF- alpha and the TNF receptor superfamily: structure – unction relationship(s). Microsc. Res. Tech. 50 (2000), 184–195.
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 184-195
    • Idriss, H.T.1    Naismith, J.H.2
  • 9
    • 0026703322 scopus 로고
    • The role of cytokines in muscle wasting: its relation with cancer cachexia
    • [9] Argilés, J.M., García-Martínez, C., Llovera, M., et al. The role of cytokines in muscle wasting: its relation with cancer cachexia. Med. Res. Rev. 12 (1992), 637–652.
    • (1992) Med. Res. Rev. , vol.12 , pp. 637-652
    • Argilés, J.M.1    García-Martínez, C.2    Llovera, M.3
  • 12
    • 14644404350 scopus 로고    scopus 로고
    • Molecular mechanisms involved in muscle wasting in cancer and ageing: cachexia versus sarcopenia
    • [12] Argiles, J.M., Busquets, S., Felipe, A., et al. Molecular mechanisms involved in muscle wasting in cancer and ageing: cachexia versus sarcopenia. Int. J. Biochem. Cell Biol. 37 (2005), 1084–1104.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 1084-1104
    • Argiles, J.M.1    Busquets, S.2    Felipe, A.3
  • 13
    • 33845265094 scopus 로고    scopus 로고
    • Elevated tumor IL-1 beta is associated with systemic inflammation: a marker of reduced survival in gastro-oesophageal cancer
    • [13] Deans, D.A., Wigmore, S.J., Gilmour, H., et al. Elevated tumor IL-1 beta is associated with systemic inflammation: a marker of reduced survival in gastro-oesophageal cancer. Br. J. Cancer 95 (2006), 1568–1575.
    • (2006) Br. J. Cancer , vol.95 , pp. 1568-1575
    • Deans, D.A.1    Wigmore, S.J.2    Gilmour, H.3
  • 14
    • 0030063921 scopus 로고    scopus 로고
    • Characterization of a cancer cachectic factor
    • [14] Todorov, P., Cariuk, P., McDevitt, T., et al. Characterization of a cancer cachectic factor. Nature 379 (1996), 739–742.
    • (1996) Nature , vol.379 , pp. 739-742
    • Todorov, P.1    Cariuk, P.2    McDevitt, T.3
  • 15
    • 0025775486 scopus 로고
    • Tumor necrosis factor – alpha and anorexia- cause or effect?
    • [15] Vaisman, N., Hahn, T., Tumor necrosis factor – alpha and anorexia- cause or effect?. Metabolism 40 (1991), 720–723.
    • (1991) Metabolism , vol.40 , pp. 720-723
    • Vaisman, N.1    Hahn, T.2
  • 16
    • 0023749977 scopus 로고
    • Cachectin/tumor necrosis factor, a possible mediator of cancer anorexia in the rat
    • [16] Stovroff, M.C., Fraker, D.L., Swedenborg, J.A., et al. Cachectin/tumor necrosis factor, a possible mediator of cancer anorexia in the rat. Cancer Res. 48 (1988), 4567–4572.
    • (1988) Cancer Res. , vol.48 , pp. 4567-4572
    • Stovroff, M.C.1    Fraker, D.L.2    Swedenborg, J.A.3
  • 17
    • 84856906459 scopus 로고    scopus 로고
    • The cachexia score (CASCO): a new tool for staging cachectic cancer patients
    • [17] Argiles, J.M., Lopez-Soriano, F.J., Toledo, M., et al. The cachexia score (CASCO): a new tool for staging cachectic cancer patients. J. Cachex. Sarcopenia Muscle 2 (2011), 87–93.
    • (2011) J. Cachex. Sarcopenia Muscle , vol.2 , pp. 87-93
    • Argiles, J.M.1    Lopez-Soriano, F.J.2    Toledo, M.3
  • 19
    • 0026801425 scopus 로고
    • Weight loss in a murine cachexia model is not associated with the cytokines tumor necrosis factor- α or interleukin-6
    • [19] Mulligan, H.D., Mahony, S.M., Ross, J.A., et al. Weight loss in a murine cachexia model is not associated with the cytokines tumor necrosis factor- α or interleukin-6. Cancer Lett. 65 (1992), 239–243.
    • (1992) Cancer Lett. , vol.65 , pp. 239-243
    • Mulligan, H.D.1    Mahony, S.M.2    Ross, J.A.3
  • 20
    • 0023638415 scopus 로고
    • Tumors secreting human TNF/cachectin induce cachexia in mice
    • [20] Oliff, A., Defeo-Jones, D., Boyer, M., et al. Tumors secreting human TNF/cachectin induce cachexia in mice. Cell 50 (1987), 555–563.
    • (1987) Cell , vol.50 , pp. 555-563
    • Oliff, A.1    Defeo-Jones, D.2    Boyer, M.3
  • 21
    • 0027331364 scopus 로고
    • Tumour necrosis factor-α mediates changes in muscle protein turnover in a cachectic rat tumour model
    • [21] Costelli, P., Carbó, N., Tessitore, L., et al. Tumour necrosis factor-α mediates changes in muscle protein turnover in a cachectic rat tumour model. J. Clin. Invest. 92 (1993), 2783–2789.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2783-2789
    • Costelli, P.1    Carbó, N.2    Tessitore, L.3
  • 22
    • 67650337580 scopus 로고    scopus 로고
    • Cancer cachexia-anorexia syndrome and skeletal muscle wasting
    • [22] Jurdana, M., Cancer cachexia-anorexia syndrome and skeletal muscle wasting. Radiol. Oncol. 43 (2009), 65–75.
    • (2009) Radiol. Oncol. , vol.43 , pp. 65-75
    • Jurdana, M.1
  • 23
    • 0036584738 scopus 로고    scopus 로고
    • Hypercatabolism and hypermetabolism in wasting states
    • [23] Baracos, V.E., Hypercatabolism and hypermetabolism in wasting states. Curr. Opin. Clin. Nutr. Metab. Care 5 (2002), 237–239.
    • (2002) Curr. Opin. Clin. Nutr. Metab. Care , vol.5 , pp. 237-239
    • Baracos, V.E.1
  • 24
    • 33845468960 scopus 로고    scopus 로고
    • Body composition changes in cancer cachexia: are they reversible?
    • [24] Winkler, M.F., Body composition changes in cancer cachexia: are they reversible?. Top. Clin. Nutr. 19 (2004), 85–94.
    • (2004) Top. Clin. Nutr. , vol.19 , pp. 85-94
    • Winkler, M.F.1
  • 25
    • 84879228968 scopus 로고    scopus 로고
    • Cancer cachexia prevention via physical exercise: molecular mechanisms
    • [25] Gould, D.W., Lahart, I., Carmichael, A.R., et al. Cancer cachexia prevention via physical exercise: molecular mechanisms. J. Cachex. Sarcopenia Muscle 4 (2013), 111–124.
    • (2013) J. Cachex. Sarcopenia Muscle , vol.4 , pp. 111-124
    • Gould, D.W.1    Lahart, I.2    Carmichael, A.R.3
  • 26
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygen mediated NF-κB activation in response to tumor necrosis factor α
    • [26] Li, Y.-P., Schwartz, R.J., Waddell, I.D., et al. Skeletal muscle myocytes undergo protein loss and reactive oxygen mediated NF-κB activation in response to tumor necrosis factor α. FASEB J. 12 (1998), 871–880.
    • (1998) FASEB J. , vol.12 , pp. 871-880
    • Li, Y.-P.1    Schwartz, R.J.2    Waddell, I.D.3
  • 27
    • 0033696398 scopus 로고    scopus 로고
    • NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes
    • [27] Li, Y.-P., Reid, M.B., NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes. Am. J. Phys. Regul. Integr. Comp. Phys., 279, 2000, R1165-R70.
    • (2000) Am. J. Phys. Regul. Integr. Comp. Phys. , vol.279 , pp. R1165-R70
    • Li, Y.-P.1    Reid, M.B.2
  • 28
    • 0027372066 scopus 로고
    • Acute treatment with tumour necrosis factor- α induces changes in protein metabolism in rat skeletal muscle
    • [28] Garcia-Martinez, C., Lopez-Soriano, F.J., Argiles, J.M., Acute treatment with tumour necrosis factor- α induces changes in protein metabolism in rat skeletal muscle. Mol. Cell. Biochem. 125 (1993), 11–18.
    • (1993) Mol. Cell. Biochem. , vol.125 , pp. 11-18
    • Garcia-Martinez, C.1    Lopez-Soriano, F.J.2    Argiles, J.M.3
  • 29
    • 0000498853 scopus 로고
    • Cachectin/TNF or IL-1 α induces cachexia with redistribution of body proteins
    • [29] Fong, Y., Moldawer, L.L., Morano, M., et al. Cachectin/TNF or IL-1 α induces cachexia with redistribution of body proteins. Am. J. Phys., 256, 1989, R659-R65.
    • (1989) Am. J. Phys. , vol.256 , pp. R659-R65
    • Fong, Y.1    Moldawer, L.L.2    Morano, M.3
  • 30
    • 0032516677 scopus 로고    scopus 로고
    • Protein turnover in skeletal muscle of tumour-bearing transgenic mice overexpressing the soluble TNF receptor-1
    • [30] Llovera, M., Garcia-Martinez, C., Lopez-Soriano, J., et al. Protein turnover in skeletal muscle of tumour-bearing transgenic mice overexpressing the soluble TNF receptor-1. Cancer Lett. 130 (1998), 19–27.
    • (1998) Cancer Lett. , vol.130 , pp. 19-27
    • Llovera, M.1    Garcia-Martinez, C.2    Lopez-Soriano, J.3
  • 31
    • 0027266801 scopus 로고
    • Tumour necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins
    • [31] Garcia-Martinez, C., Agell, N., Llovera, M., et al. Tumour necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins. FEBS Lett. 323 (1993), 211–214.
    • (1993) FEBS Lett. , vol.323 , pp. 211-214
    • Garcia-Martinez, C.1    Agell, N.2    Llovera, M.3
  • 32
    • 0029597841 scopus 로고
    • Ubiquitin gene expession in skeletal muscle is increased during sepsis: involvement of TNF-α but not IL-1
    • [32] Garcia-Martinez, C., Llovera, M., Agell, N., et al. Ubiquitin gene expession in skeletal muscle is increased during sepsis: involvement of TNF-α but not IL-1. Biochem. Biophys. Res. Commun. 217 (1995), 839–844.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 839-844
    • Garcia-Martinez, C.1    Llovera, M.2    Agell, N.3
  • 33
    • 0031566181 scopus 로고    scopus 로고
    • TNF can directly induce the expression of ubiquitin-dependent proteolytic system in rat soleus muscles
    • [33] Llovera, M., Garcia-Martinez, C., Lopez-Soriano, F.J., et al. TNF can directly induce the expression of ubiquitin-dependent proteolytic system in rat soleus muscles. Biochem. Biophys. Res. Commun. 230 (1997), 238–241.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 238-241
    • Llovera, M.1    Garcia-Martinez, C.2    Lopez-Soriano, F.J.3
  • 34
    • 0035722694 scopus 로고    scopus 로고
    • Tumor necrosis factor- α and muscle wasting: a cellular perspective
    • [34] Reid, M.B., Li, Y.P., Tumor necrosis factor- α and muscle wasting: a cellular perspective. Respir. Res. 2 (2001), 269–272.
    • (2001) Respir. Res. , vol.2 , pp. 269-272
    • Reid, M.B.1    Li, Y.P.2
  • 35
    • 0033086243 scopus 로고    scopus 로고
    • Mitochondria mediate tumor necrosis factor- α/NF-kB signaling in skeletal muscle myotubes
    • [35] Li, Y.-P., Atkins, C.M., Sweatt, J.D., et al. Mitochondria mediate tumor necrosis factor- α/NF-kB signaling in skeletal muscle myotubes. Antioxid. Redox Signal. 1 (1999), 97–104.
    • (1999) Antioxid. Redox Signal. , vol.1 , pp. 97-104
    • Li, Y.-P.1    Atkins, C.M.2    Sweatt, J.D.3
  • 36
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kB activation in response to tumor necrosis factor- α
    • [36] Li, Y.-P., Schwartz, R.J., Waddell, I.D., et al. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kB activation in response to tumor necrosis factor- α. FASEB J. 12 (1998), 871–880.
    • (1998) FASEB J. , vol.12 , pp. 871-880
    • Li, Y.-P.1    Schwartz, R.J.2    Waddell, I.D.3
  • 37
    • 0032588186 scopus 로고    scopus 로고
    • NF-kB controls cell growth and differentiation through transcriptional regulation of cyclin D1
    • [37] Guttridge, D.C., Albenese, C., Reuther, J.Y., et al. NF-kB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol. Cell. Biol. 19 (1999), 5785–5799.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1    Albenese, C.2    Reuther, J.Y.3
  • 38
    • 0031589552 scopus 로고    scopus 로고
    • Glutathione regulation of tumour necrosis factor a-induced NF-kB activation in skeletal muscle L6 cells
    • [38] Sen, C.K., Khanna, S., Resznick, A.Z., et al. Glutathione regulation of tumour necrosis factor a-induced NF-kB activation in skeletal muscle L6 cells. Biochem. Biophys. Res. Commun. 237 (1997), 645–649.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 645-649
    • Sen, C.K.1    Khanna, S.2    Resznick, A.Z.3
  • 39
    • 0032491701 scopus 로고    scopus 로고
    • Late side-effects are common after treatment of Hodgkin's disease. Muscular atrophy following radiotherapy is a neglected risk
    • [39] Johansson, A.S., Erlanson, M., Lenner, P., et al. Late side-effects are common after treatment of Hodgkin's disease. Muscular atrophy following radiotherapy is a neglected risk. Lakartidningen 95 (1998), 44–47.
    • (1998) Lakartidningen , vol.95 , pp. 44-47
    • Johansson, A.S.1    Erlanson, M.2    Lenner, P.3
  • 40
    • 0033696398 scopus 로고    scopus 로고
    • NF-kB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes
    • [40] Li, Y.-P., Reid, M.B., NF-kB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes. Am. J. Phys. Regul. Integr. Comp. Phys., 279, 2000, R1165-R70.
    • (2000) Am. J. Phys. Regul. Integr. Comp. Phys. , vol.279 , pp. R1165-R70
    • Li, Y.-P.1    Reid, M.B.2
  • 41
    • 0041319376 scopus 로고    scopus 로고
    • Skeletal muscle metabolism in physiology and in cancer disease
    • [41] Giordano, A., Calvani, M., Petillo, O., et al. Skeletal muscle metabolism in physiology and in cancer disease. J. Cell. Biochem. 90 (2003), 170–186.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 170-186
    • Giordano, A.1    Calvani, M.2    Petillo, O.3
  • 42
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin–proteasome proteolytic pathway: destruction for the sake of construction
    • [42] Glickman, M.H., Ciechanover, A., The ubiquitin–proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002), 373–428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 43
    • 0032514735 scopus 로고    scopus 로고
    • Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway
    • [43] Solomon, V., Baracos, V., Sarraf, P., et al. Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway. Proc. Natl. Acad. Sci. U. S. A. 95 (1998), 12602–12607.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12602-12607
    • Solomon, V.1    Baracos, V.2    Sarraf, P.3
  • 44
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • [44] Bodine, S.C., Latres, E., Baumhueter, S., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294 (2001), 1704–1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 45
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • [45] Lecker, S.H., Jagoe, R.T., Gilbert, A., et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J. 18 (2004), 39–51.
    • (2004) FASEB J. , vol.18 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3
  • 46
    • 37649000622 scopus 로고    scopus 로고
    • Ubiquitin ligases MuRF1 and MAFbx in human skeletal muscle atrophy
    • [46] de Palma, L., Marinelli, M., Pavan, M., et al. Ubiquitin ligases MuRF1 and MAFbx in human skeletal muscle atrophy. Joint Bone Spine 75 (2007), 53–57.
    • (2007) Joint Bone Spine , vol.75 , pp. 53-57
    • de Palma, L.1    Marinelli, M.2    Pavan, M.3
  • 47
    • 0034685026 scopus 로고    scopus 로고
    • The gene expression of ubiquitin ligase E3α is upregulated in skeletal muscle during sepsis in rats—potential role of glucocorticoids
    • [47] Fischer, D., The gene expression of ubiquitin ligase E3α is upregulated in skeletal muscle during sepsis in rats—potential role of glucocorticoids. Biochem. Biophys. Res. Commun. 267 (2000), 504–508.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 504-508
    • Fischer, D.1
  • 48
    • 85047694453 scopus 로고    scopus 로고
    • Increased muscle proteasome activity correlates with disease severity in gastric cancer patients
    • [48] Bossola, M., Muscaritoli, M., Costelli, P., et al. Increased muscle proteasome activity correlates with disease severity in gastric cancer patients. Ann. Surg. 237 (2003), 384–389.
    • (2003) Ann. Surg. , vol.237 , pp. 384-389
    • Bossola, M.1    Muscaritoli, M.2    Costelli, P.3
  • 49
    • 27144505161 scopus 로고    scopus 로고
    • Expression of the ubiquitin–proteasome pathway and muscle loss in experimental cancer cachexia
    • [49] Khal, J., Wyke, S.M., Russell, S.T., et al. Expression of the ubiquitin–proteasome pathway and muscle loss in experimental cancer cachexia. Br. J. Cancer 93 (2005), 774–780.
    • (2005) Br. J. Cancer , vol.93 , pp. 774-780
    • Khal, J.1    Wyke, S.M.2    Russell, S.T.3
  • 50
    • 23944494119 scopus 로고    scopus 로고
    • Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss
    • [50] Khal, J., Hine, A.V., Fearon, K.C.H., et al. Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss. Int. J. Biochem. Cell Biol. 37 (2005), 2196–2206.
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 2196-2206
    • Khal, J.1    Hine, A.V.2    Fearon, K.C.H.3
  • 51
    • 14944352786 scopus 로고    scopus 로고
    • NF-kappaB mediates proteolysis inducing factor induced protein degradation and expression of the ubiquitin–proteasome system in skeletal muscle
    • [51] Wyke, S.M., Tisdale, M.J., NF-kappaB mediates proteolysis inducing factor induced protein degradation and expression of the ubiquitin–proteasome system in skeletal muscle. Br. J. Cancer 92 (2005), 711–721.
    • (2005) Br. J. Cancer , vol.92 , pp. 711-721
    • Wyke, S.M.1    Tisdale, M.J.2
  • 53
    • 0035164533 scopus 로고    scopus 로고
    • Muscle cachexia: current concepts of intracellular mechanisms and molecular regulation
    • [53] Hasselgren, P.O., Fischer, J.E., Muscle cachexia: current concepts of intracellular mechanisms and molecular regulation. Ann. Surg. 233 (2001), 9–17.
    • (2001) Ann. Surg. , vol.233 , pp. 9-17
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 54
    • 0030665384 scopus 로고    scopus 로고
    • Biology of cachexia
    • [54] Tisdale, M.J., Biology of cachexia. J. Natl. Cancer Inst. 89 (1997), 1763–1773.
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1763-1773
    • Tisdale, M.J.1
  • 55
    • 85026136040 scopus 로고    scopus 로고
    • The biochemical basis of metabolism in cancer cachexia
    • [55] Tijerina, A.J., The biochemical basis of metabolism in cancer cachexia. Dimens. Crit. Care Nurs. 23 (2004), 237–243.
    • (2004) Dimens. Crit. Care Nurs. , vol.23 , pp. 237-243
    • Tijerina, A.J.1
  • 56
    • 85008644755 scopus 로고    scopus 로고
    • (2002) Tumor necrosis factor-alpha exerts interleukin-6-dependent and -independent effects on cultured skeletal muscle cells. Biochim. Biophys. Acta 1542, 66–72Tisdale MJ. Metabolic abnormalities in Cachexia and Anorexia
    • [56] Alvarez, B., Quinn, L.S., Busquets, S., Quiles, M.T., Lopez-Soriano, F.J., Argiles, J.M., (2002) Tumor necrosis factor-alpha exerts interleukin-6-dependent and -independent effects on cultured skeletal muscle cells. Biochim. Biophys. Acta 1542, 66–72Tisdale MJ. Metabolic abnormalities in Cachexia and Anorexia. Nutrition 16 (2000), 1013–1014.
    • (2000) Nutrition , vol.16 , pp. 1013-1014
    • Alvarez, B.1    Quinn, L.S.2    Busquets, S.3    Quiles, M.T.4    Lopez-Soriano, F.J.5    Argiles, J.M.6
  • 57
  • 59
    • 84938830218 scopus 로고    scopus 로고
    • Evidence and mechanisms of fat depletion in cancer
    • [59] Ebadi, M., Mazurak, V.C., Evidence and mechanisms of fat depletion in cancer. Nutrients 6 (2014), 5280–5297.
    • (2014) Nutrients , vol.6 , pp. 5280-5297
    • Ebadi, M.1    Mazurak, V.C.2
  • 60
    • 0034235124 scopus 로고    scopus 로고
    • Lipolysis and lipid oxidation in weight-losing cancer patients and healthy subjects
    • [60] Zuijdgeest-van Leeuwen, S.D., van den Berg, J.W., Wattimena, J.L., et al. Lipolysis and lipid oxidation in weight-losing cancer patients and healthy subjects. Metabolism 49 (2000), 931–936.
    • (2000) Metabolism , vol.49 , pp. 931-936
    • Zuijdgeest-van Leeuwen, S.D.1    van den Berg, J.W.2    Wattimena, J.L.3
  • 61
    • 33846621473 scopus 로고    scopus 로고
    • Fat loss in cachexia—is there a role for adipocyte lipolysis?
    • [61] Ryden, M., Arner, P., Fat loss in cachexia—is there a role for adipocyte lipolysis?. Clin. Nutr. 26 (2007), 1–6.
    • (2007) Clin. Nutr. , vol.26 , pp. 1-6
    • Ryden, M.1    Arner, P.2
  • 62
    • 84155165679 scopus 로고    scopus 로고
    • Adipose tissue inflammation and cancer cachexia: possible role of nuclear transcription factors
    • [62] Batista, M.L. Jr., Peres, S.B., McDonald, M.E., et al. Adipose tissue inflammation and cancer cachexia: possible role of nuclear transcription factors. Cytokine 57 (2012), 9–16.
    • (2012) Cytokine , vol.57 , pp. 9-16
    • Batista, M.L.1    Peres, S.B.2    McDonald, M.E.3
  • 63
    • 84864646651 scopus 로고    scopus 로고
    • Cancer cachexia: mediators, signaling and metabolic pathways
    • [63] Fearon, K., Glass, D.J., Guttridge, D.C., Cancer cachexia: mediators, signaling and metabolic pathways. Cell Metab. 16 (2012), 153–166.
    • (2012) Cell Metab. , vol.16 , pp. 153-166
    • Fearon, K.1    Glass, D.J.2    Guttridge, D.C.3
  • 64
    • 8844226709 scopus 로고    scopus 로고
    • Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase
    • [64] Zimmermann, R., Strauss, J.G., Haemmerle, G., et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science 306 (2004), 1383–1386.
    • (2004) Science , vol.306 , pp. 1383-1386
    • Zimmermann, R.1    Strauss, J.G.2    Haemmerle, G.3
  • 65
    • 0033073540 scopus 로고    scopus 로고
    • The role of TNF alpha in adipocyte metabolism
    • [65] Sethi, J.K., Hotamisligil, G.S., The role of TNF alpha in adipocyte metabolism. Semin. Cell Dev. Biol. 10 (1999), 19–29.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 19-29
    • Sethi, J.K.1    Hotamisligil, G.S.2
  • 66
    • 0022861271 scopus 로고
    • Regulation of lipoprotein lipase synthesis by recombinant tumor necrosis factor: the primary regulatory role of the hormone in 3T3-L1 adipocytes
    • [66] Price, S.R., Olivecrona, T., Pekala, P.H., Regulation of lipoprotein lipase synthesis by recombinant tumor necrosis factor: the primary regulatory role of the hormone in 3T3-L1 adipocytes. Arch. Biochem. Biophys. 251 (1986), 738–746.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 738-746
    • Price, S.R.1    Olivecrona, T.2    Pekala, P.H.3
  • 67
    • 0023871823 scopus 로고
    • Regulation of lipoprotein lipase mRNA content in 3T3-L1 cells by tumour necrosis factor
    • [67] Cornelius, P., Enerback, S., Bjursell, G., et al. Regulation of lipoprotein lipase mRNA content in 3T3-L1 cells by tumour necrosis factor. Biochem. J. 249 (1988), 765–769.
    • (1988) Biochem. J. , vol.249 , pp. 765-769
    • Cornelius, P.1    Enerback, S.2    Bjursell, G.3
  • 68
    • 0024836241 scopus 로고
    • Cachectin/tumor necrosis factor decreases human adipose tissue lipoprotein lipase mRNA levels, synthesis, and activity
    • [68] Fried, S.K., Zechner, R., Cachectin/tumor necrosis factor decreases human adipose tissue lipoprotein lipase mRNA levels, synthesis, and activity. J. Lipid Res. 30 (1989), 1917–1923.
    • (1989) J. Lipid Res. , vol.30 , pp. 1917-1923
    • Fried, S.K.1    Zechner, R.2
  • 69
    • 0023129921 scopus 로고
    • Human recombinant TNF suppresses lipoprotein lipase activity and stimulates lipolysis in 3T3-L1 cells
    • [69] Kawakami, M., Murase, T., Ogawa, H., et al. Human recombinant TNF suppresses lipoprotein lipase activity and stimulates lipolysis in 3T3-L1 cells. J. Biochem. 101 (1987), 331–338.
    • (1987) J. Biochem. , vol.101 , pp. 331-338
    • Kawakami, M.1    Murase, T.2    Ogawa, H.3
  • 70
    • 85008644760 scopus 로고    scopus 로고
    • Tumor necrosis factor- alpha suppresses adipocytes- specific genes and activates expression of preadipocyte genes in 3T3-L1 adipocytes: nuclear factor- kappa B activation by TNF- alpha is obligatory
    • [70] Ruan, H., Hacohen, N., Golub, T.R., et al. Tumor necrosis factor- alpha suppresses adipocytes- specific genes and activates expression of preadipocyte genes in 3T3-L1 adipocytes: nuclear factor- kappa B activation by TNF- alpha is obligatory. Diabetes 37 (2002), 1084–1104.
    • (2002) Diabetes , vol.37 , pp. 1084-1104
    • Ruan, H.1    Hacohen, N.2    Golub, T.R.3
  • 71
    • 0029041905 scopus 로고
    • Effects of tumour necrosis factor-alpha (TNF-α) on glucose transport and lipid metabolism of newly-differentiated human fat cells in cell culture
    • [71] Hauner, H., Petruschke, T., Russ, M., et al. Effects of tumour necrosis factor-alpha (TNF-α) on glucose transport and lipid metabolism of newly-differentiated human fat cells in cell culture. Diabetologia 38 (1995), 764–771.
    • (1995) Diabetologia , vol.38 , pp. 764-771
    • Hauner, H.1    Petruschke, T.2    Russ, M.3
  • 72
    • 0023202754 scopus 로고
    • Multiple effects of tumor necrosis factor on lipoprotein lipase in vivo
    • [72] Semb, H., Peterson, J., Tavernier, J., et al. Multiple effects of tumor necrosis factor on lipoprotein lipase in vivo. J. Biol. Chem. 262 (1987), 8390–8394.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8390-8394
    • Semb, H.1    Peterson, J.2    Tavernier, J.3
  • 73
    • 0024210007 scopus 로고
    • 14C] lipid load in virgin, lactating and litter-removed rats
    • 14C] lipid load in virgin, lactating and litter-removed rats. Biochem. J. 256 (1988), 1055–1058.
    • (1988) Biochem. J. , vol.256 , pp. 1055-1058
    • Evans, R.D.1    Williamson, D.H.2
  • 74
    • 12144281235 scopus 로고    scopus 로고
    • Adipose tissue in Walker 256 tumor-induced cachexia: possible association between decreased leptin concentration and mononuclear cell infiltration
    • [74] Machado, A.P., Costa Rosa, L.F.P.B., Seelaender, M.C.L., Adipose tissue in Walker 256 tumor-induced cachexia: possible association between decreased leptin concentration and mononuclear cell infiltration. Cell Tissue Res. 318 (2004), 503–514.
    • (2004) Cell Tissue Res. , vol.318 , pp. 503-514
    • Machado, A.P.1    Costa Rosa, L.F.P.B.2    Seelaender, M.C.L.3
  • 75
    • 0036789186 scopus 로고    scopus 로고
    • Tumor necrosis factor-α stimulates lipolysis in differentiated human adipocytes through activation of extracellular signal-related kinase and elevation of intracellular cyclic AMP
    • [75] Zhang, H.H., Halbleib, M., Ahmad, F., Manganiello, V.C., Greenberg, A.S., Tumor necrosis factor-α stimulates lipolysis in differentiated human adipocytes through activation of extracellular signal-related kinase and elevation of intracellular cyclic AMP. Diabetes 51 (2002), 2929–2935.
    • (2002) Diabetes , vol.51 , pp. 2929-2935
    • Zhang, H.H.1    Halbleib, M.2    Ahmad, F.3    Manganiello, V.C.4    Greenberg, A.S.5
  • 76
    • 0033772576 scopus 로고    scopus 로고
    • Metabolic abnormalities in cachexia and anorexia
    • [76] Tisdale, M.J., Metabolic abnormalities in cachexia and anorexia. Nutrition 16 (2000), 1013–1014.
    • (2000) Nutrition , vol.16 , pp. 1013-1014
    • Tisdale, M.J.1
  • 77
    • 0016808998 scopus 로고
    • Altered glucose metabolism in metastatic carcinoma
    • [77] Holroyde, C.P., Gabuzda, T.G., Putnam, R.C., et al. Altered glucose metabolism in metastatic carcinoma. Cancer Res. 35 (1975), 3710–3714.
    • (1975) Cancer Res. , vol.35 , pp. 3710-3714
    • Holroyde, C.P.1    Gabuzda, T.G.2    Putnam, R.C.3
  • 78
    • 0026356297 scopus 로고
    • Effect of different tumor types on resting energy expenditure
    • [78] Fredrix, E.W., Soeters, P.B., Wouters, E.F., et al. Effect of different tumor types on resting energy expenditure. Cancer Res. 51 (1991), 6138–6141.
    • (1991) Cancer Res. , vol.51 , pp. 6138-6141
    • Fredrix, E.W.1    Soeters, P.B.2    Wouters, E.F.3
  • 79
    • 0028348894 scopus 로고
    • Cytokines, the acute-phase response, and resting energy expenditure in cachectic patients with pancreatic cancer
    • [79] Falconer, J.S., Fearon, K.C., Plester, C.E., et al. Cytokines, the acute-phase response, and resting energy expenditure in cachectic patients with pancreatic cancer. Ann. Surg. 219 (1994), 325–331.
    • (1994) Ann. Surg. , vol.219 , pp. 325-331
    • Falconer, J.S.1    Fearon, K.C.2    Plester, C.E.3
  • 80
    • 0026769166 scopus 로고
    • A review of cancer cachexin and abnormal glucose metabolism in humans with cancer
    • [80] Tayek, J.A., A review of cancer cachexin and abnormal glucose metabolism in humans with cancer. J. Am. Coll. Nutr. 11 (1992), 445–456.
    • (1992) J. Am. Coll. Nutr. , vol.11 , pp. 445-456
    • Tayek, J.A.1
  • 81
    • 0027765624 scopus 로고
    • Cachectin/TNF-mediated lactate production in cultured myocytes is linked to activation of a futile substrate cycle
    • [81] Zentella, A., Manoque, K., Cerami, A., Cachectin/TNF-mediated lactate production in cultured myocytes is linked to activation of a futile substrate cycle. Cytokines 5 (1993), 436–447.
    • (1993) Cytokines , vol.5 , pp. 436-447
    • Zentella, A.1    Manoque, K.2    Cerami, A.3
  • 82
    • 67649982995 scopus 로고    scopus 로고
    • Mechanisms of cancer cachexia
    • [82] Tisdale, M.J., Mechanisms of cancer cachexia. Physiol. Rev. 89 (2009), 381–410.
    • (2009) Physiol. Rev. , vol.89 , pp. 381-410
    • Tisdale, M.J.1
  • 83
    • 84866540191 scopus 로고    scopus 로고
    • The role of insulin resistance in the development of muscle wasting during cancer cachexia
    • [83] Honors, M.A., Kinzig, K.P., The role of insulin resistance in the development of muscle wasting during cancer cachexia. J. Cachex. Sarcopenia Muscle 3 (2012), 5–11.
    • (2012) J. Cachex. Sarcopenia Muscle , vol.3 , pp. 5-11
    • Honors, M.A.1    Kinzig, K.P.2
  • 84
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • [84] Lecker, S.H., Solomon, V., Mitch, W.E., et al. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 129 (1999), 227S–237S.
    • (1999) J. Nutr. , vol.129 , pp. 227S-237S
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3
  • 85
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • [85] Lecker, S.H., Goldberg, A.L., Mitch, W.E., Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J. Am. Soc. Nephrol. 17 (2006), 1807–1819.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 86
    • 0032583609 scopus 로고    scopus 로고
    • Insulin resistance in cancer patients is associated with enhanced tumor necrosis factor α expression in skeletal muscle
    • [86] Noguchi, Y., Yoshikawa, T., Marat, D., et al. Insulin resistance in cancer patients is associated with enhanced tumor necrosis factor α expression in skeletal muscle. Biochem. Biophys. Res. Commun. 253 (1998), 887–892.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 887-892
    • Noguchi, Y.1    Yoshikawa, T.2    Marat, D.3
  • 87
    • 33745861300 scopus 로고    scopus 로고
    • Inflammation and insulin resistance
    • [87] Shoelson, S.E., Lee, J., Goldfine, A.B., Inflammation and insulin resistance. J. Clin. Invest. 116 (2006), 1793–1801.
    • (2006) J. Clin. Invest. , vol.116 , pp. 1793-1801
    • Shoelson, S.E.1    Lee, J.2    Goldfine, A.B.3
  • 88
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • [88] Ozcan, U., Cao, Q., Yilmaz, E., et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306 (2004), 457–461.
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1    Cao, Q.2    Yilmaz, E.3
  • 89
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH (2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser (307)
    • [89] Aguirre, V., Uchida, T., Yenush, L., et al. The c-Jun NH (2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser (307). J. Biol. Chem. 275 (2000), 9047–9054.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3
  • 90
    • 0037059330 scopus 로고    scopus 로고
    • Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action
    • [90] Aguirre, V., Werner, E.D., Giraud, J., et al. Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action. J. Biol. Chem. 277 (2002), 1531–1537.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1531-1537
    • Aguirre, V.1    Werner, E.D.2    Giraud, J.3
  • 91
    • 34247489726 scopus 로고    scopus 로고
    • Inflammation in obesity is the common link between defects in fatty acid metabolism and insulin resistance
    • [91] Steinberg, G.R., Inflammation in obesity is the common link between defects in fatty acid metabolism and insulin resistance. Cell Cycle 6 (2007), 888–894.
    • (2007) Cell Cycle , vol.6 , pp. 888-894
    • Steinberg, G.R.1
  • 92
    • 0031022434 scopus 로고    scopus 로고
    • TNF-α induced insulin resistance in 3T3-L1 adipocyte is accompanied by a loss of insulin receptor substrate-1 and GLUT-4 expression without a loss of insulin receptor mediated signal transduction
    • [92] Stephens, J.M., Lee, J., Pilch, P.F., TNF-α induced insulin resistance in 3T3-L1 adipocyte is accompanied by a loss of insulin receptor substrate-1 and GLUT-4 expression without a loss of insulin receptor mediated signal transduction. J. Biol. Chem. 272 (1997), 971–976.
    • (1997) J. Biol. Chem. , vol.272 , pp. 971-976
    • Stephens, J.M.1    Lee, J.2    Pilch, P.F.3
  • 93
    • 0026727093 scopus 로고
    • Serum tumor necrosis factor alpha and insulin resistance in gastrointestinal cancer
    • [93] Mc Call, J.L., Tuckey, J.A., Parry, B.R., Serum tumor necrosis factor alpha and insulin resistance in gastrointestinal cancer. Br. J. Surg. 79 (1992), 1361–1363.
    • (1992) Br. J. Surg. , vol.79 , pp. 1361-1363
    • Mc Call, J.L.1    Tuckey, J.A.2    Parry, B.R.3
  • 94
    • 0032931280 scopus 로고    scopus 로고
    • Pancreatic cancer as a model: inflammatory mediators, acute-phase response, and cancer cachexia
    • [94] Fearon, K.C.H., Barber, M.D., Falconer, J.S., et al. Pancreatic cancer as a model: inflammatory mediators, acute-phase response, and cancer cachexia. World J. Surg. 23 (1999), 584–588.
    • (1999) World J. Surg. , vol.23 , pp. 584-588
    • Fearon, K.C.H.1    Barber, M.D.2    Falconer, J.S.3
  • 95
    • 0344765509 scopus 로고    scopus 로고
    • Albumin synthesis rates are not decreased in hypoalbuminemic cachectic cancer patients with an ongoing acute-phase protein response
    • [95] Fearon, K.C., Falconer, J.S., Slater, C., et al. Albumin synthesis rates are not decreased in hypoalbuminemic cachectic cancer patients with an ongoing acute-phase protein response. Ann. Surg. 227 (1998), 249–254.
    • (1998) Ann. Surg. , vol.227 , pp. 249-254
    • Fearon, K.C.1    Falconer, J.S.2    Slater, C.3
  • 96
    • 0029089803 scopus 로고
    • Increased resting energy expenditure and weight loss are related to a systemic inflammatory response in lung cancer patients
    • [96] den Brekel, A.J., S-V, Dentener, M.A., Schols, A.M., et al. Increased resting energy expenditure and weight loss are related to a systemic inflammatory response in lung cancer patients. J. Clin. Oncol. 13 (1995), 2600–2605.
    • (1995) J. Clin. Oncol. , vol.13 , pp. 2600-2605
    • den Brekel, A.J.1    Dentener, M.A.2    Schols, A.M.3
  • 97
    • 0030018821 scopus 로고    scopus 로고
    • The relationship between weight loss and interleukin 6 in non-small cell lung cancer
    • [97] Scott, H.R., McMillan, D.C., Crilly, A., et al. The relationship between weight loss and interleukin 6 in non-small cell lung cancer. Br. J. Cancer 73 (1996), 1560–1562.
    • (1996) Br. J. Cancer , vol.73 , pp. 1560-1562
    • Scott, H.R.1    McMillan, D.C.2    Crilly, A.3
  • 98
    • 0028933898 scopus 로고
    • Acute-phase protein response and survival duration of patients with pancreatic cancer
    • [98] Falconer, J.S., Fearon, K.C., Ross, J.A., et al. Acute-phase protein response and survival duration of patients with pancreatic cancer. Cancer 75 (1995), 2077–2082.
    • (1995) Cancer , vol.75 , pp. 2077-2082
    • Falconer, J.S.1    Fearon, K.C.2    Ross, J.A.3
  • 99
    • 0032416650 scopus 로고    scopus 로고
    • Impact of weight loss, appetite, and the inflammatory response on quality of life in gastrointestinal cancer patients
    • [99] O'Gorman, P., McMillan, D., McArdle, C., Impact of weight loss, appetite, and the inflammatory response on quality of life in gastrointestinal cancer patients. Nutr. Cancer 32 (1998), 76–80.
    • (1998) Nutr. Cancer , vol.32 , pp. 76-80
    • O'Gorman, P.1    McMillan, D.2    McArdle, C.3
  • 100
    • 0033507217 scopus 로고    scopus 로고
    • Changes in nutritional, functional, and inflammatory markers in advanced pancreatic cancer
    • [100] Barber, M.D., Ross, J.A., Fearon, K.C.H., Changes in nutritional, functional, and inflammatory markers in advanced pancreatic cancer. Nutr. Cancer 35 (1999), 106–110.
    • (1999) Nutr. Cancer , vol.35 , pp. 106-110
    • Barber, M.D.1    Ross, J.A.2    Fearon, K.C.H.3
  • 101
    • 0031006421 scopus 로고    scopus 로고
    • Cytokines and the hepatic acute phase response
    • [101] Moshage, H., Cytokines and the hepatic acute phase response. J. Pathol. 181 (1997), 257–266.
    • (1997) J. Pathol. , vol.181 , pp. 257-266
    • Moshage, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.