nach oben

Calcified Tissue International

Erschienen in:

09.11.2016 | Review

Molecular Communication from Skeletal Muscle to Bone: A Review for Muscle-Derived Myokines Regulating Bone Metabolism

verfasst von: Baosheng Guo, Zong-Kang Zhang, Chao Liang, Jie Li, Jin Liu, Aiping Lu, Bao-Ting Zhang, Ge Zhang

Erschienen in: Calcified Tissue International | Ausgabe 2/2017

Einloggen, um Zugang zu erhalten

Abstract

Besides the mechanical loading-dependent paradigm, skeletal muscle also serves as an endocrine organ capable of secreting cytokines to modulate bone metabolism. In this review, we focused on reviewing the myokines involved in communication from skeletal muscle to bone, i.e. (1) myostatin and myostatin-binding proteins including follistatin and decorin, (2) interleukins including interleukin-6 (IL-6), interleukin-7 (IL-7) and interleukin-15 (IL-15), (3) insulin-like growth factor 1 (IGF-1) and its binding proteins, (4) other myokines including PGC-1α-irisin system and osteoglycin (OGN). To better understand the molecular communication from skeletal muscle to bone, we have summarized the recent advances in muscle-derived cytokines regulating bone metabolism in this review.

Schipilow JD, Macdonald HM, Liphardt AM, Kan M, Boyd SK (2013) Bone micro-architecture, estimated bone strength, and the muscle-bone interaction in elite athletes: an HR-pQCT study. Bone 56(2):281–289. doi:10.1016/j.bone.2013.06.014 CrossRefPubMed

Frost HM (2003) Bone’s mechanostat: a 2003 update. Anat Rec A Discov Mol Cell Evol Biol 275(2):1081–1101. doi:10.1002/ar.a.10119 CrossRefPubMed

Verschueren S, Gielen E, O’Neill TW, Pye SR, Adams JE, Ward KA, Wu FC, Szulc P, Laurent M, Claessens F, Vanderschueren D, Boonen S (2013) Sarcopenia and its relationship with bone mineral density in middle-aged and elderly European men. Osteoporos Int 24(1):87–98. doi:10.1007/s00198-012-2057-z CrossRefPubMed

Harry LE, Sandison A, Paleolog EM, Hansen U, Pearse MF, Nanchahal J (2008) Comparison of the healing of open tibial fractures covered with either muscle or fasciocutaneous tissue in a murine model. J Orthop Res 26(9):1238–1244. doi:10.1002/jor.20649 CrossRefPubMed

Henningsen J, Rigbolt KT, Blagoev B, Pedersen BK, Kratchmarova I (2010) Dynamics of the skeletal muscle secretome during myoblast differentiation. Mol Cell Proteomics 9(11):2482–2496. doi:10.1074/mcp.M110.002113 CrossRefPubMedPubMedCentral

Pedersen BK, Steensberg A, Fischer C, Keller C, Keller P, Plomgaard P, Febbraio M, Saltin B (2003) Searching for the exercise factor: is IL-6 a candidate? J Muscle Res Cell Motil 24(2–3):113–119CrossRefPubMed

McPherron AC, Lawler AM, Lee SJ (1997) Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 387(6628):83–90. doi:10.1038/387083a0 CrossRefPubMed

Mosher DS, Quignon P, Bustamante CD, Sutter NB, Mellersh CS, Parker HG, Ostrander EA (2007) A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs. PLoS Genet 3(5):e79. doi:10.1371/journal.pgen.0030079 CrossRefPubMedPubMedCentral

Grobet L, Martin LJ, Poncelet D, Pirottin D, Brouwers B, Riquet J, Schoeberlein A, Dunner S, Menissier F, Massabanda J, Fries R, Hanset R, Georges M (1997) A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat Genet 17(1):71–74. doi:10.1038/ng0997-71 CrossRefPubMed

10.

Schuelke M, Wagner KR, Stolz LE, Hubner C, Riebel T, Komen W, Braun T, Tobin JF, Lee SJ (2004) Myostatin mutation associated with gross muscle hypertrophy in a child. N Engl J Med 350(26):2682–2688. doi:10.1056/NEJMoa040933 CrossRefPubMed

11.

Saremi A, Gharakhanloo R, Sharghi S, Gharaati MR, Larijani B, Omidfar K (2010) Effects of oral creatine and resistance training on serum myostatin and GASP-1. Mol Cell Endocrinol 317(1–2):25–30. doi:10.1016/j.mce.2009.12.019 CrossRefPubMed

12.

Hittel DS, Axelson M, Sarna N, Shearer J, Huffman KM, Kraus WE (2010) Myostatin decreases with aerobic exercise and associates with insulin resistance. Med Sci Sports Exerc 42(11):2023–2029. doi:10.1249/MSS.0b013e3181e0b9a8 CrossRefPubMedPubMedCentral

13.

Bialek P, Parkington J, Li X, Gavin D, Wallace C, Zhang J, Root A, Yan G, Warner L, Seeherman HJ, Yaworsky PJ (2014) A myostatin and activin decoy receptor enhances bone formation in mice. Bone 60:162–171. doi:10.1016/j.bone.2013.12.002 CrossRefPubMed

14.

Park JJ, Berggren JR, Hulver MW, Houmard JA, Hoffman EP (2006) GRB14, GPD1, and GDF8 as potential network collaborators in weight loss-induced improvements in insulin action in human skeletal muscle. Physiol Genomics 27(2):114–121. doi:10.1152/physiolgenomics.00045.2006 CrossRefPubMed

15.

Elkasrawy MN, Hamrick MW (2010) Myostatin (GDF-8) as a key factor linking muscle mass and bone structure. J Musculoskelet Neuronal Interact 10(1):56–63PubMedPubMedCentral

16.

Chiu CS, Peekhaus N, Weber H, Adamski S, Murray EM, Zhang HZ, Zhao JZ, Ernst R, Lineberger J, Huang L, Hampton R, Arnold BA, Vitelli S, Hamuro L, Wang WR, Wei N, Dillon GM, Miao J, Alves SE, Glantschnig H, Wang F, Wilkinson HA (2013) Increased muscle force production and bone mineral density in ActRIIB-Fc-treated mature rodents. J Gerontol A Biol Sci Med Sci 68(10):1181–1192. doi:10.1093/gerona/glt030 CrossRefPubMed

17.

Rothney MP, Martin FP, Xia Y, Beaumont M, Davis C, Ergun D, Fay L, Ginty F, Kochhar S, Wacker W, Rezzi S (2012) Precision of GE Lunar iDXA for the measurement of total and regional body composition in nonobese adults. J Clin Densitom 15(4):399–404. doi:10.1016/j.jocd.2012.02.009 CrossRefPubMed

18.

Dankbar B, Fennen M, Brunert D, Hayer S, Frank S, Wehmeyer C, Beckmann D, Paruzel P, Bertrand J, Redlich K, Koers-Wunrau C, Stratis A, Korb-Pap A, Pap T (2015) Myostatin is a direct regulator of osteoclast differentiation and its inhibition reduces inflammatory joint destruction in mice. Nat Med 21(9):1085–1090. doi:10.1038/nm.3917 CrossRefPubMed

19.

Amthor H, Nicholas G, McKinnell I, Kemp CF, Sharma M, Kambadur R, Patel K (2004) Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis. Dev Biol 270(1):19–30. doi:10.1016/j.ydbio.2004.01.046 CrossRefPubMed

20.

Gilson H, Schakman O, Kalista S, Lause P, Tsuchida K, Thissen JP (2009) Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am J Physiol Endocrinol Metab 297(1):E157–E164. doi:10.1152/ajpendo.00193.2009 CrossRefPubMed

21.

Lee SJ, Reed LA, Davies MV, Girgenrath S, Goad ME, Tomkinson KN, Wright JF, Barker C, Ehrmantraut G, Holmstrom J, Trowell B, Gertz B, Jiang MS, Sebald SM, Matzuk M, Li E, Liang LF, Quattlebaum E, Stotish RL, Wolfman NM (2005) Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Proc Natl Acad Sci USA 102(50):18117–18122. doi:10.1073/pnas.0505996102 CrossRefPubMedPubMedCentral

22.

Sepulveda PV, Lamon S, Hagg A, Thomson RE, Winbanks CE, Qian H, Bruce CR, Russell AP, Gregorevic P (2015) Evaluation of follistatin as a therapeutic in models of skeletal muscle atrophy associated with denervation and tenotomy. Sci Rep 5:17535. doi:10.1038/srep17535 CrossRefPubMedPubMedCentral

23.

Hansen J, Brandt C, Nielsen AR, Hojman P, Whitham M, Febbraio MA, Pedersen BK, Plomgaard P (2011) Exercise induces a marked increase in plasma follistatin: evidence that follistatin is a contraction-induced hepatokine. Endocrinology 152(1):164–171. doi:10.1210/en.2010-0868 CrossRefPubMed

24.

Ouchi N, Oshima Y, Ohashi K, Higuchi A, Ikegami C, Izumiya Y, Walsh K (2008) Follistatin-like 1, a secreted muscle protein, promotes endothelial cell function and revascularization in ischemic tissue through a nitric-oxide synthase-dependent mechanism. J Biol Chem 283(47):32802–32811. doi:10.1074/jbc.M803440200 CrossRefPubMedPubMedCentral

25.

Eijken M, Swagemakers S, Koedam M, Steenbergen C, Derkx P, Uitterlinden AG, van der Spek PJ, Visser JA, de Jong FH, Pols HA, van Leeuwen JP (2007) The activin A-follistatin system: potent regulator of human extracellular matrix mineralization. FASEB J 21(11):2949–2960. doi:10.1096/fj.07-8080com CrossRefPubMed

26.

Kanzleiter T, Rath M, Gorgens SW, Jensen J, Tangen DS, Kolnes AJ, Kolnes KJ, Lee S, Eckel J, Schurmann A, Eckardt K (2014) The myokine decorin is regulated by contraction and involved in muscle hypertrophy. Biochem Biophys Res Commun 450(2):1089–1094. doi:10.1016/j.bbrc.2014.06.123 CrossRefPubMed

27.

Miura T, Kishioka Y, Wakamatsu J, Hattori A, Hennebry A, Berry CJ, Sharma M, Kambadur R, Nishimura T (2006) Decorin binds myostatin and modulates its activity to muscle cells. Biochem Biophys Res Commun 340(2):675–680. doi:10.1016/j.bbrc.2005.12.060 CrossRefPubMed

28.

Han XG, Wang DK, Gao F, Liu RH, Bi ZG (2015) Bone morphogenetic protein 2 and decorin expression in old fracture fragments and surrounding tissues. Genet Mol Res 14(3):11063–11072. doi:10.4238/2015.September.21.19 CrossRefPubMed

29.

Takeuchi Y, Kodama Y, Matsumoto T (1994) Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity. J Biol Chem 269(51):32634–32638PubMed

30.

Kristiansen OP, Mandrup-Poulsen T (2005) Interleukin-6 and diabetes: the good, the bad, or the indifferent? Diabetes 54(Suppl 2):S114–S124CrossRefPubMed

31.

Steensberg A, van Hall G, Osada T, Sacchetti M, Saltin B, Klarlund Pedersen B (2000) Production of interleukin-6 in contracting human skeletal muscles can account for the exercise-induced increase in plasma interleukin-6. J Physiol 529(Pt 1):237–242CrossRefPubMedPubMedCentral

32.

Pedersen BK, Febbraio MA (2008) Muscle as an endocrine organ: focus on muscle-derived interleukin-6. Physiol Rev 88(4):1379–1406. doi:10.1152/physrev.90100.2007 CrossRefPubMed

33.

Croisier JL, Camus G, Venneman I, Deby-Dupont G, Juchmes-Ferir A, Lamy M, Crielaard JM, Deby C, Duchateau J (1999) Effects of training on exercise-induced muscle damage and interleukin 6 production. Muscle Nerve 22(2):208–212CrossRefPubMed

34.

Carey AL, Steinberg GR, Macaulay SL, Thomas WG, Holmes AG, Ramm G, Prelovsek O, Hohnen-Behrens C, Watt MJ, James DE, Kemp BE, Pedersen BK, Febbraio MA (2006) Interleukin-6 increases insulin-stimulated glucose disposal in humans and glucose uptake and fatty acid oxidation in vitro via AMP-activated protein kinase. Diabetes 55(10):2688–2697. doi:10.2337/db05-1404 CrossRefPubMed

35.

Pedersen BK, Steensberg A, Schjerling P (2001) Exercise and interleukin-6. Curr Opin Hematol 8(3):137–141CrossRefPubMed

36.

Ellingsgaard H, Hauselmann I, Schuler B, Habib AM, Baggio LL, Meier DT, Eppler E, Bouzakri K, Wueest S, Muller YD, Hansen AM, Reinecke M, Konrad D, Gassmann M, Reimann F, Halban PA, Gromada J, Drucker DJ, Gribble FM, Ehses JA, Donath MY (2011) Interleukin-6 enhances insulin secretion by increasing glucagon-like peptide-1 secretion from L cells and alpha cells. Nat Med 17(11):1481–1489. doi:10.1038/nm.2513 CrossRefPubMedPubMedCentral

37.

Pedersen BK (2012) Muscular interleukin-6 and its role as an energy sensor. Med Sci Sports Exerc 44(3):392–396. doi:10.1249/MSS.0b013e31822f94ac CrossRefPubMed

38.

Heymann D, Rousselle AV (2000) gp130 Cytokine family and bone cells. Cytokine 12(10):1455–1468. doi:10.1006/cyto.2000.0747 CrossRefPubMed

39.

Poli V, Balena R, Fattori E, Markatos A, Yamamoto M, Tanaka H, Ciliberto G, Rodan GA, Costantini F (1994) Interleukin-6 deficient mice are protected from bone loss caused by estrogen depletion. EMBO J 13(5):1189–1196PubMedPubMedCentral

40.

De Benedetti F, Rucci N, Del Fattore A, Peruzzi B, Paro R, Longo M, Vivarelli M, Muratori F, Berni S, Ballanti P, Ferrari S, Teti A (2006) Impaired skeletal development in interleukin-6-transgenic mice: a model for the impact of chronic inflammation on the growing skeletal system. Arthritis Rheum 54(11):3551–3563. doi:10.1002/art.22175 CrossRefPubMed

41.

Yokota K, Sato K, Miyazaki T, Kitaura H, Kayama H, Miyoshi F, Araki Y, Akiyama Y, Takeda K, Mimura T (2014) Combination of tumor necrosis factor alpha and interleukin-6 induces mouse osteoclast-like cells with bone resorption activity both in vitro and in vivo. Arthritis Rheumatol 66(1):121–129. doi:10.1002/art.38218 CrossRefPubMed

42.

Duplomb L, Baud’huin M, Charrier C, Berreur M, Trichet V, Blanchard F, Heymann D (2008) Interleukin-6 inhibits receptor activator of nuclear factor kappaB ligand-induced osteoclastogenesis by diverting cells into the macrophage lineage: key role of Serine727 phosphorylation of signal transducer and activator of transcription 3. Endocrinology 149(7):3688–3697. doi:10.1210/en.2007-1719 CrossRefPubMed

43.

Kusano K, Miyaura C, Inada M, Tamura T, Ito A, Nagase H, Kamoi K, Suda T (1998) Regulation of matrix metalloproteinases (MMP-2, -3, -9, and -13) by interleukin-1 and interleukin-6 in mouse calvaria: association of MMP induction with bone resorption. Endocrinology 139(3):1338–1345. doi:10.1210/endo.139.3.5818 PubMed

44.

Yang X, Ricciardi BF, Hernandez-Soria A, Shi Y, Pleshko Camacho N, Bostrom MP (2007) Callus mineralization and maturation are delayed during fracture healing in interleukin-6 knockout mice. Bone 41(6):928–936. doi:10.1016/j.bone.2007.07.022 CrossRefPubMedPubMedCentral

45.

Bakker AD, Kulkarni RN, Klein-Nulend J, Lems WF (2014) IL-6 alters osteocyte signaling toward osteoblasts but not osteoclasts. J Dent Res 93(4):394–399. doi:10.1177/0022034514522485 CrossRefPubMed

46.

Rufo A, Del Fattore A, Capulli M, Carvello F, De Pasquale L, Ferrari S, Pierroz D, Morandi L, De Simone M, Rucci N, Bertini E, Bianchi ML, De Benedetti F, Teti A (2011) Mechanisms inducing low bone density in Duchenne muscular dystrophy in mice and humans. J Bone Miner Res 26(8):1891–1903. doi:10.1002/jbmr.410 CrossRefPubMedPubMedCentral

47.

Haugen F, Norheim F, Lian H, Wensaas AJ, Dueland S, Berg O, Funderud A, Skalhegg BS, Raastad T, Drevon CA (2010) IL-7 is expressed and secreted by human skeletal muscle cells. Am J Physiol Cell Physiol 298(4):C807–c816. doi:10.1152/ajpcell.00094.2009 CrossRefPubMed

48.

Ceredig R, Rolink AG (2012) The key role of IL-7 in lymphopoiesis. Semin Immunol 24(3):159–164. doi:10.1016/j.smim.2012.02.004 CrossRefPubMed

49.

Weitzmann MN, Roggia C, Toraldo G, Weitzmann L, Pacifici R (2002) Increased production of IL-7 uncouples bone formation from bone resorption during estrogen deficiency. J Clin Investig 110(11):1643–1650. doi:10.1172/JCI15687 CrossRefPubMedPubMedCentral

50.

Giri JG, Anderson DM, Kumaki S, Park LS, Grabstein KH, Cosman D (1995) IL-15, a novel T cell growth factor that shares activities and receptor components with IL-2. J Leukoc Biol 57(5):763–766PubMed

51.

Giri JG, Kumaki S, Ahdieh M, Friend DJ, Loomis A, Shanebeck K, DuBose R, Cosman D, Park LS, Anderson DM (1995) Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. EMBO J 14(15):3654–3663PubMedPubMedCentral

52.

Nielsen AR, Mounier R, Plomgaard P, Mortensen OH, Penkowa M, Speerschneider T, Pilegaard H, Pedersen BK (2007) Expression of interleukin-15 in human skeletal muscle effect of exercise and muscle fibre type composition. J Physiol 584(Pt 1):305–312. doi:10.1113/jphysiol.2007.139618 CrossRefPubMedPubMedCentral

53.

Carbo N, Lopez-Soriano J, Costelli P, Busquets S, Alvarez B, Baccino FM, Quinn LS, Lopez-Soriano FJ, Argiles JM (2000) Interleukin-15 antagonizes muscle protein waste in tumour-bearing rats. Br J Cancer 83(4):526–531. doi:10.1054/bjoc.2000.1299 CrossRefPubMedPubMedCentral

54.

Quinn LS, Anderson BG, Drivdahl RH, Alvarez B, Argiles JM (2002) Overexpression of interleukin-15 induces skeletal muscle hypertrophy in vitro: implications for treatment of muscle wasting disorders. Exp Cell Res 280(1):55–63CrossRefPubMed

55.

Djaafar S, Pierroz DD, Chicheportiche R, Zheng XX, Ferrari SL, Ferrari-Lacraz S (2010) Inhibition of T cell-dependent and RANKL-dependent osteoclastogenic processes associated with high levels of bone mass in interleukin-15 receptor-deficient mice. Arthritis Rheum 62(11):3300–3310. doi:10.1002/art.27645 CrossRefPubMed

56.

Feng S, Madsen SH, Viller NN, Neutzsky-Wulff AV, Geisler C, Karlsson L, Soderstrom K (2015) Interleukin-15-activated natural killer cells kill autologous osteoclasts via LFA-1, DNAM-1 and TRAIL, and inhibit osteoclast-mediated bone erosion in vitro. Immunology 145(3):367–379. doi:10.1111/imm.12449 CrossRefPubMedPubMedCentral

57.

Hamrick MW, McNeil PL, Patterson SL (2010) Role of muscle-derived growth factors in bone formation. J Musculoskelet Neuronal Interact 10(1):64–70PubMedPubMedCentral

58.

Yakar S, Rosen CJ, Beamer WG, Ackert-Bicknell CL, Wu Y, Liu JL, Ooi GT, Setser J, Frystyk J, Boisclair YR, LeRoith D (2002) Circulating levels of IGF-1 directly regulate bone growth and density. J Clin Investig 110(6):771–781. doi:10.1172/JCI15463 CrossRefPubMedPubMedCentral

59.

Perrini S, Laviola L, Carreira MC, Cignarelli A, Natalicchio A, Giorgino F (2010) The GH/IGF1 axis and signaling pathways in the muscle and bone: mechanisms underlying age-related skeletal muscle wasting and osteoporosis. J Endocrinol 205(3):201–210. doi:10.1677/JOE-09-0431 CrossRefPubMed

60.

Peng XD, Xu PZ, Chen ML, Hahn-Windgassen A, Skeen J, Jacobs J, Sundararajan D, Chen WS, Crawford SE, Coleman KG, Hay N (2003) Dwarfism, impaired skin development, skeletal muscle atrophy, delayed bone development, and impeded adipogenesis in mice lacking Akt1 and Akt2. Genes Dev 17(11):1352–1365. doi:10.1101/gad.1089403 CrossRefPubMedPubMedCentral

61.

Ambrogini E, Almeida M, Martin-Millan M, Paik JH, Depinho RA, Han L, Goellner J, Weinstein RS, Jilka RL, O’Brien CA, Manolagas SC (2010) FoxO-mediated defense against oxidative stress in osteoblasts is indispensable for skeletal homeostasis in mice. Cell Metab 11(2):136–146. doi:10.1016/j.cmet.2009.12.009 CrossRefPubMedPubMedCentral

62.

Jones JI, Clemmons DR (1995) Insulin-like growth factors and their binding proteins: biological actions. Endocr Rev 16(1):3–34. doi:10.1210/edrv-16-1-3 PubMed

63.

Safian D, Fuentes EN, Valdes JA, Molina A (2012) Dynamic transcriptional regulation of autocrine/paracrine igfbp1, 2, 3, 4, 5, and 6 in the skeletal muscle of the fine flounder during different nutritional statuses. J Endocrinol 214(1):95–108. doi:10.1530/JOE-12-0057 CrossRefPubMed

64.

Jennische E, Hall CM (2000) Expression and localisation of IGF-binding protein mRNAs in regenerating rat skeletal muscle. APMIS 108(11):747–755CrossRefPubMed

65.

Lebrasseur NK, Achenbach SJ, Melton LJ 3rd, Amin S, Khosla S (2012) Skeletal muscle mass is associated with bone geometry and microstructure and serum insulin-like growth factor binding protein-2 levels in adult women and men. J Bone Miner Res 27(10):2159–2169. doi:10.1002/jbmr.1666 CrossRefPubMedPubMedCentral

66.

Rajaram S, Baylink DJ, Mohan S (1997) Insulin-like growth factor-binding proteins in serum and other biological fluids: regulation and functions. Endocr Rev 18(6):801–831. doi:10.1210/edrv.18.6.0321 PubMed

67.

Amin S, Riggs BL, Melton LJ 3rd, Achenbach SJ, Atkinson EJ, Khosla S (2007) High serum IGFBP-2 is predictive of increased bone turnover in aging men and women. J Bone Miner Res 22(6):799–807. doi:10.1359/jbmr.070306 CrossRefPubMed

68.

Bostrom P, Wu J, Jedrychowski MP, Korde A, Ye L, Lo JC, Rasbach KA, Bostrom EA, Choi JH, Long JZ, Kajimura S, Zingaretti MC, Vind BF, Tu H, Cinti S, Hojlund K, Gygi SP, Spiegelman BM (2012) A PGC1-alpha-dependent myokine that drives brown-fat-like development of white fat and thermogenesis. Nature 481(7382):463–468. doi:10.1038/nature10777 CrossRefPubMedPubMedCentral

69.

Lee P, Linderman JD, Smith S, Brychta RJ, Wang J, Idelson C, Perron RM, Werner CD, Phan GQ, Kammula US, Kebebew E, Pacak K, Chen KY, Celi FS (2014) Irisin and FGF21 are cold-induced endocrine activators of brown fat function in humans. Cell metabolism 19(2):302–309. doi:10.1016/j.cmet.2013.12.017 CrossRefPubMed

70.

Vaughan RA, Gannon NP, Barberena MA, Garcia-Smith R, Bisoffi M, Mermier CM, Conn CA, Trujillo KA (2014) Characterization of the metabolic effects of irisin on skeletal muscle in vitro. Diabetes Obes Metab 16(8):711–718. doi:10.1111/dom.12268 CrossRefPubMed

71.

Colaianni G, Cuscito C, Mongelli T, Pignataro P, Buccoliero C, Liu P, Lu P, Sartini L, Di Comite M, Mori G, Di Benedetto A, Brunetti G, Yuen T, Sun L, Reseland JE, Colucci S, New MI, Zaidi M, Cinti S, Grano M (2015) The myokine irisin increases cortical bone mass. Proc Natl Acad Sci USA 112(39):12157–12162. doi:10.1073/pnas.1516622112 CrossRefPubMedPubMedCentral

72.

Colaianni G, Cuscito C, Mongelli T, Oranger A, Mori G, Brunetti G, Colucci S, Cinti S, Grano M (2014) Irisin enhances osteoblast differentiation in vitro. Int J Endocrinol 2014:902186. doi:10.1155/2014/902186 CrossRefPubMedPubMedCentral

73.

Albrecht E, Norheim F, Thiede B, Holen T, Ohashi T, Schering L, Lee S, Brenmoehl J, Thomas S, Drevon CA, Erickson HP, Maak S (2015) Irisin - a myth rather than an exercise-inducible myokine. Sci Rep 5:8889. doi:10.1038/srep08889 CrossRefPubMedPubMedCentral

74.

Jedrychowski MP, Wrann CD, Paulo JA, Gerber KK, Szpyt J, Robinson MM, Nair KS, Gygi SP, Spiegelman BM (2015) Detection and quantitation of circulating human irisin by tandem mass spectrometry. Cell Metab 22(4):734–740. doi:10.1016/j.cmet.2015.08.001 CrossRefPubMedPubMedCentral

75.

Chan CY, Masui O, Krakovska O, Belozerov VE, Voisin S, Ghanny S, Chen J, Moyez D, Zhu P, Evans KR, McDermott JC, Siu KW (2011) Identification of differentially regulated secretome components during skeletal myogenesis. Mol Cell Proteomics 10 (5):M110 004804. doi:10.1074/mcp.M110.004804

76.

Chan CY, McDermott JC, Siu KW (2011) Secretome analysis of skeletal myogenesis using SILAC and shotgun proteomics. Int J Proteomics 2011:329467. doi:10.1155/2011/329467 CrossRefPubMedPubMedCentral

77.

Shore EM, Xu M, Feldman GJ, Fenstermacher DA, Cho TJ, Choi IH, Connor JM, Delai P, Glaser DL, LeMerrer M, Morhart R, Rogers JG, Smith R, Triffitt JT, Urtizberea JA, Zasloff M, Brown MA, Kaplan FS (2006) A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. Nat Genet 38(5):525–527. doi:10.1038/ng1783 CrossRefPubMed

78.

Tanaka K, Matsumoto E, Higashimaki Y, Katagiri T, Sugimoto T, Seino S, Kaji H (2012) Role of osteoglycin in the linkage between muscle and bone. J Biol Chem 287(15):11616–11628. doi:10.1074/jbc.M111.292193 CrossRefPubMedPubMedCentral

79.

Ouchi N, Parker JL, Lugus JJ, Walsh K (2011) Adipokines in inflammation and metabolic disease. Nat Rev Immunol 11(2):85–97. doi:10.1038/nri2921 CrossRefPubMedPubMedCentral

Titel: Molecular Communication from Skeletal Muscle to Bone: A Review for Muscle-Derived Myokines Regulating Bone Metabolism
verfasst von: Baosheng Guo
Zong-Kang Zhang
Chao Liang
Jie Li
Jin Liu
Aiping Lu
Bao-Ting Zhang
Ge Zhang
Publikationsdatum: 09.11.2016
Verlag: Springer US
Erschienen in: Calcified Tissue International / Ausgabe 2/2017
Print ISSN: 0171-967X
Elektronische ISSN: 1432-0827
DOI: https://doi.org/10.1007/s00223-016-0209-4

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

^{Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag}

Kostenlos registrieren

Neu im Fachgebiet Innere Medizin

25.04.2024 | Hypotonie | Nachrichten

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.

Newsletter bestellen

Springer Medizin

Molecular Communication from Skeletal Muscle to Bone: A Review for Muscle-Derived Myokines Regulating Bone Metabolism

Abstract

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Niedriger diastolischer Blutdruck erhöht Risiko für schwere kardiovaskuläre Komplikationen

Therapiestart mit Blutdrucksenkern erhöht Frakturrisiko

Adjuvante Immuntherapie verlängert Leben bei RCC

Alectinib verbessert krankheitsfreies Überleben bei ALK-positivem NSCLC

Update Innere Medizin

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 2/2017

Diabetes and Bone

Epidemiology of Fractures in Diabetes

Pathophysiology of Bone Fragility in Patients with Diabetes

Bone-Derived Factors: A New Gateway to Regulate Glycemia

Diabetes Drug Effects on the Skeleton

Efficacy of Osteoporosis Therapies in Diabetic Patients

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Niedriger diastolischer Blutdruck erhöht Risiko für schwere kardiovaskuläre Komplikationen

Therapiestart mit Blutdrucksenkern erhöht Frakturrisiko

Adjuvante Immuntherapie verlängert Leben bei RCC

Alectinib verbessert krankheitsfreies Überleben bei ALK-positivem NSCLC

Update Innere Medizin