메뉴 건너뛰기




Volumn 80, Issue , 2015, Pages 24-36

Bone and skeletal muscle: Key players in mechanotransduction and potential overlapping mechanisms

Author keywords

Bone mineral density; Growth; Hypertrophy; Mechanical loading; MTORC1

Indexed keywords

7 NITROINDAZOLE; BETA CATENIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE ALPHA; DIACYLGLYCEROL KINASE; DIACYLGLYCEROL KINASE ZETA; G PROTEIN COUPLED RECEPTOR; HYDROGEN PEROXIDE; INDUCIBLE NITRIC OXIDE SYNTHASE; LYSOPHOSPHATIDIC ACID; LYSOPHOSPHATIDIC ACID ACYLTRANSFERASE THETA; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NEURONAL NITRIC OXIDE SYNTHASE; PHOSPHATIDIC ACID; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE D1; POLYCYSTIN 1; POLYCYSTIN 2; PROSTAGLANDIN E2; PROTEIN KINASE B; REACTIVE NITROGEN SPECIES; RHEB PROTEIN; SOMATOMEDIN C; TUBERIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VANILLOID RECEPTOR 4; WNT7B PROTEIN; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; TARGET OF RAPAMYCIN KINASE;

EID: 84943631887     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bone.2015.04.014     Document Type: Review
Times cited : (109)

References (229)
  • 1
    • 84864283300 scopus 로고    scopus 로고
    • Muscles, exercise and obesity: skeletal muscle as a secretory organ
    • Pedersen B.K., Febbraio M.A. Muscles, exercise and obesity: skeletal muscle as a secretory organ. Nat Rev Endocrinol 2012, 8:457-465.
    • (2012) Nat Rev Endocrinol , vol.8 , pp. 457-465
    • Pedersen, B.K.1    Febbraio, M.A.2
  • 2
    • 84896714585 scopus 로고    scopus 로고
    • Enhanced skeletal muscle for effective glucose homeostasis
    • Academic Press, T. Ya-Xiong (Ed.)
    • Yang J. Enhanced skeletal muscle for effective glucose homeostasis. Progress in molecular biology and translational science 2014, 133-163. Academic Press. T. Ya-Xiong (Ed.).
    • (2014) Progress in molecular biology and translational science , pp. 133-163
    • Yang, J.1
  • 3
    • 33750093325 scopus 로고    scopus 로고
    • The underappreciated role of muscle in health and disease
    • Wolfe R.R. The underappreciated role of muscle in health and disease. Am J Clin Nutr 2006, 84:475-482.
    • (2006) Am J Clin Nutr , vol.84 , pp. 475-482
    • Wolfe, R.R.1
  • 4
    • 84879198193 scopus 로고    scopus 로고
    • Bone and skeletal muscle: neighbors with close ties
    • DiGirolamo D.J., Kiel D.P., Esser K.A. Bone and skeletal muscle: neighbors with close ties. J Bone Miner Res 2013, 28:1509-1518.
    • (2013) J Bone Miner Res , vol.28 , pp. 1509-1518
    • DiGirolamo, D.J.1    Kiel, D.P.2    Esser, K.A.3
  • 5
    • 84857279874 scopus 로고    scopus 로고
    • Biology without walls: the novel endocrinology of bone
    • Karsenty G., Oury F. Biology without walls: the novel endocrinology of bone. Annu Rev Physiol 2012, 74:87-105.
    • (2012) Annu Rev Physiol , vol.74 , pp. 87-105
    • Karsenty, G.1    Oury, F.2
  • 7
    • 84882733761 scopus 로고    scopus 로고
    • Mechanisms regulating skeletal muscle growth and atrophy
    • Schiaffino S., Dyar K.A., Ciciliot S., Blaauw B., Sandri M. Mechanisms regulating skeletal muscle growth and atrophy. FEBS J 2013, 280:4294-4314.
    • (2013) FEBS J , vol.280 , pp. 4294-4314
    • Schiaffino, S.1    Dyar, K.A.2    Ciciliot, S.3    Blaauw, B.4    Sandri, M.5
  • 8
    • 84865789881 scopus 로고    scopus 로고
    • The interaction of biological factors with mechanical signals in bone adaptation: recent developments
    • Robling A.G. The interaction of biological factors with mechanical signals in bone adaptation: recent developments. Curr Osteoporos Rep 2012, 10:126-131.
    • (2012) Curr Osteoporos Rep , vol.10 , pp. 126-131
    • Robling, A.G.1
  • 9
    • 84899709626 scopus 로고    scopus 로고
    • The role of mTORC1 in regulating protein synthesis and skeletal muscle mass in response to various mechanical stimuli
    • Goodman C.A. The role of mTORC1 in regulating protein synthesis and skeletal muscle mass in response to various mechanical stimuli. Rev Physiol Biochem Pharmacol 2014, 166:1-53.
    • (2014) Rev Physiol Biochem Pharmacol , vol.166 , pp. 1-53
    • Goodman, C.A.1
  • 10
    • 84891685343 scopus 로고    scopus 로고
    • Characterization and regulation of mechanical loading-induced compensatory muscle hypertrophy
    • Adams G.R., Bamman M.M. Characterization and regulation of mechanical loading-induced compensatory muscle hypertrophy. Compr Physiol 2012, 2:2829-2870.
    • (2012) Compr Physiol , vol.2 , pp. 2829-2870
    • Adams, G.R.1    Bamman, M.M.2
  • 11
    • 79960925868 scopus 로고    scopus 로고
    • Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
    • Hornberger T.A. Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle. Int J Biochem Cell Biol 2011, 43:1267-1276.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1267-1276
    • Hornberger, T.A.1
  • 13
    • 84867166678 scopus 로고    scopus 로고
    • Mechanical loading and how it affects bone cells: the role of the osteocyte cytoskeleton in maintaining our skeleton
    • Klein-Nulend J., Bacabac R.G., Bakker A.D. Mechanical loading and how it affects bone cells: the role of the osteocyte cytoskeleton in maintaining our skeleton. Eur Cell Mater 2012, 24:278-291.
    • (2012) Eur Cell Mater , vol.24 , pp. 278-291
    • Klein-Nulend, J.1    Bacabac, R.G.2    Bakker, A.D.3
  • 14
    • 70349974398 scopus 로고    scopus 로고
    • Mechanical signaling for bone modeling and remodeling
    • Robling A.G., Turner C.H. Mechanical signaling for bone modeling and remodeling. Cirt Rev Eukaryot Gene Expr 2009, 19:319-338.
    • (2009) Cirt Rev Eukaryot Gene Expr , vol.19 , pp. 319-338
    • Robling, A.G.1    Turner, C.H.2
  • 15
    • 0031278813 scopus 로고    scopus 로고
    • Influence of muscle activity on the forces in the femur: an in vivo study
    • Lu T.W., Taylor S.J., O'Connor J.J., Walker P.S. Influence of muscle activity on the forces in the femur: an in vivo study. J Biomech 1997, 30:1101-1106.
    • (1997) J Biomech , vol.30 , pp. 1101-1106
    • Lu, T.W.1    Taylor, S.J.2    O'Connor, J.J.3    Walker, P.S.4
  • 16
    • 0031243584 scopus 로고    scopus 로고
    • Muscle strength, bone mass, and age-related bone loss
    • Burr D.B. Muscle strength, bone mass, and age-related bone loss. J Bone Miner Res 1997, 12:1547-1551.
    • (1997) J Bone Miner Res , vol.12 , pp. 1547-1551
    • Burr, D.B.1
  • 17
    • 0023766452 scopus 로고
    • Changes in the long bones due to fetal immobility caused by neuromuscular disease. A radiographic and histological study
    • Rodríguez J.I., Garcia-Alix A., Palacios J., Paniagua R. Changes in the long bones due to fetal immobility caused by neuromuscular disease. A radiographic and histological study. J Bone Joint Surg Am 1988, 70:1052-1060.
    • (1988) J Bone Joint Surg Am , vol.70 , pp. 1052-1060
    • Rodríguez, J.I.1    Garcia-Alix, A.2    Palacios, J.3    Paniagua, R.4
  • 18
    • 0024207540 scopus 로고
    • Effects of immobilization on fetal bone development. A morphometric study in newborns with congenital neuromuscular diseases with intrauterine onset
    • Rodríguez J., Palacios J., García-Alix A., Pastor I., Paniagua R. Effects of immobilization on fetal bone development. A morphometric study in newborns with congenital neuromuscular diseases with intrauterine onset. Calcif Tissue Int 1988, 43:335-339.
    • (1988) Calcif Tissue Int , vol.43 , pp. 335-339
    • Rodríguez, J.1    Palacios, J.2    García-Alix, A.3    Pastor, I.4    Paniagua, R.5
  • 19
    • 79960182290 scopus 로고    scopus 로고
    • Muscle force regulates bone shaping for optimal load-bearing capacity during embryogenesis
    • Sharir A., Stern T., Rot C., Shahar R., Zelzer E. Muscle force regulates bone shaping for optimal load-bearing capacity during embryogenesis. Development 2011, 138:3247-3259.
    • (2011) Development , vol.138 , pp. 3247-3259
    • Sharir, A.1    Stern, T.2    Rot, C.3    Shahar, R.4    Zelzer, E.5
  • 20
    • 0025029366 scopus 로고
    • Paralysis and growth of the musculoskeletal system in the embryonic chick
    • Hall B.K., Herring S.W. Paralysis and growth of the musculoskeletal system in the embryonic chick. J Morphol 1990, 206:45-56.
    • (1990) J Morphol , vol.206 , pp. 45-56
    • Hall, B.K.1    Herring, S.W.2
  • 21
    • 77957360491 scopus 로고    scopus 로고
    • Importance of muscle movement for normal craniofacial development
    • Hall J.G. Importance of muscle movement for normal craniofacial development. J Craniofac Surg 2010, 21:1336-1338.
    • (2010) J Craniofac Surg , vol.21 , pp. 1336-1338
    • Hall, J.G.1
  • 23
    • 56749103743 scopus 로고    scopus 로고
    • Peripheral quantitative computed tomography of the proximal radius in young subjects-new reference data and interpretation of results
    • Rauch F., Schoenau E. Peripheral quantitative computed tomography of the proximal radius in young subjects-new reference data and interpretation of results. J Musculoskelet Neuronal Interact 2008, 8:217-226.
    • (2008) J Musculoskelet Neuronal Interact , vol.8 , pp. 217-226
    • Rauch, F.1    Schoenau, E.2
  • 24
    • 78449294917 scopus 로고    scopus 로고
    • Analyses of muscular mass and function: the impact on bone mineral density and peak muscle mass
    • Fricke O., Beccard R., Semler O., Schoenau E. Analyses of muscular mass and function: the impact on bone mineral density and peak muscle mass. Pediatr Nephrol 2010, 25:2393-2400.
    • (2010) Pediatr Nephrol , vol.25 , pp. 2393-2400
    • Fricke, O.1    Beccard, R.2    Semler, O.3    Schoenau, E.4
  • 25
    • 0033962313 scopus 로고    scopus 로고
    • Bone mineral density and fractures in boys with Duchenne muscular dystrophy
    • Larson C.M., Henderson R.C. Bone mineral density and fractures in boys with Duchenne muscular dystrophy. J Pediatr Orthop 2000, 20:71-74.
    • (2000) J Pediatr Orthop , vol.20 , pp. 71-74
    • Larson, C.M.1    Henderson, R.C.2
  • 27
    • 2342482496 scopus 로고    scopus 로고
    • Relationship between the duration of paralysis and bone structure: a pQCT study of spinal cord injured individuals
    • Eser P., Frotzler A., Zehnder Y., Wick L., Knecht H., Denoth J., et al. Relationship between the duration of paralysis and bone structure: a pQCT study of spinal cord injured individuals. Bone 2004, 34:869-880.
    • (2004) Bone , vol.34 , pp. 869-880
    • Eser, P.1    Frotzler, A.2    Zehnder, Y.3    Wick, L.4    Knecht, H.5    Denoth, J.6
  • 28
    • 12344309568 scopus 로고    scopus 로고
    • Cortical and trabecular bone mineral loss from the spine and hip in long-duration spaceflight
    • Lang T., LeBlanc A., Evans H., Lu Y., Genant H., Yu A. Cortical and trabecular bone mineral loss from the spine and hip in long-duration spaceflight. J Bone Miner Res 2004, 19:1006-1012.
    • (2004) J Bone Miner Res , vol.19 , pp. 1006-1012
    • Lang, T.1    LeBlanc, A.2    Evans, H.3    Lu, Y.4    Genant, H.5    Yu, A.6
  • 29
    • 28044444896 scopus 로고    scopus 로고
    • From mechanostat theory to development of the "Functional Muscle-Bone-Unit"
    • Schoenau E. From mechanostat theory to development of the "Functional Muscle-Bone-Unit". J Musculoskelet Neuronal Interact 2005, 5:232-238.
    • (2005) J Musculoskelet Neuronal Interact , vol.5 , pp. 232-238
    • Schoenau, E.1
  • 30
    • 84890435577 scopus 로고    scopus 로고
    • What's in a name revisited: should osteoporosis and sarcopenia be considered components of "dysmobility syndrome?"
    • Binkley N., Krueger D., Buehring B. What's in a name revisited: should osteoporosis and sarcopenia be considered components of "dysmobility syndrome?". Osteoporos Int 2013, 24:2955-2959.
    • (2013) Osteoporos Int , vol.24 , pp. 2955-2959
    • Binkley, N.1    Krueger, D.2    Buehring, B.3
  • 31
    • 80053272231 scopus 로고    scopus 로고
    • Recent progress towards understanding the molecular mechanisms that regulate skeletal muscle mass
    • Goodman C.A., Mayhew D.L., Hornberger T.A. Recent progress towards understanding the molecular mechanisms that regulate skeletal muscle mass. Cell Signal 2011, 23:1896-1906.
    • (2011) Cell Signal , vol.23 , pp. 1896-1906
    • Goodman, C.A.1    Mayhew, D.L.2    Hornberger, T.A.3
  • 32
    • 42049097879 scopus 로고    scopus 로고
    • Role of {beta}-adrenoceptor signaling in skeletal muscle: implications for muscle wasting and disease
    • Lynch G.S., Ryall J.G. Role of {beta}-adrenoceptor signaling in skeletal muscle: implications for muscle wasting and disease. Physiol Rev 2008, 88:729-767.
    • (2008) Physiol Rev , vol.88 , pp. 729-767
    • Lynch, G.S.1    Ryall, J.G.2
  • 33
    • 79952111161 scopus 로고    scopus 로고
    • PI3 kinase regulation of skeletal muscle hypertrophy and atrophy
    • Glass D.J. PI3 kinase regulation of skeletal muscle hypertrophy and atrophy. Curr Top Microbiol Immunol 2010, 346.
    • (2010) Curr Top Microbiol Immunol , vol.346
    • Glass, D.J.1
  • 34
    • 79958767884 scopus 로고    scopus 로고
    • Myostatin: a novel insight into its role in metabolism, signal pathways, and expression regulation
    • Huang Z., Chen X., Chen D. Myostatin: a novel insight into its role in metabolism, signal pathways, and expression regulation. Cell Signal 2011, 23:1441-1446.
    • (2011) Cell Signal , vol.23 , pp. 1441-1446
    • Huang, Z.1    Chen, X.2    Chen, D.3
  • 35
    • 79952722882 scopus 로고    scopus 로고
    • Polyamines, androgens and skeletal muscle hypertrophy
    • Lee N.K.L., MacLean H.E. Polyamines, androgens and skeletal muscle hypertrophy. J Cell Physiol 2011, 226:1453-1460.
    • (2011) J Cell Physiol , vol.226 , pp. 1453-1460
    • Lee, N.K.L.1    MacLean, H.E.2
  • 36
    • 79959935009 scopus 로고    scopus 로고
    • The MyomiR network in skeletal muscle plasticity
    • McCarthy J.J. The MyomiR network in skeletal muscle plasticity. Exerc Sport Sci Rev 2011, 39:150-154.
    • (2011) Exerc Sport Sci Rev , vol.39 , pp. 150-154
    • McCarthy, J.J.1
  • 38
    • 83455215759 scopus 로고    scopus 로고
    • Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
    • Schiaffino S., Mammucari C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle 2011, 1:4.
    • (2011) Skelet Muscle , vol.1 , pp. 4
    • Schiaffino, S.1    Mammucari, C.2
  • 39
    • 84862750154 scopus 로고    scopus 로고
    • CAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration
    • Berdeaux R., Stewart R. cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration. Am J Physiol Endocrinol Metab 2012, 303:E1-E17.
    • (2012) Am J Physiol Endocrinol Metab , vol.303 , pp. E1-E17
    • Berdeaux, R.1    Stewart, R.2
  • 40
    • 84863561473 scopus 로고    scopus 로고
    • Androgens and skeletal muscle: cellular and molecular action mechanisms underlying the anabolic actions
    • Dubois V., Laurent M., Boonen S., Vanderschueren D., Claessens F. Androgens and skeletal muscle: cellular and molecular action mechanisms underlying the anabolic actions. Cell Mol Life Sci 2012, 69:1651-1667.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1651-1667
    • Dubois, V.1    Laurent, M.2    Boonen, S.3    Vanderschueren, D.4    Claessens, F.5
  • 41
    • 84892679130 scopus 로고    scopus 로고
    • Mechanisms of muscle growth and atrophy in mammals and Drosophila
    • Piccirillo R., Demontis F., Perrimon N., Goldberg A.L. Mechanisms of muscle growth and atrophy in mammals and Drosophila. Dev Dyn 2014, 243(2):201-215.
    • (2014) Dev Dyn , vol.243 , Issue.2 , pp. 201-215
    • Piccirillo, R.1    Demontis, F.2    Perrimon, N.3    Goldberg, A.L.4
  • 42
    • 84899475134 scopus 로고    scopus 로고
    • The role of satellite cells in muscle hypertrophy
    • Blaauw B., Reggiani C. The role of satellite cells in muscle hypertrophy. J Muscle Res Cell Motil 2014, 35:3-10.
    • (2014) J Muscle Res Cell Motil , vol.35 , pp. 3-10
    • Blaauw, B.1    Reggiani, C.2
  • 44
    • 84892582312 scopus 로고    scopus 로고
    • Mechano-growth factor peptide, the COOH terminus of unprocessed insulin-like growth factor 1, has no apparent effect on myoblasts or primary muscle stem cells
    • Fornaro M., Hinken A.C., Needle S., Hu E., Trendelenburg A.U., Mayer A., et al. Mechano-growth factor peptide, the COOH terminus of unprocessed insulin-like growth factor 1, has no apparent effect on myoblasts or primary muscle stem cells. Am J Physiol Endocrinol Metab 2015, 306(2):E150-E156.
    • (2015) Am J Physiol Endocrinol Metab , vol.306 , Issue.2 , pp. E150-E156
    • Fornaro, M.1    Hinken, A.C.2    Needle, S.3    Hu, E.4    Trendelenburg, A.U.5    Mayer, A.6
  • 45
    • 34548412555 scopus 로고    scopus 로고
    • Last word on point:counterpoint: satellite cell addition is/is not obligatory for skeletal muscle hypertrophy
    • O'Connor R.S., Pavlath G.K., McCarthy J.J., Esser K.A. Last word on point:counterpoint: satellite cell addition is/is not obligatory for skeletal muscle hypertrophy. J Appl Physiol 2007, 103:1107.
    • (2007) J Appl Physiol , vol.103 , pp. 1107
    • O'Connor, R.S.1    Pavlath, G.K.2    McCarthy, J.J.3    Esser, K.A.4
  • 46
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M., Sabatini David M. mTOR signaling in growth control and disease. Cell 2012, 149:274-293.
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 47
    • 77956697347 scopus 로고    scopus 로고
    • Cell signaling in protein synthesis ribosome biogenesis and translation initiation and elongation
    • Mahoney S.J., Dempsey J.M., Blenis J. Cell signaling in protein synthesis ribosome biogenesis and translation initiation and elongation. Prog Mol Biol Transl Sci 2009, 90C:53-107.
    • (2009) Prog Mol Biol Transl Sci , vol.90C , pp. 53-107
    • Mahoney, S.J.1    Dempsey, J.M.2    Blenis, J.3
  • 48
    • 79954618679 scopus 로고    scopus 로고
    • Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique
    • Goodman C.A., Mabrey D.M., Frey J.W., Miu M.H., Schmidt E.K., Pierre P., et al. Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique. FASEB J 2011, 25:1028-1039.
    • (2011) FASEB J , vol.25 , pp. 1028-1039
    • Goodman, C.A.1    Mabrey, D.M.2    Frey, J.W.3    Miu, M.H.4    Schmidt, E.K.5    Pierre, P.6
  • 49
    • 77956677109 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy
    • Goodman C.A., Miu M.H., Frey J.W., Mabrey D.M., Lincoln H.C., Ge Y., et al. A phosphatidylinositol 3-kinase/protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy. Mol Biol Cell 2010, 21:3258-3268.
    • (2010) Mol Biol Cell , vol.21 , pp. 3258-3268
    • Goodman, C.A.1    Miu, M.H.2    Frey, J.W.3    Mabrey, D.M.4    Lincoln, H.C.5    Ge, Y.6
  • 50
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine S.C., Stitt T.N., Gonzalez M., Kline W.O., Stover G.L., Bauerlein R., et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol 2001, 3:1014-1019.
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3    Kline, W.O.4    Stover, G.L.5    Bauerlein, R.6
  • 51
    • 81255169943 scopus 로고    scopus 로고
    • The role of skeletal muscle mTOR in the regulation of mechanical load-induced growth
    • Goodman C.A., Frey J.W., Mabrey D.M., Jacobs B.L., Lincoln H.C., You J.-S., et al. The role of skeletal muscle mTOR in the regulation of mechanical load-induced growth. J Physiol 2011, 589:5485-5501.
    • (2011) J Physiol , vol.589 , pp. 5485-5501
    • Goodman, C.A.1    Frey, J.W.2    Mabrey, D.M.3    Jacobs, B.L.4    Lincoln, H.C.5    You, J.-S.6
  • 52
    • 0028959316 scopus 로고
    • Collagen and stretch modulate autocrine secretion of insulin-like growth factor-1 and insulin-like growth factor binding proteins from differentiated skeletal muscle cells
    • Perrone C.E., Fenwick-Smith D., Vandenburgh H.H. Collagen and stretch modulate autocrine secretion of insulin-like growth factor-1 and insulin-like growth factor binding proteins from differentiated skeletal muscle cells. J Biol Chem 1995, 270:2099-2106.
    • (1995) J Biol Chem , vol.270 , pp. 2099-2106
    • Perrone, C.E.1    Fenwick-Smith, D.2    Vandenburgh, H.H.3
  • 53
    • 0029798147 scopus 로고    scopus 로고
    • Cloning and characterization of an IGF-1 isoform expressed in skeletal muscle subjected to stretch
    • Yang S., Alnaqeeb M., Simpson H., Goldspink G. Cloning and characterization of an IGF-1 isoform expressed in skeletal muscle subjected to stretch. J Muscle Res Cell Motil 1996, 17:487-495.
    • (1996) J Muscle Res Cell Motil , vol.17 , pp. 487-495
    • Yang, S.1    Alnaqeeb, M.2    Simpson, H.3    Goldspink, G.4
  • 54
    • 0033560860 scopus 로고    scopus 로고
    • Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation
    • McKoy G., Ashley W., Mander J., Yang S.Y., Williams N., Russell B., et al. Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation. J Physiol 1999, 516:583-592.
    • (1999) J Physiol , vol.516 , pp. 583-592
    • McKoy, G.1    Ashley, W.2    Mander, J.3    Yang, S.Y.4    Williams, N.5    Russell, B.6
  • 55
    • 0037440667 scopus 로고    scopus 로고
    • Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise
    • Hameed M., Orrell R.W., Cobbold M., Goldspink G., Harridge S.D. Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise. J Physiol 2003, 547:247-254.
    • (2003) J Physiol , vol.547 , pp. 247-254
    • Hameed, M.1    Orrell, R.W.2    Cobbold, M.3    Goldspink, G.4    Harridge, S.D.5
  • 56
    • 0020640347 scopus 로고
    • Insulin and insulin-like growth factor I. Effects on protein synthesis in isolated muscles from lean and goldthioglucose-obese mice
    • Monier S., Le Cam A., Le Marchand-Brustel Y. Insulin and insulin-like growth factor I. Effects on protein synthesis in isolated muscles from lean and goldthioglucose-obese mice. Diabetes 1983, 32:392-397.
    • (1983) Diabetes , vol.32 , pp. 392-397
    • Monier, S.1    Le Cam, A.2    Le Marchand-Brustel, Y.3
  • 57
    • 0024370493 scopus 로고
    • Regulation of protein synthesis and degradation in L8 myotubes. Effects of serum, insulin and insulin-like growth factors
    • Gulve E.A., Dice J.F. Regulation of protein synthesis and degradation in L8 myotubes. Effects of serum, insulin and insulin-like growth factors. Biochem J 1989, 260:377-387.
    • (1989) Biochem J , vol.260 , pp. 377-387
    • Gulve, E.A.1    Dice, J.F.2
  • 58
    • 0029040848 scopus 로고
    • Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice
    • Coleman M.E., DeMayo F., Yin K.C., Lee H.M., Geske R., Montgomery C., et al. Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice. J Biol Chem 1995, 270:12109-12116.
    • (1995) J Biol Chem , vol.270 , pp. 12109-12116
    • Coleman, M.E.1    DeMayo, F.2    Yin, K.C.3    Lee, H.M.4    Geske, R.5    Montgomery, C.6
  • 59
    • 0032416479 scopus 로고    scopus 로고
    • Viral mediated expression of insulin-like growth factor I blocks the aging-related loss of skeletal muscle function
    • Barton-Davis E.R., Shoturma D.I., Musaro A., Rosenthal N., Sweeney H.L. Viral mediated expression of insulin-like growth factor I blocks the aging-related loss of skeletal muscle function. Proc Natl Acad Sci U S A 1998, 95:15603-15607.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15603-15607
    • Barton-Davis, E.R.1    Shoturma, D.I.2    Musaro, A.3    Rosenthal, N.4    Sweeney, H.L.5
  • 60
    • 0035136062 scopus 로고    scopus 로고
    • Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
    • Musaro A., McCullagh K., Paul A., Houghton L., Dobrowolny G., Molinaro M., et al. Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nat Genet 2001, 27:195-200.
    • (2001) Nat Genet , vol.27 , pp. 195-200
    • Musaro, A.1    McCullagh, K.2    Paul, A.3    Houghton, L.4    Dobrowolny, G.5    Molinaro, M.6
  • 61
    • 0029779604 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and p70 s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I
    • Dardevet D., Sornet C., Vary T., Grizard J. Phosphatidylinositol 3-kinase and p70 s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I. Endocrinology 1996, 137:4087-4094.
    • (1996) Endocrinology , vol.137 , pp. 4087-4094
    • Dardevet, D.1    Sornet, C.2    Vary, T.3    Grizard, J.4
  • 62
    • 0033304652 scopus 로고    scopus 로고
    • Differential effects of insulin-like growth factor I (IGF-I) and IGF-binding protein-1 on protein metabolism in human skeletal muscle cells
    • Frost R.A., Lang C.H. Differential effects of insulin-like growth factor I (IGF-I) and IGF-binding protein-1 on protein metabolism in human skeletal muscle cells. Endocrinology 1999, 140:3962-3970.
    • (1999) Endocrinology , vol.140 , pp. 3962-3970
    • Frost, R.A.1    Lang, C.H.2
  • 63
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel C., Bodine S.C., Clarke B.A., Rossman R., Nunez L., Stitt T.N., et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol 2001, 3:1009-1013.
    • (2001) Nat Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3    Rossman, R.4    Nunez, L.5    Stitt, T.N.6
  • 64
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E., Amini A.R., Amini A.A., Griffiths J., Martin F.J., Wei Y., et al. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 2005, 280:2737-2744.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6
  • 65
    • 23944521632 scopus 로고    scopus 로고
    • Skeletal myocyte hypertrophy requires mTOR kinase activity and S6K1
    • Park I.H., Erbay E., Nuzzi P., Chen J. Skeletal myocyte hypertrophy requires mTOR kinase activity and S6K1. Exp Cell Res 2005, 309:211-219.
    • (2005) Exp Cell Res , vol.309 , pp. 211-219
    • Park, I.H.1    Erbay, E.2    Nuzzi, P.3    Chen, J.4
  • 66
    • 0034987615 scopus 로고    scopus 로고
    • Immunization against IGF-I prevents increases in protein synthesis in diabetic rats after resistance exercise
    • Fedele M.J., Lang C.H., Farrell P.A. Immunization against IGF-I prevents increases in protein synthesis in diabetic rats after resistance exercise. Am J Physiol Endocrinol Metab 2001, 280:E877-E885.
    • (2001) Am J Physiol Endocrinol Metab , vol.280 , pp. E877-E885
    • Fedele, M.J.1    Lang, C.H.2    Farrell, P.A.3
  • 67
    • 0027496895 scopus 로고
    • Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)
    • Liu J.-P., Baker J., Perkins A.S., Robertson E.J., Efstratiadis A. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 1993, 75:59-72.
    • (1993) Cell , vol.75 , pp. 59-72
    • Liu, J.-P.1    Baker, J.2    Perkins, A.S.3    Robertson, E.J.4    Efstratiadis, A.5
  • 68
    • 0034912299 scopus 로고    scopus 로고
    • Insight into skeletal muscle mechanotransduction: MAPK activation is quantitatively related to tension
    • Martineau L.C., Gardiner P.F. Insight into skeletal muscle mechanotransduction: MAPK activation is quantitatively related to tension. J Appl Physiol 2001, 91:693-702.
    • (2001) J Appl Physiol , vol.91 , pp. 693-702
    • Martineau, L.C.1    Gardiner, P.F.2
  • 69
    • 63849130621 scopus 로고    scopus 로고
    • Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis
    • Drummond M.J., Fry C.S., Glynn E.L., Dreyer H.C., Dhanani S., Timmerman K.L., et al. Rapamycin administration in humans blocks the contraction-induced increase in skeletal muscle protein synthesis. J Physiol 2009, 587:1535-1546.
    • (2009) J Physiol , vol.587 , pp. 1535-1546
    • Drummond, M.J.1    Fry, C.S.2    Glynn, E.L.3    Dreyer, H.C.4    Dhanani, S.5    Timmerman, K.L.6
  • 70
    • 66149154339 scopus 로고    scopus 로고
    • Maximal lengthening contractions induce different signaling responses in the type I and type II fibers of human skeletal muscle
    • Tannerstedt J., Apro W., Blomstrand E. Maximal lengthening contractions induce different signaling responses in the type I and type II fibers of human skeletal muscle. J Appl Physiol 2009, 106:1412-1418.
    • (2009) J Appl Physiol , vol.106 , pp. 1412-1418
    • Tannerstedt, J.1    Apro, W.2    Blomstrand, E.3
  • 72
    • 79953152152 scopus 로고    scopus 로고
    • Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3-kinase/Akt signalling
    • Miyazaki M., McCarthy J.J., Fedele M.J., Esser K.A. Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3-kinase/Akt signalling. J Physiol 2011, 589:1831-1846.
    • (2011) J Physiol , vol.589 , pp. 1831-1846
    • Miyazaki, M.1    McCarthy, J.J.2    Fedele, M.J.3    Esser, K.A.4
  • 74
    • 84867525052 scopus 로고    scopus 로고
    • Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism: implications for a direct activation of mTOR by phosphatidic acid
    • You J.S., Frey J.W., Hornberger T.A. Mechanical stimulation induces mTOR signaling via an ERK-independent mechanism: implications for a direct activation of mTOR by phosphatidic acid. PLoS One 2012, 7:e47258.
    • (2012) PLoS One , vol.7 , pp. e47258
    • You, J.S.1    Frey, J.W.2    Hornberger, T.A.3
  • 75
    • 4544384577 scopus 로고    scopus 로고
    • Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase
    • Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J. Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase. Proc Natl Acad Sci U S A 2004, 101:13489-13494.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13489-13494
    • Roux, P.P.1    Ballif, B.A.2    Anjum, R.3    Gygi, S.P.4    Blenis, J.5
  • 76
    • 17444431201 scopus 로고    scopus 로고
    • Phosphorylation and functional inactivation of TSC2 by Erk: implications for tuberous sclerosisand cancer pathogenesis
    • Ma L., Chen Z., Erdjument-Bromage H., Tempst P., Pandolfi P.P. Phosphorylation and functional inactivation of TSC2 by Erk: implications for tuberous sclerosisand cancer pathogenesis. Cell 2005, 121:179-193.
    • (2005) Cell , vol.121 , pp. 179-193
    • Ma, L.1    Chen, Z.2    Erdjument-Bromage, H.3    Tempst, P.4    Pandolfi, P.P.5
  • 77
    • 51049083138 scopus 로고    scopus 로고
    • Signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation
    • Carrière A., Cargnello M., Julien L.-A., Gao H., Bonneil É., Thibault P., et al. Signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation. Curr Biol 2008, 18:1269-1277.
    • (2008) Curr Biol , vol.18 , pp. 1269-1277
    • Carrière, A.1    Cargnello, M.2    Julien, L.-A.3    Gao, H.4    Bonneil, É.5    Thibault, P.6
  • 78
    • 79961011264 scopus 로고    scopus 로고
    • Pharmacological and genetic evaluation of proposed roles of mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK), extracellular signal-regulated kinase (ERK), and p90RSK in the control of mTORC1 protein signaling by phorbol esters
    • Fonseca B.D., Alain T., Finestone L.K., Huang B.P.H., Rolfe M., Jiang T., et al. Pharmacological and genetic evaluation of proposed roles of mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK), extracellular signal-regulated kinase (ERK), and p90RSK in the control of mTORC1 protein signaling by phorbol esters. J Biol Chem 2011, 286:27111-27122.
    • (2011) J Biol Chem , vol.286 , pp. 27111-27122
    • Fonseca, B.D.1    Alain, T.2    Finestone, L.K.3    Huang, B.P.H.4    Rolfe, M.5    Jiang, T.6
  • 79
    • 52449095361 scopus 로고    scopus 로고
    • The RSK family of kinases: emerging roles in cellular signalling
    • Anjum R., Blenis J. The RSK family of kinases: emerging roles in cellular signalling. Nat Rev Mol Cell Biol 2008, 9:747-758.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 747-758
    • Anjum, R.1    Blenis, J.2
  • 80
    • 84902688943 scopus 로고    scopus 로고
    • Activation of ERK by sodium tungstate induces protein synthesis and prevents protein degradation in rat L6 myotubes
    • Salto R., Vílchez J.D., Cabrera E., Guinovart J.J., Girón M.D. Activation of ERK by sodium tungstate induces protein synthesis and prevents protein degradation in rat L6 myotubes. FEBS Lett 2014, 588:2246-2254.
    • (2014) FEBS Lett , vol.588 , pp. 2246-2254
    • Salto, R.1    Vílchez, J.D.2    Cabrera, E.3    Guinovart, J.J.4    Girón, M.D.5
  • 81
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y., Vilella-Bach M., Bachmann R., Flanigan A., Chen J. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 2001, 294:1942-1945.
    • (2001) Science , vol.294 , pp. 1942-1945
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 82
    • 80051917141 scopus 로고    scopus 로고
    • Phosphatidic acid activates mammalian target of rapamycin complex 1 (mTORC1) kinase by displacing FK506 binding protein 38 (FKBP38) and exerting an allosteric effect
    • Yoon M.S., Sun Y., Arauz E., Jiang Y., Chen J. Phosphatidic acid activates mammalian target of rapamycin complex 1 (mTORC1) kinase by displacing FK506 binding protein 38 (FKBP38) and exerting an allosteric effect. J Biol Chem 2011, 286:29568-29574.
    • (2011) J Biol Chem , vol.286 , pp. 29568-29574
    • Yoon, M.S.1    Sun, Y.2    Arauz, E.3    Jiang, Y.4    Chen, J.5
  • 83
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • Avila-Flores A., Santos T., Rincon E., Merida I. Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid. J Biol Chem 2005, 280:10091-10099.
    • (2005) J Biol Chem , vol.280 , pp. 10091-10099
    • Avila-Flores, A.1    Santos, T.2    Rincon, E.3    Merida, I.4
  • 84
    • 33750813851 scopus 로고    scopus 로고
    • Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway
    • Tang W., Yuan J., Chen X., Gu X., Luo K., Li J., et al. Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway. J Biochem Mol Biol 2006, 39:626-635.
    • (2006) J Biochem Mol Biol , vol.39 , pp. 626-635
    • Tang, W.1    Yuan, J.2    Chen, X.3    Gu, X.4    Luo, K.5    Li, J.6
  • 85
    • 67651096033 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase and phosphatidic acid in the regulation of mammalian target of rapamycin following eccentric contractions
    • O'Neil T.K., Duffy L.R., Frey J.W., Hornberger T.A. The role of phosphoinositide 3-kinase and phosphatidic acid in the regulation of mammalian target of rapamycin following eccentric contractions. J Physiol 2009, 587:3691-3701.
    • (2009) J Physiol , vol.587 , pp. 3691-3701
    • O'Neil, T.K.1    Duffy, L.R.2    Frey, J.W.3    Hornberger, T.A.4
  • 86
    • 33846438568 scopus 로고    scopus 로고
    • Regulation of mTOR by phosphatidic acid?
    • Foster D.A. Regulation of mTOR by phosphatidic acid?. Cancer Res 2007, 67:1-4.
    • (2007) Cancer Res , vol.67 , pp. 1-4
    • Foster, D.A.1
  • 87
    • 84880882397 scopus 로고    scopus 로고
    • Phospholipase D regulates the size of skeletal muscle cells through the activation of mTOR signaling
    • Jaafar R., De Larichaudy J., Chanon S., Euthine V., Durand C., Naro F., et al. Phospholipase D regulates the size of skeletal muscle cells through the activation of mTOR signaling. Cell Commun Signal 2013, 11:55.
    • (2013) Cell Commun Signal , vol.11 , pp. 55
    • Jaafar, R.1    De Larichaudy, J.2    Chanon, S.3    Euthine, V.4    Durand, C.5    Naro, F.6
  • 88
    • 84892657844 scopus 로고    scopus 로고
    • The role of diacylglycerol kinase and phosphatidic acid in the mechanical activation of mammalian target of rapamycin (mTOR) signaling and skeletal muscle hypertrophy
    • You J.-S., Lincoln H.C., Kim C.-R., Frey J.W., Goodman C.A., Zhong X.-P., et al. The role of diacylglycerol kinase and phosphatidic acid in the mechanical activation of mammalian target of rapamycin (mTOR) signaling and skeletal muscle hypertrophy. J Biol Chem 2014, 289:1551-1563.
    • (2014) J Biol Chem , vol.289 , pp. 1551-1563
    • You, J.-S.1    Lincoln, H.C.2    Kim, C.-R.3    Frey, J.W.4    Goodman, C.A.5    Zhong, X.-P.6
  • 89
    • 33645241260 scopus 로고    scopus 로고
    • The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle
    • Hornberger T.A., Chu W.K., Mak Y.W., Hsiung J.W., Huang S.A., Chien S. The role of phospholipase D and phosphatidic acid in the mechanical activation of mTOR signaling in skeletal muscle. Proc Natl Acad Sci U S A 2006, 103:4741-4746.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4741-4746
    • Hornberger, T.A.1    Chu, W.K.2    Mak, Y.W.3    Hsiung, J.W.4    Huang, S.A.5    Chien, S.6
  • 90
    • 44449161481 scopus 로고    scopus 로고
    • The TSC1-TSC2 complex: a molecular switchboard controlling cell growth
    • Huang J., Manning B.D. The TSC1-TSC2 complex: a molecular switchboard controlling cell growth. Biochem J 2008, 412:179-190.
    • (2008) Biochem J , vol.412 , pp. 179-190
    • Huang, J.1    Manning, B.D.2
  • 91
    • 3142546236 scopus 로고    scopus 로고
    • The Rheb family of GTP-binding proteins
    • Aspuria P.-J., Tamanoi F. The Rheb family of GTP-binding proteins. Cell Signal 2004, 16:1105-1112.
    • (2004) Cell Signal , vol.16 , pp. 1105-1112
    • Aspuria, P.-J.1    Tamanoi, F.2
  • 93
    • 67649823420 scopus 로고    scopus 로고
    • Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein
    • Sato T., Nakashima A., Guo L., Tamanoi F. Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein. J Biol Chem 2009, 284:12783-12791.
    • (2009) J Biol Chem , vol.284 , pp. 12783-12791
    • Sato, T.1    Nakashima, A.2    Guo, L.3    Tamanoi, F.4
  • 94
    • 0043127125 scopus 로고    scopus 로고
    • Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
    • Inoki K., Li Y., Xu T., Guan K.-L. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev 2003, 17:1829-1834.
    • (2003) Genes Dev , vol.17 , pp. 1829-1834
    • Inoki, K.1    Li, Y.2    Xu, T.3    Guan, K.-L.4
  • 95
    • 0042701991 scopus 로고    scopus 로고
    • Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb
    • Tee A.R., Manning B.D., Roux P.P., Cantley L.C., Blenis J. Tuberous sclerosis complex gene products, tuberin and hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol 2003, 13:1259-1268.
    • (2003) Curr Biol , vol.13 , pp. 1259-1268
    • Tee, A.R.1    Manning, B.D.2    Roux, P.P.3    Cantley, L.C.4    Blenis, J.5
  • 96
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang Y., Gao X., Saucedo L.J., Ru B., Edgar B.A., Pan D. Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat Cell Biol 2003, 5:578-581.
    • (2003) Nat Cell Biol , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 97
    • 84884254389 scopus 로고    scopus 로고
    • Eccentric contractions increase TSC2 phosphorylation and alter the targeting of TSC2 and mTOR to the lysosome
    • Jacobs B.L., You J.-S., Frey J.W., Goodman C.A., Gundermann D.M., Hornberger T.A. Eccentric contractions increase TSC2 phosphorylation and alter the targeting of TSC2 and mTOR to the lysosome. J Physiol 2013, 591:4611-4620.
    • (2013) J Physiol , vol.591 , pp. 4611-4620
    • Jacobs, B.L.1    You, J.-S.2    Frey, J.W.3    Goodman, C.A.4    Gundermann, D.M.5    Hornberger, T.A.6
  • 98
    • 84899471750 scopus 로고    scopus 로고
    • The mechanical activation of mTOR signaling: an emerging role for late endosome/lysosomal targeting
    • Jacobs B.L., Goodman C.A., Hornberger T.A. The mechanical activation of mTOR signaling: an emerging role for late endosome/lysosomal targeting. J Muscle Res Cell Motil 2013, 35:11-21.
    • (2013) J Muscle Res Cell Motil , vol.35 , pp. 11-21
    • Jacobs, B.L.1    Goodman, C.A.2    Hornberger, T.A.3
  • 99
    • 0031937650 scopus 로고    scopus 로고
    • Events of the excitation-contraction-relaxation (E-C-R) cycle in fast- and slow-twitch mammalian muscle fibres relevant to muscle fatigue
    • Stephenson D.G., Lamb G.D., Stephenson G.M. Events of the excitation-contraction-relaxation (E-C-R) cycle in fast- and slow-twitch mammalian muscle fibres relevant to muscle fatigue. Acta Physiol Scand 1998, 162:229-245.
    • (1998) Acta Physiol Scand , vol.162 , pp. 229-245
    • Stephenson, D.G.1    Lamb, G.D.2    Stephenson, G.M.3
  • 101
    • 0025111374 scopus 로고
    • Stretch-sensitive channels in developing muscle cells from a mouse cell line
    • Franco A., Lansman J.B. Stretch-sensitive channels in developing muscle cells from a mouse cell line. J Physiol 1990, 427:361-380.
    • (1990) J Physiol , vol.427 , pp. 361-380
    • Franco, A.1    Lansman, J.B.2
  • 102
    • 0031019664 scopus 로고    scopus 로고
    • An intracellular calcium signal activates p70 but not p90 ribosomal S6 kinase in liver epithelial cells
    • Graves L.M., He Y., Lambert J., Hunter D., Li X., Earp H.S. An intracellular calcium signal activates p70 but not p90 ribosomal S6 kinase in liver epithelial cells. J Biol Chem 1997, 272:1920-1928.
    • (1997) J Biol Chem , vol.272 , pp. 1920-1928
    • Graves, L.M.1    He, Y.2    Lambert, J.3    Hunter, D.4    Li, X.5    Earp, H.S.6
  • 103
    • 0032548942 scopus 로고    scopus 로고
    • Differential regulation by calcium reveals distinct signaling requirements for the activation of Akt and p70S6k
    • Conus N.M., Hemmings B.A., Pearson R.B. Differential regulation by calcium reveals distinct signaling requirements for the activation of Akt and p70S6k. J Biol Chem 1998, 273:4776-4782.
    • (1998) J Biol Chem , vol.273 , pp. 4776-4782
    • Conus, N.M.1    Hemmings, B.A.2    Pearson, R.B.3
  • 104
    • 0018751697 scopus 로고
    • Calcium-dependent regulation of protein synthesis and degradation in muscle
    • Kameyama T., Etlinger J.D. Calcium-dependent regulation of protein synthesis and degradation in muscle. Nature 1979, 279:344-346.
    • (1979) Nature , vol.279 , pp. 344-346
    • Kameyama, T.1    Etlinger, J.D.2
  • 105
    • 41749097424 scopus 로고    scopus 로고
    • Intracellular calcium accumulation following eccentric contractions in rat skeletal muscle in vivo: role of stretch-activated channels
    • Sonobe T., Inagaki T., Poole D.C., Kano Y. Intracellular calcium accumulation following eccentric contractions in rat skeletal muscle in vivo: role of stretch-activated channels. Am J Physiol Regul Integr Comp Physiol 2008, 294:R1329-R1337.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.294 , pp. R1329-R1337
    • Sonobe, T.1    Inagaki, T.2    Poole, D.C.3    Kano, Y.4
  • 106
    • 33644826679 scopus 로고    scopus 로고
    • Inhibition of stretch-activated channels during eccentric muscle contraction attenuates p70S6K activation
    • Spangenburg E.E., McBride T.A. Inhibition of stretch-activated channels during eccentric muscle contraction attenuates p70S6K activation. J Appl Physiol 2006, 100:129-135.
    • (2006) J Appl Physiol , vol.100 , pp. 129-135
    • Spangenburg, E.E.1    McBride, T.A.2
  • 107
    • 84872055469 scopus 로고    scopus 로고
    • Activation of calcium signaling through Trpv1 by nNOS and peroxynitrite as a key trigger of skeletal muscle hypertrophy
    • Ito N., Ruegg U.T., Kudo A., Miyagoe-Suzuki Y., Takeda Si. Activation of calcium signaling through Trpv1 by nNOS and peroxynitrite as a key trigger of skeletal muscle hypertrophy. Nat Med 2013, 19:101-106.
    • (2013) Nat Med , vol.19 , pp. 101-106
    • Ito, N.1    Ruegg, U.T.2    Kudo, A.3    Miyagoe-Suzuki, Y.4    Takeda, S.5
  • 108
    • 84878250751 scopus 로고    scopus 로고
    • Capsaicin mimics mechanical load-induced intracellular signaling events: involvement of TRPV1-mediated calcium signaling in induction of skeletal muscle hypertrophy
    • Ito N., Ruegg U.T., Kudo A., Miyagoe-Suzuki Y., Takeda Si. Capsaicin mimics mechanical load-induced intracellular signaling events: involvement of TRPV1-mediated calcium signaling in induction of skeletal muscle hypertrophy. Channels 2013, 7:221-224.
    • (2013) Channels , vol.7 , pp. 221-224
    • Ito, N.1    Ruegg, U.T.2    Kudo, A.3    Miyagoe-Suzuki, Y.4    Takeda, S.5
  • 109
    • 40949146900 scopus 로고    scopus 로고
    • Normal hypertrophy accompanied by phosphoryation and activation of AMP-activated protein kinase α1 following overload in LKB1 knockout mice
    • McGee S.L., Mustard K.J., Hardie D.G., Baar K. Normal hypertrophy accompanied by phosphoryation and activation of AMP-activated protein kinase α1 following overload in LKB1 knockout mice. J Physiol 2008, 586:1731-1741.
    • (2008) J Physiol , vol.586 , pp. 1731-1741
    • McGee, S.L.1    Mustard, K.J.2    Hardie, D.G.3    Baar, K.4
  • 110
    • 84908052787 scopus 로고    scopus 로고
    • Constitutive activation of CaMKKα signaling is sufficient but not necessary for mTORC1 activation and growth in mouse skeletal muscle
    • [2014; in press]
    • Ferey J.L.A., Brault J.J., Smith C.A.S., Witczak C.A. Constitutive activation of CaMKKα signaling is sufficient but not necessary for mTORC1 activation and growth in mouse skeletal muscle. Am J Physiol Endocrinol Metab 2015, [2014; in press]. 10.1152/ajpendo.00322.2014.
    • (2015) Am J Physiol Endocrinol Metab
    • Ferey, J.L.A.1    Brault, J.J.2    Smith, C.A.S.3    Witczak, C.A.4
  • 111
    • 33750058023 scopus 로고    scopus 로고
    • Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?
    • Corradetti M.N., Guan K.L. Upstream of the mammalian target of rapamycin: do all roads pass through mTOR?. Oncogene 2006, 25:6347-6360.
    • (2006) Oncogene , vol.25 , pp. 6347-6360
    • Corradetti, M.N.1    Guan, K.L.2
  • 112
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production
    • Powers S.K., Jackson M.J. Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol Rev 2008, 88:1243-1276.
    • (2008) Physiol Rev , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2
  • 113
    • 0036088330 scopus 로고    scopus 로고
    • Involvement of nitric oxide synthase in skeletal muscle adaptation to chronic overload
    • Smith L.W., Smith J.D., Criswell D.S. Involvement of nitric oxide synthase in skeletal muscle adaptation to chronic overload. J Appl Physiol 2002, 92:2005-2011.
    • (2002) J Appl Physiol , vol.92 , pp. 2005-2011
    • Smith, L.W.1    Smith, J.D.2    Criswell, D.S.3
  • 116
    • 34848913758 scopus 로고    scopus 로고
    • NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS
    • Suzuki N., Motohashi N., Uezumi A., Fukada S.-I., Yoshimura T., Itoyama Y., et al. NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J Clin Invest 2007, 117:2468-2476.
    • (2007) J Clin Invest , vol.117 , pp. 2468-2476
    • Suzuki, N.1    Motohashi, N.2    Uezumi, A.3    Fukada, S.-I.4    Yoshimura, T.5    Itoyama, Y.6
  • 119
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010, 141:290-303.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 121
    • 84865592978 scopus 로고    scopus 로고
    • Amino acids and mTORC1: from lysosomes to disease
    • Efeyan A., Zoncu R., Sabatini D.M. Amino acids and mTORC1: from lysosomes to disease. Trends Mol Med 2012, 18:524-533.
    • (2012) Trends Mol Med , vol.18 , pp. 524-533
    • Efeyan, A.1    Zoncu, R.2    Sabatini, D.M.3
  • 122
    • 0033808169 scopus 로고    scopus 로고
    • Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway
    • Anthony J.C., Yoshizawa F., Anthony T.G., Vary T.C., Jefferson L.S., Kimball S.R. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J Nutr 2000, 130:2413-2419.
    • (2000) J Nutr , vol.130 , pp. 2413-2419
    • Anthony, J.C.1    Yoshizawa, F.2    Anthony, T.G.3    Vary, T.C.4    Jefferson, L.S.5    Kimball, S.R.6
  • 123
    • 79955486262 scopus 로고    scopus 로고
    • Mammalian target of rapamycin complex 1 activation is required for the stimulation of human skeletal muscle protein synthesis by essential amino acids
    • Dickinson J.M., Fry C.S., Drummond M.J., Gundermann D.M., Walker D.K., Glynn E.L., et al. Mammalian target of rapamycin complex 1 activation is required for the stimulation of human skeletal muscle protein synthesis by essential amino acids. J Nutr 2011, 141:856-862.
    • (2011) J Nutr , vol.141 , pp. 856-862
    • Dickinson, J.M.1    Fry, C.S.2    Drummond, M.J.3    Gundermann, D.M.4    Walker, D.K.5    Glynn, E.L.6
  • 126
    • 79959445342 scopus 로고    scopus 로고
    • The actions of exogenous leucine on mTOR signalling and amino acid transporters in human myotubes
    • Gran P., Cameron-Smith D. The actions of exogenous leucine on mTOR signalling and amino acid transporters in human myotubes. BMC Physiol 2011, 11:10.
    • (2011) BMC Physiol , vol.11 , pp. 10
    • Gran, P.1    Cameron-Smith, D.2
  • 127
    • 79960387847 scopus 로고    scopus 로고
    • Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1)
    • Xu L., Salloum D., Medlin P.S., Saqcena M., Yellen P., Perrella B., et al. Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1). J Biol Chem 2011, 286:25477-25486.
    • (2011) J Biol Chem , vol.286 , pp. 25477-25486
    • Xu, L.1    Salloum, D.2    Medlin, P.S.3    Saqcena, M.4    Yellen, P.5    Perrella, B.6
  • 128
    • 84855731134 scopus 로고    scopus 로고
    • Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway
    • Yoon M.-S., Du G., Backer J.M., Frohman M.A., Chen J. Class III PI-3-kinase activates phospholipase D in an amino acid-sensing mTORC1 pathway. J Cell Biol 2011, 195:435-447.
    • (2011) J Cell Biol , vol.195 , pp. 435-447
    • Yoon, M.-S.1    Du, G.2    Backer, J.M.3    Frohman, M.A.4    Chen, J.5
  • 129
    • 85002667363 scopus 로고    scopus 로고
    • Dose-dependent increases in p70S6K phosphorylation and intramuscular branched-chain amino acids in older men following resistance exercise and protein intake
    • D'Souza R.F., Marworth J.F., Figueiredo V.C., Della Gatta P.A., Petersen A.C., Mitchell C.J., et al. Dose-dependent increases in p70S6K phosphorylation and intramuscular branched-chain amino acids in older men following resistance exercise and protein intake. Physiol Rep 2014, 2.
    • (2014) Physiol Rep , vol.2
    • D'Souza, R.F.1    Marworth, J.F.2    Figueiredo, V.C.3    Della Gatta, P.A.4    Petersen, A.C.5    Mitchell, C.J.6
  • 131
    • 37249057821 scopus 로고    scopus 로고
    • Osteocytes as dynamic multifunctional cells
    • Bonewald L.F. Osteocytes as dynamic multifunctional cells. Ann N Y Acad Sci 2007, 1116:281-290.
    • (2007) Ann N Y Acad Sci , vol.1116 , pp. 281-290
    • Bonewald, L.F.1
  • 132
    • 33644512051 scopus 로고    scopus 로고
    • Generation and function of osteocyte dendritic processes
    • Bonewald L.F. Generation and function of osteocyte dendritic processes. J Musculoskelet Neuronal Interact 2005, 5:321-324.
    • (2005) J Musculoskelet Neuronal Interact , vol.5 , pp. 321-324
    • Bonewald, L.F.1
  • 133
    • 0027199847 scopus 로고
    • Osteocytes, strain detection, bone modeling and remodeling
    • [discussion S106-7]
    • Lanyon L.E. Osteocytes, strain detection, bone modeling and remodeling. Calcif Tissue Int 1993, 53(Suppl. 1):S102-S106. [discussion S106-7].
    • (1993) Calcif Tissue Int , vol.53 , pp. S102-S106
    • Lanyon, L.E.1
  • 135
    • 84875823720 scopus 로고    scopus 로고
    • Gap junction and hemichannel functions in osteocytes
    • Loiselle A.E., Jiang J.X., Donahue H.J. Gap junction and hemichannel functions in osteocytes. Bone 2013, 54:205-212.
    • (2013) Bone , vol.54 , pp. 205-212
    • Loiselle, A.E.1    Jiang, J.X.2    Donahue, H.J.3
  • 136
    • 77955301116 scopus 로고    scopus 로고
    • Osteocyte remodeling of the perilacunar and pericanalicular matrix
    • Qing H., Bonewald L.F. Osteocyte remodeling of the perilacunar and pericanalicular matrix. Int J Oral Sci 2009, 1:59-65.
    • (2009) Int J Oral Sci , vol.1 , pp. 59-65
    • Qing, H.1    Bonewald, L.F.2
  • 138
    • 68849117424 scopus 로고    scopus 로고
    • Identification of differentially expressed genes between osteoblasts and osteocytes
    • Paic F., Igwe J.C., Nori R., Kronenberg M.S., Franceschetti T., Harrington P., et al. Identification of differentially expressed genes between osteoblasts and osteocytes. Bone 2009, 45:682-692.
    • (2009) Bone , vol.45 , pp. 682-692
    • Paic, F.1    Igwe, J.C.2    Nori, R.3    Kronenberg, M.S.4    Franceschetti, T.5    Harrington, P.6
  • 139
    • 16644367867 scopus 로고    scopus 로고
    • Estimating the sensitivity of mechanosensitive ion channels to membrane strain and tension
    • Charras G.T., Williams B.A., Sims S.M., Horton M.A. Estimating the sensitivity of mechanosensitive ion channels to membrane strain and tension. Biophys J 2004, 87:2870-2884.
    • (2004) Biophys J , vol.87 , pp. 2870-2884
    • Charras, G.T.1    Williams, B.A.2    Sims, S.M.3    Horton, M.A.4
  • 140
    • 84937028361 scopus 로고    scopus 로고
    • Inserted rest period resensitizes MC3T3-E1 cells to fluid shear stress in a time-dependent manner via F-actin-regulated mechanosensitive channel(s)
    • Gong X., Fan Y., Zhang Y., Luo C., Duan X., Yang L., et al. Inserted rest period resensitizes MC3T3-E1 cells to fluid shear stress in a time-dependent manner via F-actin-regulated mechanosensitive channel(s). Biosci Biotechnol Biochem 2014, 78:565-573.
    • (2014) Biosci Biotechnol Biochem , vol.78 , pp. 565-573
    • Gong, X.1    Fan, Y.2    Zhang, Y.3    Luo, C.4    Duan, X.5    Yang, L.6
  • 141
    • 0034086263 scopus 로고    scopus 로고
    • Ca(2+) regulates fluid shear-induced cytoskeletal reorganization and gene expression in osteoblasts
    • Chen N.X., Ryder K.D., Pavalko F.M., Turner C.H., Burr D.B., Qiu J., et al. Ca(2+) regulates fluid shear-induced cytoskeletal reorganization and gene expression in osteoblasts. Am J Physiol Cell Physiol 2000, 278:C989-C997.
    • (2000) Am J Physiol Cell Physiol , vol.278 , pp. C989-C997
    • Chen, N.X.1    Ryder, K.D.2    Pavalko, F.M.3    Turner, C.H.4    Burr, D.B.5    Qiu, J.6
  • 142
    • 0035143357 scopus 로고    scopus 로고
    • Parathyroid hormone enhances fluid shear-induced [Ca2+]i signaling in osteoblastic cells through activation of mechanosensitive and voltage-sensitive Ca2+ channels
    • Ryder K.D., Duncan R.L. Parathyroid hormone enhances fluid shear-induced [Ca2+]i signaling in osteoblastic cells through activation of mechanosensitive and voltage-sensitive Ca2+ channels. J Bone Miner Res 2001, 16:240-248.
    • (2001) J Bone Miner Res , vol.16 , pp. 240-248
    • Ryder, K.D.1    Duncan, R.L.2
  • 143
    • 84873836628 scopus 로고    scopus 로고
    • The involvement of TRP channels in bone homeostasis
    • Lieben L., Carmeliet G. The involvement of TRP channels in bone homeostasis. Front Endocrinol (Lausanne) 2012, 3:99.
    • (2012) Front Endocrinol (Lausanne) , vol.3 , pp. 99
    • Lieben, L.1    Carmeliet, G.2
  • 144
    • 77950648327 scopus 로고    scopus 로고
    • Transient receptor potential vanilloid 4: the sixth sense of the musculoskeletal system?
    • Guilak F., Leddy H.A., Liedtke W. Transient receptor potential vanilloid 4: the sixth sense of the musculoskeletal system?. Ann N Y Acad Sci 2010, 1192:404-409.
    • (2010) Ann N Y Acad Sci , vol.1192 , pp. 404-409
    • Guilak, F.1    Leddy, H.A.2    Liedtke, W.3
  • 146
    • 44449142487 scopus 로고    scopus 로고
    • Transient receptor potential vanilloid 4 deficiency suppresses unloading-induced bone loss
    • Mizoguchi F., Mizuno A., Hayata T., Nakashima K., Heller S., Ushida T., et al. Transient receptor potential vanilloid 4 deficiency suppresses unloading-induced bone loss. J Cell Physiol 2008, 216:47-53.
    • (2008) J Cell Physiol , vol.216 , pp. 47-53
    • Mizoguchi, F.1    Mizuno, A.2    Hayata, T.3    Nakashima, K.4    Heller, S.5    Ushida, T.6
  • 147
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • Nauli S.M., Alenghat F.J., Luo Y., Williams E., Vassilev P., Li X., et al. Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 2003, 33:129-137.
    • (2003) Nat Genet , vol.33 , pp. 129-137
    • Nauli, S.M.1    Alenghat, F.J.2    Luo, Y.3    Williams, E.4    Vassilev, P.5    Li, X.6
  • 148
    • 84901439340 scopus 로고    scopus 로고
    • From the cytoplasm into the cilium: bon voyage
    • Malicki J., Avidor-Reiss T. From the cytoplasm into the cilium: bon voyage. Organogenesis 2014, 10:138-157.
    • (2014) Organogenesis , vol.10 , pp. 138-157
    • Malicki, J.1    Avidor-Reiss, T.2
  • 149
    • 77956261961 scopus 로고    scopus 로고
    • Polycystins and renovascular mechanosensory transduction
    • Patel A., Honore E. Polycystins and renovascular mechanosensory transduction. Nat Rev Nephrol 2010, 6:530-538.
    • (2010) Nat Rev Nephrol , vol.6 , pp. 530-538
    • Patel, A.1    Honore, E.2
  • 150
    • 79960169162 scopus 로고    scopus 로고
    • Conditional deletion of Pkd1 in osteocytes disrupts skeletal mechanosensing in mice
    • Xiao Z., Dallas M., Qiu N., Nicolella D., Cao L., Johnson M., et al. Conditional deletion of Pkd1 in osteocytes disrupts skeletal mechanosensing in mice. FASEB J 2011, 25:2418-2432.
    • (2011) FASEB J , vol.25 , pp. 2418-2432
    • Xiao, Z.1    Dallas, M.2    Qiu, N.3    Nicolella, D.4    Cao, L.5    Johnson, M.6
  • 151
    • 84897541931 scopus 로고    scopus 로고
    • Polycystin-1 mediates mechanical strain-induced osteoblastic mechanoresponses via potentiation of intracellular calcium and Akt/beta-catenin pathway
    • Wang H., Sun W., Ma J., Pan Y., Wang L., Zhang W. Polycystin-1 mediates mechanical strain-induced osteoblastic mechanoresponses via potentiation of intracellular calcium and Akt/beta-catenin pathway. PLoS One 2014, 9:e91730.
    • (2014) PLoS One , vol.9 , pp. e91730
    • Wang, H.1    Sun, W.2    Ma, J.3    Pan, Y.4    Wang, L.5    Zhang, W.6
  • 153
    • 84890890929 scopus 로고    scopus 로고
    • Functional selectivity of GPCR signaling in animals
    • Zhou L., Bohn L.M. Functional selectivity of GPCR signaling in animals. Curr Opin Cell Biol 2014, 27:102-108.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 102-108
    • Zhou, L.1    Bohn, L.M.2
  • 154
    • 0031046164 scopus 로고    scopus 로고
    • Activation of G proteins mediates flow-induced prostaglandin E2 production in osteoblasts
    • Reich K.M., McAllister T.N., Gudi S., Frangos J.A. Activation of G proteins mediates flow-induced prostaglandin E2 production in osteoblasts. Endocrinology 1997, 138:1014-1018.
    • (1997) Endocrinology , vol.138 , pp. 1014-1018
    • Reich, K.M.1    McAllister, T.N.2    Gudi, S.3    Frangos, J.A.4
  • 155
    • 33750366860 scopus 로고    scopus 로고
    • G protein-coupled receptors sense fluid shear stress in endothelial cells
    • Chachisvilis M., Zhang Y.L., Frangos J.A. G protein-coupled receptors sense fluid shear stress in endothelial cells. Proc Natl Acad Sci U S A 2006, 103:15463-15468.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15463-15468
    • Chachisvilis, M.1    Zhang, Y.L.2    Frangos, J.A.3
  • 156
    • 66749151000 scopus 로고    scopus 로고
    • Mechanical stimulus alters conformation of type 1 parathyroid hormone receptor in bone cells
    • Zhang Y.L., Frangos J.A., Chachisvilis M. Mechanical stimulus alters conformation of type 1 parathyroid hormone receptor in bone cells. Am J Physiol Cell Physiol 2009, 296:C1391-C1399.
    • (2009) Am J Physiol Cell Physiol , vol.296 , pp. C1391-C1399
    • Zhang, Y.L.1    Frangos, J.A.2    Chachisvilis, M.3
  • 157
    • 0032478310 scopus 로고    scopus 로고
    • Modulation of GTPase activity of G proteins by fluid shear stress and phospholipid composition
    • Gudi S., Nolan J.P., Frangos J.A. Modulation of GTPase activity of G proteins by fluid shear stress and phospholipid composition. Proc Natl Acad Sci U S A 1998, 95:2515-2519.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2515-2519
    • Gudi, S.1    Nolan, J.P.2    Frangos, J.A.3
  • 158
    • 84873127246 scopus 로고    scopus 로고
    • Prostanoids receptors signaling in different diseases/cancers progression
    • Yang Y., Tang L.Q., Wei W. Prostanoids receptors signaling in different diseases/cancers progression. J Recept Signal Transduct Res 2013, 33:14-27.
    • (2013) J Recept Signal Transduct Res , vol.33 , pp. 14-27
    • Yang, Y.1    Tang, L.Q.2    Wei, W.3
  • 159
    • 0029807755 scopus 로고    scopus 로고
    • In situ microdialysis in bone tissue. Stimulation of prostaglandin E2 release by weight-bearing mechanical loading
    • Thorsen K., Kristoffersson A.O., Lerner U.H., Lorentzon R.P. In situ microdialysis in bone tissue. Stimulation of prostaglandin E2 release by weight-bearing mechanical loading. J Clin Invest 1996, 98:2446-2449.
    • (1996) J Clin Invest , vol.98 , pp. 2446-2449
    • Thorsen, K.1    Kristoffersson, A.O.2    Lerner, U.H.3    Lorentzon, R.P.4
  • 160
    • 0031593465 scopus 로고    scopus 로고
    • Localisation of prostaglandin endoperoxide H synthase (PGHS)-1 and PGHS-2 in bone following mechanical loading in vivo
    • Forwood M.R., Kelly W.L., Worth N.F. Localisation of prostaglandin endoperoxide H synthase (PGHS)-1 and PGHS-2 in bone following mechanical loading in vivo. Anat Rec 1998, 252:580-586.
    • (1998) Anat Rec , vol.252 , pp. 580-586
    • Forwood, M.R.1    Kelly, W.L.2    Worth, N.F.3
  • 161
    • 0029998565 scopus 로고    scopus 로고
    • Inducible cyclo-oxygenase (COX-2) mediates the induction of bone formation by mechanical loading in vivo
    • Forwood M.R. Inducible cyclo-oxygenase (COX-2) mediates the induction of bone formation by mechanical loading in vivo. J Bone Miner Res 1996, 11:1688-1693.
    • (1996) J Bone Miner Res , vol.11 , pp. 1688-1693
    • Forwood, M.R.1
  • 162
    • 0036551229 scopus 로고    scopus 로고
    • Suppression of prostaglandin synthesis with NS-398 has different effects on endocortical and periosteal bone formation induced by mechanical loading
    • Li J., Burr D.B., Turner C.H. Suppression of prostaglandin synthesis with NS-398 has different effects on endocortical and periosteal bone formation induced by mechanical loading. Calcif Tissue Int 2002, 70:320-329.
    • (2002) Calcif Tissue Int , vol.70 , pp. 320-329
    • Li, J.1    Burr, D.B.2    Turner, C.H.3
  • 163
    • 84891351252 scopus 로고    scopus 로고
    • Prostaglandin E2 modulates F-actin stress fiber in FSS-stimulated MC3T3-E1 cells in a PKA-dependent manner
    • Gong X., Yang W., Wang L., Duncan R.L., Pan J. Prostaglandin E2 modulates F-actin stress fiber in FSS-stimulated MC3T3-E1 cells in a PKA-dependent manner. Acta Biochim Biophys Sin (Shanghai) 2014, 46:40-47.
    • (2014) Acta Biochim Biophys Sin (Shanghai) , vol.46 , pp. 40-47
    • Gong, X.1    Yang, W.2    Wang, L.3    Duncan, R.L.4    Pan, J.5
  • 165
    • 84885415693 scopus 로고    scopus 로고
    • The responses of osteoblasts to fluid shear stress depend on substrate chemistries
    • Li Y., Luo Y., Huang K., Xing J., Xie Z., Lin M., et al. The responses of osteoblasts to fluid shear stress depend on substrate chemistries. Arch Biochem Biophys 2013, 539:38-50.
    • (2013) Arch Biochem Biophys , vol.539 , pp. 38-50
    • Li, Y.1    Luo, Y.2    Huang, K.3    Xing, J.4    Xie, Z.5    Lin, M.6
  • 166
    • 84857738933 scopus 로고    scopus 로고
    • Mechanical stress-activated integrin alpha5beta1 induces opening of connexin 43 hemichannels
    • Batra N., Burra S., Siller-Jackson A.J., Gu S., Xia X., Weber G.F., et al. Mechanical stress-activated integrin alpha5beta1 induces opening of connexin 43 hemichannels. Proc Natl Acad Sci U S A 2012, 109:3359-3364.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 3359-3364
    • Batra, N.1    Burra, S.2    Siller-Jackson, A.J.3    Gu, S.4    Xia, X.5    Weber, G.F.6
  • 167
    • 40849111180 scopus 로고    scopus 로고
    • Activation of extracellular-signal regulated kinase (ERK1/2) by fluid shear is Ca(2+)- and ATP-dependent in MC3T3-E1 osteoblasts
    • Liu D., Genetos D.C., Shao Y., Geist D.J., Li J., Ke H.Z., et al. Activation of extracellular-signal regulated kinase (ERK1/2) by fluid shear is Ca(2+)- and ATP-dependent in MC3T3-E1 osteoblasts. Bone 2008, 42:644-652.
    • (2008) Bone , vol.42 , pp. 644-652
    • Liu, D.1    Genetos, D.C.2    Shao, Y.3    Geist, D.J.4    Li, J.5    Ke, H.Z.6
  • 168
    • 30044443068 scopus 로고    scopus 로고
    • The P2X7 nucleotide receptor mediates skeletal mechanotransduction
    • Li J., Liu D., Ke H.Z., Duncan R.L., Turner C.H. The P2X7 nucleotide receptor mediates skeletal mechanotransduction. J Biol Chem 2005, 280:42952-42959.
    • (2005) J Biol Chem , vol.280 , pp. 42952-42959
    • Li, J.1    Liu, D.2    Ke, H.Z.3    Duncan, R.L.4    Turner, C.H.5
  • 169
    • 79960922344 scopus 로고    scopus 로고
    • Sost down-regulation by mechanical strain in human osteoblastic cells involves PGE2 signaling via EP4
    • Galea G.L., Sunters A., Meakin L.B., Zaman G., Sugiyama T., Lanyon L.E., et al. Sost down-regulation by mechanical strain in human osteoblastic cells involves PGE2 signaling via EP4. FEBS Lett 2011, 585:2450-2454.
    • (2011) FEBS Lett , vol.585 , pp. 2450-2454
    • Galea, G.L.1    Sunters, A.2    Meakin, L.B.3    Zaman, G.4    Sugiyama, T.5    Lanyon, L.E.6
  • 170
    • 34648828632 scopus 로고    scopus 로고
    • Effect of compressive force on the production of prostaglandin E(2) and its receptors in osteoblastic Saos-2 cells
    • Sanuki R., Mitsui N., Suzuki N., Koyama Y., Yamaguchi A., Isokawa K., et al. Effect of compressive force on the production of prostaglandin E(2) and its receptors in osteoblastic Saos-2 cells. Connect Tissue Res 2007, 48:246-253.
    • (2007) Connect Tissue Res , vol.48 , pp. 246-253
    • Sanuki, R.1    Mitsui, N.2    Suzuki, N.3    Koyama, Y.4    Yamaguchi, A.5    Isokawa, K.6
  • 171
    • 40849106249 scopus 로고    scopus 로고
    • Osteocytes, mechanosensing and Wnt signaling
    • Bonewald L.F., Johnson M.L. Osteocytes, mechanosensing and Wnt signaling. Bone 2008, 42:606-615.
    • (2008) Bone , vol.42 , pp. 606-615
    • Bonewald, L.F.1    Johnson, M.L.2
  • 172
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling and disease
    • Clevers H., Nusse R. Wnt/beta-catenin signaling and disease. Cell 2012, 149:1192-1205.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 173
    • 33644813850 scopus 로고    scopus 로고
    • Regulation of Wnt signaling by protein-protein interaction and post-translational modifications
    • Kikuchi A., Kishida S., Yamamoto H. Regulation of Wnt signaling by protein-protein interaction and post-translational modifications. Exp Mol Med 2006, 38:1-10.
    • (2006) Exp Mol Med , vol.38 , pp. 1-10
    • Kikuchi, A.1    Kishida, S.2    Yamamoto, H.3
  • 174
    • 20844449569 scopus 로고    scopus 로고
    • TOPGAL mice show that the canonical Wnt signaling pathway is active during bone development and growth and is activated by mechanical loading in vitro
    • Hens J.R., Wilson K.M., Dann P., Chen X., Horowitz M.C., Wysolmerski J.J. TOPGAL mice show that the canonical Wnt signaling pathway is active during bone development and growth and is activated by mechanical loading in vitro. J Bone Miner Res 2005, 20:1103-1113.
    • (2005) J Bone Miner Res , vol.20 , pp. 1103-1113
    • Hens, J.R.1    Wilson, K.M.2    Dann, P.3    Chen, X.4    Horowitz, M.C.5    Wysolmerski, J.J.6
  • 176
    • 77957755212 scopus 로고    scopus 로고
    • Activation of beta-catenin signaling in MLO-Y4 osteocytic cells versus 2T3 osteoblastic cells by fluid flow shear stress and PGE2: implications for the study of mechanosensation in bone
    • Kamel M.A., Picconi J.L., Lara-Castillo N., Johnson M.L. Activation of beta-catenin signaling in MLO-Y4 osteocytic cells versus 2T3 osteoblastic cells by fluid flow shear stress and PGE2: implications for the study of mechanosensation in bone. Bone 2010, 47:872-881.
    • (2010) Bone , vol.47 , pp. 872-881
    • Kamel, M.A.1    Picconi, J.L.2    Lara-Castillo, N.3    Johnson, M.L.4
  • 177
    • 33747674263 scopus 로고    scopus 로고
    • The Wnt co-receptor LRP5 is essential for skeletal mechanotransduction but not for the anabolic bone response to parathyroid hormone treatment
    • Sawakami K., Robling A.G., Ai M., Pitner N.D., Liu D., Warden S.J., et al. The Wnt co-receptor LRP5 is essential for skeletal mechanotransduction but not for the anabolic bone response to parathyroid hormone treatment. J Biol Chem 2006, 281:23698-23711.
    • (2006) J Biol Chem , vol.281 , pp. 23698-23711
    • Sawakami, K.1    Robling, A.G.2    Ai, M.3    Pitner, N.D.4    Liu, D.5    Warden, S.J.6
  • 178
    • 79958772955 scopus 로고    scopus 로고
    • Analysis of multiple bone responses to graded strains above functional levels, and to disuse, in mice in vivo show that the human Lrp5 G171V High Bone Mass mutation increases the osteogenic response to loading but that lack of Lrp5 activity reduces it
    • Saxon L.K., Jackson B.F., Sugiyama T., Lanyon L.E., Price J.S. Analysis of multiple bone responses to graded strains above functional levels, and to disuse, in mice in vivo show that the human Lrp5 G171V High Bone Mass mutation increases the osteogenic response to loading but that lack of Lrp5 activity reduces it. Bone 2011, 49:184-193.
    • (2011) Bone , vol.49 , pp. 184-193
    • Saxon, L.K.1    Jackson, B.F.2    Sugiyama, T.3    Lanyon, L.E.4    Price, J.S.5
  • 179
    • 41949089764 scopus 로고    scopus 로고
    • Mechanical stimulation of bone in vivo reduces osteocyte expression of Sost/sclerostin
    • Robling A.G., Niziolek P.J., Baldridge L.A., Condon K.W., Allen M.R., Alam I., et al. Mechanical stimulation of bone in vivo reduces osteocyte expression of Sost/sclerostin. J Biol Chem 2008, 283:5866-5875.
    • (2008) J Biol Chem , vol.283 , pp. 5866-5875
    • Robling, A.G.1    Niziolek, P.J.2    Baldridge, L.A.3    Condon, K.W.4    Allen, M.R.5    Alam, I.6
  • 180
    • 81155148568 scopus 로고    scopus 로고
    • Sost downregulation and local Wnt signaling are required for the osteogenic response to mechanical loading
    • Tu X., Rhee Y., Condon K.W., Bivi N., Allen M.R., Dwyer D., et al. Sost downregulation and local Wnt signaling are required for the osteogenic response to mechanical loading. Bone 2012, 50:209-217.
    • (2012) Bone , vol.50 , pp. 209-217
    • Tu, X.1    Rhee, Y.2    Condon, K.W.3    Bivi, N.4    Allen, M.R.5    Dwyer, D.6
  • 182
    • 70349934212 scopus 로고    scopus 로고
    • Sclerostin Mediates bone response to mechanical unloading through antagonizing Wnt/β-catenin signaling
    • Lin C., Jiang X., Dai Z., Guo X., Weng T., Wang J., et al. Sclerostin Mediates bone response to mechanical unloading through antagonizing Wnt/β-catenin signaling. J Bone Miner Res 2009, 24:1651-1661.
    • (2009) J Bone Miner Res , vol.24 , pp. 1651-1661
    • Lin, C.1    Jiang, X.2    Dai, Z.3    Guo, X.4    Weng, T.5    Wang, J.6
  • 183
  • 184
    • 84867477893 scopus 로고    scopus 로고
    • Disruption of the insulin-like growth factor-1 gene in osteocytes impairs developmental bone growth in mice
    • Sheng M.H.C., Zhou X.-D., Bonewald L.F., Baylink D.J., Lau K.H.W. Disruption of the insulin-like growth factor-1 gene in osteocytes impairs developmental bone growth in mice. Bone 2013, 52:133-144.
    • (2013) Bone , vol.52 , pp. 133-144
    • Sheng, M.H.C.1    Zhou, X.-D.2    Bonewald, L.F.3    Baylink, D.J.4    Lau, K.H.W.5
  • 186
    • 33947377168 scopus 로고    scopus 로고
    • Effect of mechanical loading on insulin-like growth factor-I gene expression in rat tibia
    • Reijnders C.M.A., Bravenboer N., Tromp A.M., Blankenstein M.A., Lips P. Effect of mechanical loading on insulin-like growth factor-I gene expression in rat tibia. J Endocrinol 2007, 192:131-140.
    • (2007) J Endocrinol , vol.192 , pp. 131-140
    • Reijnders, C.M.A.1    Bravenboer, N.2    Tromp, A.M.3    Blankenstein, M.A.4    Lips, P.5
  • 187
    • 0028929151 scopus 로고
    • Increased insulin-like growth factor I mRNA expression in rat osteocytes in response to mechanical stimulation
    • Lean J.M., Jagger C.J., Chambers T.J., Chow J.W. Increased insulin-like growth factor I mRNA expression in rat osteocytes in response to mechanical stimulation. Am J Physiol 1995, 268:E318-E327.
    • (1995) Am J Physiol , vol.268 , pp. E318-E327
    • Lean, J.M.1    Jagger, C.J.2    Chambers, T.J.3    Chow, J.W.4
  • 188
    • 2942711895 scopus 로고    scopus 로고
    • Skeletal unloading induces resistance to insulin-like growth factor-I (IGF-I) by inhibiting activation of the IGF-I signaling pathways
    • Sakata T., Wang Y., Halloran B.P., Elalieh H.Z., Cao J., Bikle D.D. Skeletal unloading induces resistance to insulin-like growth factor-I (IGF-I) by inhibiting activation of the IGF-I signaling pathways. J Bone Miner Res 2004, 19:436-446.
    • (2004) J Bone Miner Res , vol.19 , pp. 436-446
    • Sakata, T.1    Wang, Y.2    Halloran, B.P.3    Elalieh, H.Z.4    Cao, J.5    Bikle, D.D.6
  • 189
    • 0036179760 scopus 로고    scopus 로고
    • Noninvasive loading of the murine tibia: an in vivo model for the study of mechanotransduction
    • Gross T.S., Srinivasan S., Liu C.C., Clemens T.L., Bain S.D. Noninvasive loading of the murine tibia: an in vivo model for the study of mechanotransduction. J Bone Miner Res 2002, 17:493-501.
    • (2002) J Bone Miner Res , vol.17 , pp. 493-501
    • Gross, T.S.1    Srinivasan, S.2    Liu, C.C.3    Clemens, T.L.4    Bain, S.D.5
  • 190
    • 82355163211 scopus 로고    scopus 로고
    • Conditional disruption of IGF-I gene in type 1alpha collagen-expressing cells shows an essential role of IGF-I in skeletal anabolic response to loading
    • Kesavan C., Wergedal J.E., Lau K.H., Mohan S. Conditional disruption of IGF-I gene in type 1alpha collagen-expressing cells shows an essential role of IGF-I in skeletal anabolic response to loading. Am J Physiol Endocrinol Metab 2011, 301:E1191-E1197.
    • (2011) Am J Physiol Endocrinol Metab , vol.301 , pp. E1191-E1197
    • Kesavan, C.1    Wergedal, J.E.2    Lau, K.H.3    Mohan, S.4
  • 191
    • 84880154299 scopus 로고    scopus 로고
    • Osteocyte-derived insulin-like growth factor I is essential for determining bone mechanosensitivity
    • Lau K.H., Baylink D.J., Zhou X.D., Rodriguez D., Bonewald L.F., Li Z., et al. Osteocyte-derived insulin-like growth factor I is essential for determining bone mechanosensitivity. Am J Physiol Endocrinol Metab 2013, 305:E271-E281.
    • (2013) Am J Physiol Endocrinol Metab , vol.305 , pp. E271-E281
    • Lau, K.H.1    Baylink, D.J.2    Zhou, X.D.3    Rodriguez, D.4    Bonewald, L.F.5    Li, Z.6
  • 192
    • 0028268416 scopus 로고
    • Insulin-like growth factor-I increases trabecular bone formation and osteoblastic cell proliferation in unloaded rats
    • Machwate M., Zerath E., Holy X., Pastoureau P., Marie P.J. Insulin-like growth factor-I increases trabecular bone formation and osteoblastic cell proliferation in unloaded rats. Endocrinology 1994, 134:1031-1038.
    • (1994) Endocrinology , vol.134 , pp. 1031-1038
    • Machwate, M.1    Zerath, E.2    Holy, X.3    Pastoureau, P.4    Marie, P.J.5
  • 193
    • 84885665073 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 receptor in mature osteoblasts is required for periosteal bone formation induced by reloading
    • Kubota T., Elalieh H.Z., Saless N., Fong C., Wang Y., Babey M., et al. Insulin-like growth factor-1 receptor in mature osteoblasts is required for periosteal bone formation induced by reloading. Acta Astronaut 2013, 92:73-78.
    • (2013) Acta Astronaut , vol.92 , pp. 73-78
    • Kubota, T.1    Elalieh, H.Z.2    Saless, N.3    Fong, C.4    Wang, Y.5    Babey, M.6
  • 195
    • 67749097771 scopus 로고    scopus 로고
    • Fluid shear stress magnitude, duration, and total applied load regulate gene expression and nitric oxide production in primary calvarial osteoblast cultures
    • Gonzalez O., Fong K.D., Trindade M.C., Warren S.M., Longaker M.T., Smith R.L. Fluid shear stress magnitude, duration, and total applied load regulate gene expression and nitric oxide production in primary calvarial osteoblast cultures. Plast Reconstr Surg 2008, 122:419-428.
    • (2008) Plast Reconstr Surg , vol.122 , pp. 419-428
    • Gonzalez, O.1    Fong, K.D.2    Trindade, M.C.3    Warren, S.M.4    Longaker, M.T.5    Smith, R.L.6
  • 196
    • 15444368753 scopus 로고    scopus 로고
    • The effect of cytoskeletal disruption on pulsatile fluid flow-induced nitric oxide and prostaglandin E2 release in osteocytes and osteoblasts
    • McGarry J.G., Klein-Nulend J., Prendergast P.J. The effect of cytoskeletal disruption on pulsatile fluid flow-induced nitric oxide and prostaglandin E2 release in osteocytes and osteoblasts. Biochem Biophys Res Commun 2005, 330:341-348.
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 341-348
    • McGarry, J.G.1    Klein-Nulend, J.2    Prendergast, P.J.3
  • 197
    • 0034643303 scopus 로고    scopus 로고
    • Fluid shear stress stimulates prostaglandin and nitric oxide release in bone marrow-derived preosteoclast-like cells
    • McAllister T.N., Du T., Frangos J.A. Fluid shear stress stimulates prostaglandin and nitric oxide release in bone marrow-derived preosteoclast-like cells. Biochem Biophys Res Commun 2000, 270:643-648.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 643-648
    • McAllister, T.N.1    Du, T.2    Frangos, J.A.3
  • 198
    • 0029940159 scopus 로고    scopus 로고
    • Nitric oxide inhibitor l-NAME suppresses mechanically induced bone formation in rats
    • Turner C.H., Takano Y., Owan I., Murrell G.A. Nitric oxide inhibitor l-NAME suppresses mechanically induced bone formation in rats. Am J Physiol 1996, 270:E634-E639.
    • (1996) Am J Physiol , vol.270 , pp. E634-E639
    • Turner, C.H.1    Takano, Y.2    Owan, I.3    Murrell, G.A.4
  • 199
    • 0035999441 scopus 로고    scopus 로고
    • Role of inducible nitric oxide synthase in skeletal adaptation to acute increases in mechanical loading
    • Watanuki M., Sakai A., Sakata T., Tsurukami H., Miwa M., Uchida Y., et al. Role of inducible nitric oxide synthase in skeletal adaptation to acute increases in mechanical loading. J Bone Miner Res 2002, 17:1015-1025.
    • (2002) J Bone Miner Res , vol.17 , pp. 1015-1025
    • Watanuki, M.1    Sakai, A.2    Sakata, T.3    Tsurukami, H.4    Miwa, M.5    Uchida, Y.6
  • 200
    • 46549083294 scopus 로고    scopus 로고
    • The role of nitric oxide in the mechanical repression of RANKL in bone stromal cells
    • Rahnert J., Fan X., Case N., Murphy T.C., Grassi F., Sen B., et al. The role of nitric oxide in the mechanical repression of RANKL in bone stromal cells. Bone 2008, 43:48-54.
    • (2008) Bone , vol.43 , pp. 48-54
    • Rahnert, J.1    Fan, X.2    Case, N.3    Murphy, T.C.4    Grassi, F.5    Sen, B.6
  • 201
    • 78649542978 scopus 로고    scopus 로고
    • Mechanical induction of PGE2 in osteocytes blocks glucocorticoid-induced apoptosis through both the beta-catenin and PKA pathways
    • Kitase Y., Barragan L., Qing H., Kondoh S., Jiang J.X., Johnson M.L., et al. Mechanical induction of PGE2 in osteocytes blocks glucocorticoid-induced apoptosis through both the beta-catenin and PKA pathways. J Bone Miner Res 2010, 25:2657-2668.
    • (2010) J Bone Miner Res , vol.25 , pp. 2657-2668
    • Kitase, Y.1    Barragan, L.2    Qing, H.3    Kondoh, S.4    Jiang, J.X.5    Johnson, M.L.6
  • 203
    • 0020067211 scopus 로고
    • Arachidonic acid, prostaglandin E2 and F2 alpha influence rates of protein turnover in skeletal and cardiac muscle
    • Rodemann H.P., Goldberg A.L. Arachidonic acid, prostaglandin E2 and F2 alpha influence rates of protein turnover in skeletal and cardiac muscle. J Biol Chem 1982, 257:1632-1638.
    • (1982) J Biol Chem , vol.257 , pp. 1632-1638
    • Rodemann, H.P.1    Goldberg, A.L.2
  • 204
    • 79952173258 scopus 로고    scopus 로고
    • Prostaglandin F2α stimulates PI3K/ERK/mTOR signaling and skeletal myotube hypertrophy
    • Markworth J.F., Cameron-Smith D. Prostaglandin F2α stimulates PI3K/ERK/mTOR signaling and skeletal myotube hypertrophy. Am J Physiol Cell Physiol 2011, 300:C671-C682.
    • (2011) Am J Physiol Cell Physiol , vol.300 , pp. C671-C682
    • Markworth, J.F.1    Cameron-Smith, D.2
  • 205
    • 0020560578 scopus 로고
    • Protein synthesis in isolated rabbit forelimb muscles. The possible role of metabolites of arachidonic acid in the response to intermittent stretching
    • Smith R.H., Palmer R.M., Reeds P.J. Protein synthesis in isolated rabbit forelimb muscles. The possible role of metabolites of arachidonic acid in the response to intermittent stretching. Biochem J 1983, 214:153-161.
    • (1983) Biochem J , vol.214 , pp. 153-161
    • Smith, R.H.1    Palmer, R.M.2    Reeds, P.J.3
  • 206
    • 84871888797 scopus 로고    scopus 로고
    • Arachidonic acid supplementation enhances in vitro skeletal muscle cell growth via a COX-2-dependent pathway
    • Markworth J.F., Cameron-Smith D. Arachidonic acid supplementation enhances in vitro skeletal muscle cell growth via a COX-2-dependent pathway. Am J Physiol Cell Physiol 2013, 304:C56-C67.
    • (2013) Am J Physiol Cell Physiol , vol.304 , pp. C56-C67
    • Markworth, J.F.1    Cameron-Smith, D.2
  • 207
    • 84899947018 scopus 로고    scopus 로고
    • The skeletal muscle arachidonic acid cascade in health and inflammatory disease
    • Korotkova M., Lundberg I.E. The skeletal muscle arachidonic acid cascade in health and inflammatory disease. Nat Rev Rheumatol 2014, 10:295-303.
    • (2014) Nat Rev Rheumatol , vol.10 , pp. 295-303
    • Korotkova, M.1    Lundberg, I.E.2
  • 208
    • 84884215334 scopus 로고    scopus 로고
    • Effects of prostaglandins and COX-inhibiting drugs on skeletal muscle adaptations to exercise
    • Trappe T.A., Liu S.Z. Effects of prostaglandins and COX-inhibiting drugs on skeletal muscle adaptations to exercise. J Appl Physiol 2013, 115:909-919.
    • (2013) J Appl Physiol , vol.115 , pp. 909-919
    • Trappe, T.A.1    Liu, S.Z.2
  • 209
    • 0025270953 scopus 로고
    • Prostaglandins and the control of muscle protein synthesis and degradation
    • Palmer R.M. Prostaglandins and the control of muscle protein synthesis and degradation. Prostaglandins Leukot Essent Fatty Acids 1990, 39:95-104.
    • (1990) Prostaglandins Leukot Essent Fatty Acids , vol.39 , pp. 95-104
    • Palmer, R.M.1
  • 213
    • 77953296459 scopus 로고    scopus 로고
    • Notch and Wnt signaling, physiological stimuli and postnatal myogenesis
    • Tsivitse S. Notch and Wnt signaling, physiological stimuli and postnatal myogenesis. Int J Biol Sci 2010, 6:268-281.
    • (2010) Int J Biol Sci , vol.6 , pp. 268-281
    • Tsivitse, S.1
  • 214
    • 33745857968 scopus 로고    scopus 로고
    • Regulation of Dishevelled and beta-catenin in rat skeletal muscle: an alternative exercise-induced GSK-3beta signaling pathway
    • Aschenbach W.G., Ho R.C., Sakamoto K., Fujii N., Li Y., Kim Y.-B., et al. Regulation of Dishevelled and beta-catenin in rat skeletal muscle: an alternative exercise-induced GSK-3beta signaling pathway. Am J Physiol Endocrinol Metab 2006, 291:E152-E158.
    • (2006) Am J Physiol Endocrinol Metab , vol.291 , pp. E152-E158
    • Aschenbach, W.G.1    Ho, R.C.2    Sakamoto, K.3    Fujii, N.4    Li, Y.5    Kim, Y.-B.6
  • 216
    • 25444472900 scopus 로고    scopus 로고
    • Wnt/{beta}-catenin signaling activates growth-control genes during overload-induced skeletal muscle hypertrophy
    • Armstrong D.D., Esser K.A. Wnt/{beta}-catenin signaling activates growth-control genes during overload-induced skeletal muscle hypertrophy. Am J Physiol Cell Physiol 2005, 289:C853-C859.
    • (2005) Am J Physiol Cell Physiol , vol.289 , pp. C853-C859
    • Armstrong, D.D.1    Esser, K.A.2
  • 217
    • 33745686080 scopus 로고    scopus 로고
    • Expression of beta-catenin is necessary for physiological growth of adult skeletal muscle
    • Armstrong D.D., Wong V.L., Esser K.A. Expression of beta-catenin is necessary for physiological growth of adult skeletal muscle. Am J Physiol Cell Physiol 2006, 291:C185-C188.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. C185-C188
    • Armstrong, D.D.1    Wong, V.L.2    Esser, K.A.3
  • 218
    • 84856500662 scopus 로고    scopus 로고
    • Wnt7a-Fzd7 signalling directly activates the Akt/mTOR anabolic growth pathway in skeletal muscle
    • von Maltzahn J., Bentzinger C.F., Rudnicki M.A. Wnt7a-Fzd7 signalling directly activates the Akt/mTOR anabolic growth pathway in skeletal muscle. Nat Cell Biol 2012, 14:186-191.
    • (2012) Nat Cell Biol , vol.14 , pp. 186-191
    • von Maltzahn, J.1    Bentzinger, C.F.2    Rudnicki, M.A.3
  • 221
    • 63049094292 scopus 로고    scopus 로고
    • Bone growth during rapamycin therapy in young rats
    • Sanchez C., He Y.-Z. Bone growth during rapamycin therapy in young rats. BMC Pediatr 2009, 9:3.
    • (2009) BMC Pediatr , vol.9 , pp. 3
    • Sanchez, C.1    He, Y.-Z.2
  • 223
    • 84859508642 scopus 로고    scopus 로고
    • Growth hormone improves growth retardation induced by rapamycin without blocking its antiproliferative and antiangiogenic effects on rat growth plate
    • Álvarez-García Ó., García-López E., Loredo V., Gil-Peña H., Mejía-Gaviria N., Rodríguez-Suárez J., et al. Growth hormone improves growth retardation induced by rapamycin without blocking its antiproliferative and antiangiogenic effects on rat growth plate. PLoS One 2012, 7:e34788.
    • (2012) PLoS One , vol.7 , pp. e34788
    • Álvarez-García, Ó.1    García-López, E.2    Loredo, V.3    Gil-Peña, H.4    Mejía-Gaviria, N.5    Rodríguez-Suárez, J.6
  • 225
    • 84907707647 scopus 로고    scopus 로고
    • Mechanical activation of mammalian target of rapamycin pathway is required for cartilage development
    • Guan Y., Yang X., Yang W., Charbonneau C., Chen Q. Mechanical activation of mammalian target of rapamycin pathway is required for cartilage development. FASEB J 2014, 28(10):4470-4481.
    • (2014) FASEB J , vol.28 , Issue.10 , pp. 4470-4481
    • Guan, Y.1    Yang, X.2    Yang, W.3    Charbonneau, C.4    Chen, Q.5
  • 226
    • 38649110155 scopus 로고    scopus 로고
    • Rapamycin inhibits osteoblast proliferation and differentiation in MC3T3-E1 cells and primary mouse bone marrow stromal cells
    • Singha U.K., Jiang Y., Yu S., Luo M., Lu Y., Zhang J., et al. Rapamycin inhibits osteoblast proliferation and differentiation in MC3T3-E1 cells and primary mouse bone marrow stromal cells. J Cell Biochem 2008, 103:434-446.
    • (2008) J Cell Biochem , vol.103 , pp. 434-446
    • Singha, U.K.1    Jiang, Y.2    Yu, S.3    Luo, M.4    Lu, Y.5    Zhang, J.6
  • 227
    • 84055212618 scopus 로고    scopus 로고
    • Erythropoietin mediated bone formation is regulated by mTOR signaling
    • Kim J., Jung Y., Sun H., Joseph J., Mishra A., Shiozawa Y., et al. Erythropoietin mediated bone formation is regulated by mTOR signaling. J Cell Biochem 2012, 113:220-228.
    • (2012) J Cell Biochem , vol.113 , pp. 220-228
    • Kim, J.1    Jung, Y.2    Sun, H.3    Joseph, J.4    Mishra, A.5    Shiozawa, Y.6
  • 228
    • 84896717086 scopus 로고    scopus 로고
    • WNT7B promotes bone formation in part through mTORC1
    • Chen J., Tu X., Esen E., Joeng K.S., Lin C., Arbeit J.M., et al. WNT7B promotes bone formation in part through mTORC1. PLoS Genet 2014, 10:e1004145.
    • (2014) PLoS Genet , vol.10 , pp. e1004145
    • Chen, J.1    Tu, X.2    Esen, E.3    Joeng, K.S.4    Lin, C.5    Arbeit, J.M.6
  • 229
    • 84881227235 scopus 로고    scopus 로고
    • Bone effects of mammalian target of rapamycin (mTOR) inhibition with everolimus
    • Hadji P., Coleman R., Gnant M. Bone effects of mammalian target of rapamycin (mTOR) inhibition with everolimus. Crit Rev Oncol Hematol 2013, 87:101-111.
    • (2013) Crit Rev Oncol Hematol , vol.87 , pp. 101-111
    • Hadji, P.1    Coleman, R.2    Gnant, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.