메뉴 건너뛰기




Volumn 24, Issue 4, 2010, Pages 1284-1295

Myoferlin is required for insulin-like growth factor response and muscle growth

Author keywords

Lysosome; Myoblast fusion; Receptor trafficking; Signaling

Indexed keywords

MEMBRANE PROTEIN; MYOFERLIN; SOMATOMEDIN; SOMATOMEDIN C RECEPTOR; UNCLASSIFIED DRUG; INSULIN LIKE GROWTH FACTOR 1, MOUSE; INSULIN-LIKE GROWTH FACTOR-1, MOUSE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MUSCLE PROTEIN; MYOFERLIN PROTEIN, MOUSE; SOMATOMEDIN C;

EID: 77951640392     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-136309     Document Type: Article
Times cited : (50)

References (49)
  • 1
    • 34047092903 scopus 로고    scopus 로고
    • The ABCs of IGF-I isoforms: Impact on muscle hypertrophy and implications for repair
    • Barton, E. R. (2006) The ABCs of IGF-I isoforms: impact on muscle hypertrophy and implications for repair. Appl. Physiol. Nutr. Metab. 31, 791-797
    • (2006) Appl. Physiol. Nutr. Metab. , vol.31 , pp. 791-797
    • Barton, E.R.1
  • 3
    • 0037014652 scopus 로고    scopus 로고
    • Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation
    • Yang, S. Y., and Goldspink, G. (2002) Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett. 522, 156-160
    • (2002) FEBS Lett. , vol.522 , pp. 156-160
    • Yang, S.Y.1    Goldspink, G.2
  • 4
    • 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., and Schwartz, R. J. (1995) Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice. J. Biol. Chem. 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    Schwartz, R.J.7
  • 5
    • 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., and Efstratiadis, A. (1993) Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 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
  • 7
    • 0033526991 scopus 로고    scopus 로고
    • IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NFATc1
    • Musaro, A., McCullagh, K. J., Naya, F. J., Olson, E. N., and Rosenthal, N. (1999) IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NFATc1. Nature 400, 581-585
    • (1999) Nature , vol.400 , pp. 581-585
    • Musaro, A.1    McCullagh, K.J.2    Naya, F.J.3    Olson, E.N.4    Rosenthal, N.5
  • 8
    • 33746042956 scopus 로고    scopus 로고
    • Liver-specific overexpression of the insulin-like growth factor-I enhances somatic growth and partially prevents the effects of growth hormone deficiency
    • Liao, L., Dearth, R. K., Zhou, S., Britton, O. L., Lee, A. V., and Xu, J. (2006) Liver-specific overexpression of the insulin-like growth factor-I enhances somatic growth and partially prevents the effects of growth hormone deficiency. Endocrinology 147, 3877-3888
    • (2006) Endocrinology , vol.147 , pp. 3877-3888
    • Liao, L.1    Dearth, R.K.2    Zhou, S.3    Britton, O.L.4    Lee, A.V.5    Xu, J.6
  • 9
    • 24744449943 scopus 로고    scopus 로고
    • IGF-1, inflammation and stem cells: Interactions during muscle regeneration
    • Mourkioti, F., and Rosenthal, N. (2005) IGF-1, inflammation and stem cells: interactions during muscle regeneration. Trends Immunol. 26, 535-542
    • (2005) Trends Immunol. , vol.26 , pp. 535-542
    • Mourkioti, F.1    Rosenthal, N.2
  • 10
    • 0030934472 scopus 로고    scopus 로고
    • The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways
    • Coolican, S. A., Samuel, D. S., Ewton, D. Z., McWade, F. J., and Florini, J. R. (1997) The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways. J. Biol. Chem. 272, 6653-6662
    • (1997) J. Biol. Chem. , vol.272 , pp. 6653-6662
    • Coolican, S.A.1    Samuel, D.S.2    Ewton, D.Z.3    McWade, F.J.4    Florini, J.R.5
  • 12
    • 0042427273 scopus 로고    scopus 로고
    • Repairing the tears: Dysferlin in muscle membrane repair
    • Doherty, K. R., and McNally, E. M. (2003) Repairing the tears: dysferlin in muscle membrane repair. Trends Mol. Med. 9, 327-330
    • (2003) Trends Mol. Med. , vol.9 , pp. 327-330
    • Doherty, K.R.1    McNally, E.M.2
  • 16
    • 33846940049 scopus 로고    scopus 로고
    • Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans
    • George, M., Ying, G., Rainey, M. A., Solomon, A., Parikh, P. T., Gao, Q., Band, V., and Band, H. (2007) Shared as well as distinct roles of EHD proteins revealed by biochemical and functional comparisons in mammalian cells and C. elegans. BMC Cell Biol. 8, 3
    • (2007) BMC Cell Biol. , vol.8 , pp. 3
    • George, M.1    Ying, G.2    Rainey, M.A.3    Solomon, A.4    Parikh, P.T.5    Gao, Q.6    Band, V.7    Band, H.8
  • 17
    • 0035067333 scopus 로고    scopus 로고
    • IGF-I treatment improves the functional properties of fast- and slow-twitch skeletal muscles from dystrophic mice
    • Lynch, G. S., Cuffe, S. A., Plant, D. R., and Gregorevic, P. (2001) IGF-I treatment improves the functional properties of fast- and slow-twitch skeletal muscles from dystrophic mice. Neuromuscul. Disord. 11, 260-268
    • (2001) Neuromuscul. Disord. , vol.11 , pp. 260-268
    • Lynch, G.S.1    Cuffe, S.A.2    Plant, D.R.3    Gregorevic, P.4
  • 19
    • 0027418205 scopus 로고
    • Measurement of co-localisation of objects in dual-colour confocal images
    • Manders, E. E. M. (1993) Measurement of co-localisation of objects in dual-colour confocal images. J. Microsc. 169, 375-382
    • (1993) J. Microsc. , vol.169 , pp. 375-382
    • Manders, E.E.M.1
  • 21
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • Wiley, H. S., and Cunningham, D. D. (1981) A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands. Cell 25, 433-440
    • (1981) Cell , vol.25 , pp. 433-440
    • Wiley, H.S.1    Cunningham, D.D.2
  • 22
    • 0032548865 scopus 로고    scopus 로고
    • Insulin-like growth factor-I receptor internalization regulates signaling via the Shc/mitogen-activated protein kinase pathway, but not the insulin receptor substrate-1 pathway
    • Chow, J. C., Condorelli, G., and Smith, R. J. (1998) Insulin-like growth factor-I receptor internalization regulates signaling via the Shc/mitogen-activated protein kinase pathway, but not the insulin receptor substrate-1 pathway. J. Biol. Chem. 273, 4672-4680
    • (1998) J. Biol. Chem. , vol.273 , pp. 4672-4680
    • Chow, J.C.1    Condorelli, G.2    Smith, R.J.3
  • 23
    • 0020557702 scopus 로고
    • Preferential enhancement of myoblast differentiation by insulin-like growth factors (IGF I and IGF II) in primary cultures of chicken embryonic cells
    • Schmid, C., Steiner, T., and Froesch, E. R. (1983) Preferential enhancement of myoblast differentiation by insulin-like growth factors (IGF I and IGF II) in primary cultures of chicken embryonic cells. FEBS Lett. 161, 117-121
    • (1983) FEBS Lett. , vol.161 , pp. 117-121
    • Schmid, C.1    Steiner, T.2    Froesch, E.R.3
  • 24
    • 0028355734 scopus 로고
    • Comparison of the intracellular itineraries of insulin-like growth factor-I and insulin and their receptors in Rat-1 fibroblasts
    • Zapf, A., Hsu, D., and Olefsky, J. M. (1994) Comparison of the intracellular itineraries of insulin-like growth factor-I and insulin and their receptors in Rat-1 fibroblasts. Endocrinology 134, 2445-2452
    • (1994) Endocrinology , vol.134 , pp. 2445-2452
    • Zapf, A.1    Hsu, D.2    Olefsky, J.M.3
  • 25
    • 0018356877 scopus 로고
    • Membrane events involved in myoblast fusion
    • Kalderon, N., and Gilula, N. B. (1979) Membrane events involved in myoblast fusion. J. Cell Biol. 81, 411-425
    • (1979) J. Cell Biol. , vol.81 , pp. 411-425
    • Kalderon, N.1    Gilula, N.B.2
  • 26
    • 0028910579 scopus 로고
    • Muscle regeneration following injury can be modified in vivo by immune neutralization of basic fibroblast growth factor, transforming growth factor beta 1 or insulin-like growth factor I
    • Lefaucheur, J. P., and Sebille, A. (1995) Muscle regeneration following injury can be modified in vivo by immune neutralization of basic fibroblast growth factor, transforming growth factor beta 1 or insulin-like growth factor I. J. Neuroimmunol. 57, 85-91
    • (1995) J. Neuroimmunol. , vol.57 , pp. 85-91
    • Lefaucheur, J.P.1    Sebille, A.2
  • 27
    • 34547830243 scopus 로고    scopus 로고
    • IGF-I and insulin activate mitogen-activated protein kinase via the type 1 IGF receptor in mouse embryonic stem cells
    • Nguyen, T. T., Sheppard, A. M., Kaye, P. L., and Noakes, P. G. (2007) IGF-I and insulin activate mitogen-activated protein kinase via the type 1 IGF receptor in mouse embryonic stem cells. Reproduction 134, 41-49
    • (2007) Reproduction , vol.134 , pp. 41-49
    • Nguyen, T.T.1    Sheppard, A.M.2    Kaye, P.L.3    Noakes, P.G.4
  • 29
    • 84934438243 scopus 로고    scopus 로고
    • Fine structure of the autophagosome
    • Eskelinen, E. L. (2008) Fine structure of the autophagosome. Methods Mol. Biol. 445, 11-28
    • (2008) Methods Mol. Biol. , vol.445 , pp. 11-28
    • Eskelinen, E.L.1
  • 30
    • 0030866081 scopus 로고    scopus 로고
    • Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2]i in fibroblasts
    • Bakker, A. C., Webster, P., Jacob, W. A., and Andrews, N. W. (1997) Homotypic fusion between aggregated lysosomes triggered by elevated [Ca2]i in fibroblasts. J. Cell Sci. 110(Pt. 18), 2227-2238
    • (1997) J. Cell Sci. , vol.110 , Issue.PART. 18 , pp. 2227-2238
    • Bakker, A.C.1    Webster, P.2    Jacob, W.A.3    Andrews, N.W.4
  • 31
    • 13244284886 scopus 로고    scopus 로고
    • Ultrastructural changes in dysferlinopathy support defective membrane repair mechanism
    • Cenacchi, G., Fanin, M., De Giorgi, L. B., and Angelini, C. (2005) Ultrastructural changes in dysferlinopathy support defective membrane repair mechanism. J. Clin. Pathol. 58, 190-195
    • (2005) J. Clin. Pathol. , vol.58 , pp. 190-195
    • Cenacchi, G.1    Fanin, M.2    De Giorgi, L.B.3    Angelini, C.4
  • 32
    • 54449085789 scopus 로고    scopus 로고
    • Modulation of GH/IGF-1 axis: Potential strategies to counteract sarcopenia in older adults
    • Giovannini, S., Marzetti, E., Borst, S. E., and Leeuwenburgh, C. (2008) Modulation of GH/IGF-1 axis: potential strategies to counteract sarcopenia in older adults. Mech. Ageing Dev. 129, 593-601
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 593-601
    • Giovannini, S.1    Marzetti, E.2    Borst, S.E.3    Leeuwenburgh, C.4
  • 33
    • 0033377468 scopus 로고    scopus 로고
    • Contribution of satellite cells to IGF-I induced hypertrophy of skeletal muscle
    • Barton-Davis, E. R., Shoturma, D. I., and Sweeney, H. L. (1999) Contribution of satellite cells to IGF-I induced hypertrophy of skeletal muscle. Acta Physiol. Scand. 167, 301-305
    • (1999) Acta Physiol. Scand. , vol.167 , pp. 301-305
    • Barton-Davis, E.R.1    Shoturma, D.I.2    Sweeney, H.L.3
  • 34
    • 0037151075 scopus 로고    scopus 로고
    • Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains
    • Davis, D. B., Doherty, K. R., Delmonte, A. J., and McNally, E. M. (2002) Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. J. Biol. Chem. 277, 22883-22888
    • (2002) J. Biol. Chem. , vol.277 , pp. 22883-22888
    • Davis, D.B.1    Doherty, K.R.2    Delmonte, A.J.3    McNally, E.M.4
  • 35
    • 56149084770 scopus 로고    scopus 로고
    • Mechanisms of EHD/RME-1 protein function in endocytic transport
    • Grant, B. D., and Caplan, S. (2008) Mechanisms of EHD/RME-1 protein function in endocytic transport. Traffic 9, 2043-2052
    • (2008) Traffic , vol.9 , pp. 2043-2052
    • Grant, B.D.1    Caplan, S.2
  • 37
    • 0037726553 scopus 로고    scopus 로고
    • IL-4 acts as a myoblast recruitment factor during mammalian muscle growth
    • Horsley, V., Jansen, K. M., Mills, S. T., and Pavlath, G. K. (2003) IL-4 acts as a myoblast recruitment factor during mammalian muscle growth. Cell 113, 483-494
    • (2003) Cell , vol.113 , pp. 483-494
    • Horsley, V.1    Jansen, K.M.2    Mills, S.T.3    Pavlath, G.K.4
  • 38
    • 33746611993 scopus 로고    scopus 로고
    • Mannose receptor regulates myoblast motility and muscle growth
    • Jansen, K. M., and Pavlath, G. K. (2006) Mannose receptor regulates myoblast motility and muscle growth. J. Cell Biol. 174, 403-413
    • (2006) J. Cell Biol. , vol.174 , pp. 403-413
    • Jansen, K.M.1    Pavlath, G.K.2
  • 41
    • 56049124302 scopus 로고    scopus 로고
    • Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form
    • Heidrych, P., Zimmermann, U., Bress, A., Pusch, C. M., Ruth, P., Pfister, M., Knipper, M., and Blin, N. (2008) Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form. Hum. Mol. Genet. 17, 3814-3821
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3814-3821
    • Heidrych, P.1    Zimmermann, U.2    Bress, A.3    Pusch, C.M.4    Ruth, P.5    Pfister, M.6    Knipper, M.7    Blin, N.8
  • 42
    • 48249101885 scopus 로고    scopus 로고
    • Rab8 regulates basolateral secretory, but not recycling, traffic at the recycling endosome
    • Henry, L., and Sheff, D. R. (2008) Rab8 regulates basolateral secretory, but not recycling, traffic at the recycling endosome. Mol. Biol. Cell 19, 2059-2068
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2059-2068
    • Henry, L.1    Sheff, D.R.2
  • 43
    • 0023886620 scopus 로고
    • Receptor-mediated endocytosis and lysosomal processing of insulin-like growth factor I by mitogenically responsive cells
    • Furlanetto, R. W. (1988) Receptor-mediated endocytosis and lysosomal processing of insulin-like growth factor I by mitogenically responsive cells. Endocrinology 122, 2044-2053
    • (1988) Endocrinology , vol.122 , pp. 2044-2053
    • Furlanetto, R.W.1
  • 44
    • 33645732101 scopus 로고    scopus 로고
    • Vesicular trafficking of tyrosine kinase receptors and associated proteins in the regulation of signaling and vascular function
    • Mukherjee, S., Tessema, M., and Wandinger-Ness, A. (2006) Vesicular trafficking of tyrosine kinase receptors and associated proteins in the regulation of signaling and vascular function. Circ. Res. 98, 743-756
    • (2006) Circ. Res. , vol.98 , pp. 743-756
    • Mukherjee, S.1    Tessema, M.2    Wandinger-Ness, A.3
  • 45
    • 0024592373 scopus 로고
    • Induction of insulin-like growth factor I messenger ribonucleic acid during regeneration of rat skeletal muscle
    • Edwall, D., Schalling, M., Jennische, E., and Norstedt, G. (1989) Induction of insulin-like growth factor I messenger ribonucleic acid during regeneration of rat skeletal muscle. Endocrinology 124, 820-825
    • (1989) Endocrinology , vol.124 , pp. 820-825
    • Edwall, D.1    Schalling, M.2    Jennische, E.3    Norstedt, G.4
  • 46
    • 57049094929 scopus 로고    scopus 로고
    • Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease
    • Raben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., Ralston, E., and Plotz, P. (2008) Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease. Hum. Mol. Genet. 17, 3897-3908
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3897-3908
    • Raben, N.1    Hill, V.2    Shea, L.3    Takikita, S.4    Baum, R.5    Mizushima, N.6    Ralston, E.7    Plotz, P.8
  • 49
    • 0033972161 scopus 로고    scopus 로고
    • Myoferlin, a candidate gene and potential modifier of muscular dystrophy
    • Davis, D. B., Delmonte, A. J., Ly, C. T., and McNally, E. M. (2000) Myoferlin, a candidate gene and potential modifier of muscular dystrophy. Hum. Mol. Genet. 9, 217-226
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 217-226
    • Davis, D.B.1    Delmonte, A.J.2    Ly, C.T.3    McNally, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.