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Volumn 20, Issue 5, 2010, Pages 603-616

Desialylation of insulin receptors and IGF-1 receptors by neuraminidase-1 controls the net proliferative response of L6 myoblasts to insulin

Author keywords

IGF 1 receptor; Insulin insulin receptor; Neuraminidase 1; Skeletal myoblasts proliferation

Indexed keywords

INSULIN; INSULIN RECEPTOR; NEURAMINIDASE 1; SIALIDASE; SOMATOMEDIN C RECEPTOR; UNCLASSIFIED DRUG;

EID: 77952844482     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwq010     Document Type: Article
Times cited : (50)

References (72)
  • 1
    • 70450223518 scopus 로고    scopus 로고
    • Desialylation of sialyl alpha-2 3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling
    • Amith SR, Jayanth P, Franchuk S, Finlay T, Seyrantepe V, Beyaert R, Pshezhetsky AV, Szewczuk MR. 2010. Desialylation of sialyl alpha-2, 3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling. Cell Signal. 22(2):314-324.
    • (2010) Cell Signal , vol.22 , Issue.2 , pp. 314-324
    • Amith, S.R.1    Jayanth, P.2    Franchuk, S.3    Finlay, T.4    Seyrantepe, V.5    Beyaert, R.6    Pshezhetsky, A.V.7    Szewczuk, M.R.8
  • 2
    • 0034765199 scopus 로고    scopus 로고
    • Differential phosphorylation of IRS-1 by insulin and insulin-like growth factor I receptors in Chinese hamster ovary cells
    • Amoui M, Craddock BP, Miller WT. 2001. Differential phosphorylation of IRS-1 by insulin and insulin-like growth factor I receptors in Chinese hamster ovary cells. J Endocrinol. 171:153-162.
    • (2001) J Endocrinol , vol.171 , pp. 153-162
    • Amoui, M.1    Craddock, B.P.2    Miller, W.T.3
  • 3
    • 61349094775 scopus 로고    scopus 로고
    • NEU3 sialidase strictly modulates GM3 levels in skeletal myoblasts C2C12 thus favoring their differentiation and protecting them from apoptosis
    • Anastasia L, Papini N, Colazzo F, Palazzolo G, Tringali C, Dileo L, Piccoli M, Conforti E, Sitzia C, Monti E, et al. 2008. NEU3 sialidase strictly modulates GM3 levels in skeletal myoblasts C2C12 thus favoring their differentiation and protecting them from apoptosis. J Biol Chem. 283:36265-36271.
    • (2008) J Biol Chem , vol.283 , pp. 36265-36271
    • Anastasia, L.1    Papini, N.2    Colazzo, F.3    Palazzolo, G.4    Tringali, C.5    Dileo, L.6    Piccoli, M.7    Conforti, E.8    Sitzia, C.9    Monti, E.10
  • 4
    • 84934441342 scopus 로고    scopus 로고
    • Dissecting GLUT4 traffic components in L6 myocytes by fluorescence-based, single-cell assays
    • Antonescu CN, Randhawa VK, Klip A. 2008. Dissecting GLUT4 traffic components in L6 myocytes by fluorescence-based, single-cell assays. Methods Mol Biol. 457:367-378.
    • (2008) Methods Mol Biol , vol.457 , pp. 367-378
    • Antonescu, C.N.1    Randhawa, V.K.2    Klip, A.3
  • 5
    • 53649106687 scopus 로고    scopus 로고
    • The role of IGF-system in vascular insulin resistance
    • Arnqvist HJ. 2008. The role of IGF-system in vascular insulin resistance. Horm Metab Res. 40:588-592.
    • (2008) Horm Metab Res , vol.40 , pp. 588-592
    • Arnqvist, H.J.1
  • 6
    • 0348230858 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms regulat-ing skeletal muscle development
    • Orlando(FL): Academic
    • Asakura A, Rudnicki MA. 2002. Cellular and molecular mechanisms regulating skeletal muscle development. Mouse Development.Orlando(FL): Academic. p. 253-278.
    • (2002) Mouse Development , pp. 253-278
    • Asakura, A.1    Rudnicki, M.A.2
  • 7
    • 0028786552 scopus 로고
    • Lysosomal protective protein/cathepsin A Role of the "linker" domain in catalytic activation
    • Bonten EJ, Galjart NJ, Willemsen R, Usmany M, Vlak JM, d'Azzo A. 1995. Lysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation. J Biol Chem. 270:26441-26445.
    • (1995) J Biol Chem , vol.270 , pp. 26441-26445
    • Bonten, E.J.1    Galjart, N.J.2    Willemsen, R.3    Usmany, M.4    Vlak, J.M.5    d'Azzo, A.6
  • 8
    • 0034535503 scopus 로고    scopus 로고
    • Lysosomal neuraminidase Catalytic activation in insect cells is controlled by the protective protein/cathepsin A
    • Bonten EJ, d'Azzo A. 2000. Lysosomal neuraminidase. Catalytic activation in insect cells is controlled by the protective protein/cathepsin A. J Biol Chem. 275:37657-37663.
    • (2000) J Biol Chem , vol.275 , pp. 37657-37663
    • Bonten, E.J.1    d'Azzo, A.2
  • 9
    • 27444439662 scopus 로고    scopus 로고
    • Overexpression of MyoD-inducible lysosomal sialidase (neu1) inhibits myogenesis in C2C12 cells
    • Champigny MJ, Perry R, Rudnicki M, Igdoura SA. 2005. Overexpression of MyoD-inducible lysosomal sialidase (neu1) inhibits myogenesis in C2C12 cells. Exp Cell Res. 311:157-166.
    • (2005) Exp Cell Res , vol.311 , pp. 157-166
    • Champigny, M.J.1    Perry, R.2    Rudnicki, M.3    Igdoura, S.A.4
  • 10
    • 0347989458 scopus 로고    scopus 로고
    • Cellular and molecular regulation of muscle regeneration
    • Charge SB, Rudnicki MA. 2004. Cellular and molecular regulation of muscle regeneration. Physiol Rev. 84:209-238.
    • (2004) Physiol Rev , vol.84 , pp. 209-238
    • Charge, S.B.1    Rudnicki, M.A.2
  • 11
    • 26244441717 scopus 로고    scopus 로고
    • Expression and function of receptors for insulin-like growth factor-I and insulin in human coronary artery smooth muscle cells
    • Chisalita SI, Arnqvist H. 2005. Expression and function of receptors for insulin-like growth factor-I and insulin in human coronary artery smooth muscle cells. Diabetologia. 48:2155-2161.
    • (2005) Diabetologia , vol.48 , pp. 2155-2161
    • Chisalita, S.I.1    Arnqvist, H.2
  • 12
    • 0026669686 scopus 로고
    • Characteristics of the beta-galactosidase-carboxypeptidase complex in GM1-gangliosidosis and beta-galactosialidosis fibroblasts
    • D'Agrosa R, Hubbes M, Zhang S, Shankaran R, Callahan J. 1992. Characteristics of the beta-galactosidase-carboxypeptidase complex in GM1-gangliosidosis and beta-galactosialidosis fibroblasts. Biochem J. 285:833-838.
    • (1992) Biochem J , vol.285 , pp. 833-838
    • D'Agrosa, R.1    Hubbes, M.2    Zhang, S.3    Shankaran, R.4    Callahan, J.5
  • 15
    • 0030881301 scopus 로고    scopus 로고
    • Replicative potential and telomere length in human skeletal muscle: Implications for satellite cell-mediated gene therapy
    • Decary S, Mouly V, Hamida CB, Sautet A, Barbet JP, Butler-Browne GS. 1997. Replicative potential and telomere length in human skeletal muscle: Implications for satellite cell-mediated gene therapy. Hum Gene Ther. 8:1429-1438.
    • (1997) Hum Gene Ther , vol.8 , pp. 1429-1438
    • Decary, S.1    Mouly, V.2    Hamida, C.B.3    Sautet, A.4    Barbet, J.P.5    Butler-Browne, G.S.6
  • 16
    • 71749085538 scopus 로고    scopus 로고
    • Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice
    • de Geest N, Bonten E, Mann L, de Sousa-Hitzler J, Hahn C, d'Azzo A. 2002. Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice. Hum Mol Genet. 11:1455-1464.
    • (2002) Hum Mol Genet , vol.11 , pp. 1455-1464
    • de Geest, N.1    Bonten, E.2    Mann, L.3    de Sousa-Hitzler, J.4    Hahn, C.5    d'Azzo, A.6
  • 19
    • 0022416139 scopus 로고
    • Removal of sialic acids from the purified insulin receptor results in enhanced insulin-binding and kinase activities
    • Fujita-Yamaguchi Y, Sato Y, Kathuria S. 1985. Removal of sialic acids from the purified insulin receptor results in enhanced insulin-binding and kinase activities. Biochem Biophys Res Commun. 129:739-745.
    • (1985) Biochem Biophys Res Commun , vol.129 , pp. 739-745
    • Fujita-Yamaguchi, Y.1    Sato, Y.2    Kathuria, S.3
  • 20
    • 0027523611 scopus 로고
    • Regulation of alpha 2 3-sialyltransferase expression correlates with conversion of peanut agglutinin (PNA)+ to PNAphenotype in developing thymocytes
    • Gillespie W, Paulson JC, Kelm S, Pang M, Baum LG. 1993. Regulation of alpha 2, 3-sialyltransferase expression correlates with conversion of peanut agglutinin (PNA)+ to PNAphenotype in developing thymocytes. J Biol Chem. 268:3801-3804.
    • (1993) J Biol Chem , vol.268 , pp. 3801-3804
    • Gillespie, W.1    Paulson, J.C.2    Kelm, S.3    Pang, M.4    Baum, L.G.5
  • 21
    • 0942276379 scopus 로고    scopus 로고
    • Nutrient-dependent and insulinstimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling
    • Giraud J, Leshan R, Lee YH, White MF. 2004. Nutrient-dependent and insulinstimulated phosphorylation of insulin receptor substrate-1 on serine 302 correlates with increased insulin signaling. J Biol Chem. 279:3447-3454.
    • (2004) J Biol Chem , vol.279 , pp. 3447-3454
    • Giraud, J.1    Leshan, R.2    Lee, Y.H.3    White, M.F.4
  • 23
    • 36749061251 scopus 로고    scopus 로고
    • Skeletal muscle satellite cells and adult myogenesis
    • Le Grand F, Rudnicki MA. 2007. Skeletal muscle satellite cells and adult myogenesis. Curr Opin Cell Biol. 19:628-633.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 628-633
    • Le Grand, F.1    Rudnicki, M.A.2
  • 24
    • 0033388867 scopus 로고    scopus 로고
    • Muscle regeneration: Molecular aspects and therapeutic implications
    • Grounds MD. 1999. Muscle regeneration: Molecular aspects and therapeutic implications. Curr Opin Neurol. 12:535-543.
    • (1999) Curr Opin Neurol , vol.12 , pp. 535-543
    • Grounds, M.D.1
  • 25
    • 49549161101 scopus 로고
    • A simple method for the purification of commercial neuraminidase preparations free from proteases
    • Hatton MWC, Regoeczi E. 1973. A simple method for the purification of commercial neuraminidase preparations free from proteases. Biochim Biophys Acta. 327:114-120.
    • (1973) Biochim Biophys Acta , vol.327 , pp. 114-120
    • Hatton, M.W.C.1    Regoeczi, E.2
  • 26
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke TJ, Garry DJ. 2001. Myogenic satellite cells: Physiology to molecular biology. J Appl Physiol. 91:534-551.
    • (2001) J Appl Physiol , vol.91 , pp. 534-551
    • Hawke, T.J.1    Garry, D.J.2
  • 27
    • 0022647664 scopus 로고
    • Oligosaccharide heterogeneity of insulin receptors Comparison of N-linked glycosylation of insulin receptors in adipocytes and brain
    • Heidenreich K, Brandenburg D. 1986. Oligosaccharide heterogeneity of insulin receptors. Comparison of N-linked glycosylation of insulin receptors in adipocytes and brain. Endocrinology. 118:1835-1842.
    • (1986) Endocrinology , vol.118 , pp. 1835-1842
    • Heidenreich, K.1    Brandenburg, D.2
  • 28
    • 0027479052 scopus 로고
    • The 67kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of beta-galactosidase
    • Hinek A, Rabinovitch M, Keeley F, Okamura OY, Callahan JW. 1993. The 67kD elastin/laminin-binding protein is related to an enzymatically inactive, alternatively spliced form of beta-galactosidase. J Clin Invest. 91:1198-1205.
    • (1993) J Clin Invest , vol.91 , pp. 1198-1205
    • Hinek, A.1    Rabinovitch, M.2    Keeley, F.3    Okamura, O.Y.4    Callahan, J.W.5
  • 29
    • 33645640140 scopus 로고    scopus 로고
    • Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly
    • Hinek A, Pshezhetsky AV, von Itzstein M, Starcher B. 2006. Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly. J Biol Chem. 281:3698-3710.
    • (2006) J Biol Chem , vol.281 , pp. 3698-3710
    • Hinek, A.1    Pshezhetsky, A.V.2    von Itzstein, M.3    Starcher, B.4
  • 30
    • 53149103203 scopus 로고    scopus 로고
    • Neuraminidase-1, a subunit of the cell surface elastin receptor, desialylates and functionally inactivates adjacent receptors interacting with the mitogenic growth factors PDGF-BB and IGF-II
    • Hinek A, Bodnaruk TD, Bunda S, Wang Y, Liu K. 2008. Neuraminidase-1, a subunit of the cell surface elastin receptor, desialylates and functionally inactivates adjacent receptors interacting with the mitogenic growth factors PDGF-BB and IGF-II. Am J Pathol. 173:1042-1056.
    • (2008) Am J Pathol , vol.173 , pp. 1042-1056
    • Hinek, A.1    Bodnaruk, T.D.2    Bunda, S.3    Wang, Y.4    Liu, K.5
  • 31
    • 0031975165 scopus 로고    scopus 로고
    • Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts
    • Igdoura SA, Gafuik C, Mertineit C, Saberi F, Pshezhetsky AV, Potier M, Trasler JM, Gravel RA. 1998. Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts. Hum Mol Genet. 7:115-121.
    • (1998) Hum Mol Genet , vol.7 , pp. 115-121
    • Igdoura, S.A.1    Gafuik, C.2    Mertineit, C.3    Saberi, F.4    Pshezhetsky, A.V.5    Potier, M.6    Trasler, J.M.7    Gravel, R.A.8
  • 32
    • 0027500072 scopus 로고
    • Purification and characterization of human lysosomal protective protein expressed in stably transformed Chinese hamster ovary cells
    • Itoh K, Takiyama N, Kase R, Kondoh K, Sano A, Oshima A, Sakuraba H, Suzuki Y. 1993. Purification and characterization of human lysosomal protective protein expressed in stably transformed Chinese hamster ovary cells. J Biol Chem. 268:1180-1186.
    • (1993) J Biol Chem , vol.268 , pp. 1180-1186
    • Itoh, K.1    Takiyama, N.2    Kase, R.3    Kondoh, K.4    Sano, A.5    Oshima, A.6    Sakuraba, H.7    Suzuki, Y.8
  • 33
    • 33751168727 scopus 로고    scopus 로고
    • Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid insulin/IGF-I receptors in vascular smooth muscle cells
    • Johansson GS, Arnqvist HJ. 2006. Insulin and IGF-I action on insulin receptors, IGF-I receptors, and hybrid insulin/IGF-I receptors in vascular smooth muscle cells. Am J Physiol Endocrinol Metab. 291:E1124-E1130.
    • (2006) Am J Physiol Endocrinol Metab , vol.291
    • Johansson, G.S.1    Arnqvist, H.J.2
  • 35
    • 0018951092 scopus 로고
    • Effects of neuraminidase treatment on solubilized insulin receptor
    • Kasuga M, Ezaki O, Akanuma Y, Kosaka K. 1980. Effects of neuraminidase treatment on solubilized insulin receptor. Horm Metab Res. 10:494-496.
    • (1980) Horm Metab Res , vol.10 , pp. 494-496
    • Kasuga, M.1    Ezaki, O.2    Akanuma, Y.3    Kosaka, K.4
  • 36
    • 63849311264 scopus 로고    scopus 로고
    • Regulation of glucose transporter 4 traffic by energy deprivation from mitochondrial compromise
    • Klip A, Schertzer JD, Bilan PJ, Thong F, Antonescu C. 2009. Regulation of glucose transporter 4 traffic by energy deprivation from mitochondrial compromise. Acta Physiol (Oxf). 196:27-35.
    • (2009) Acta Physiol (Oxf) , vol.196 , pp. 27-35
    • Klip, A.1    Schertzer, J.D.2    Bilan, P.J.3    Thong, F.4    Antonescu, C.5
  • 37
    • 0027283552 scopus 로고
    • Binding determinants of the sialic acid-specific lectin from the slug Limax flavus
    • Knibbs RN, Osborner SE, Glick GD, Goldstein IJ. 1993. Binding determinants of the sialic acid-specific lectin from the slug Limax flavus. J Biol Chem. 268:18524-18531.
    • (1993) J Biol Chem , vol.268 , pp. 18524-18531
    • Knibbs, R.N.1    Osborner, S.E.2    Glick, G.D.3    Goldstein, I.J.4
  • 38
    • 37549054341 scopus 로고    scopus 로고
    • The emerging biology of satellite cells and their therapeutic potential
    • Kuang S, Rudnicki MA. 2008. The emerging biology of satellite cells and their therapeutic potential. Trends Mol Med. 14:82-91.
    • (2008) Trends Mol Med , vol.14 , pp. 82-91
    • Kuang, S.1    Rudnicki, M.A.2
  • 41
    • 0027256304 scopus 로고
    • Differential effect of various inhibitors on four types of rat sialidase
    • Miyagi T, Hata K, Hasegawa A, Aoyagi T. 1993. Differential effect of various inhibitors on four types of rat sialidase. Glycoconj J. 10:45-49.
    • (1993) Glycoconj J , vol.10 , pp. 45-49
    • Miyagi, T.1    Hata, K.2    Hasegawa, A.3    Aoyagi, T.4
  • 42
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membraneassociated sialidase specific for gangliosides
    • Miyagi T, Wada T, Iwamatsu A, Hata K, Yoshikawa Y, Tokuyama S, Sawada M. 1999. Molecular cloning and characterization of a plasma membraneassociated sialidase specific for gangliosides. J Biol Chem. 274:5004-5011.
    • (1999) J Biol Chem , vol.274 , pp. 5004-5011
    • Miyagi, T.1    Wada, T.2    Iwamatsu, A.3    Hata, K.4    Yoshikawa, Y.5    Tokuyama, S.6    Sawada, M.7
  • 43
    • 59149093715 scopus 로고    scopus 로고
    • Aberrant expression of sialidase and cancer progression
    • Miyagi T. 2008. Aberrant expression of sialidase and cancer progression. Proc Jpn Acad SerB. 84.
    • (2008) Proc Jpn Acad SerB , pp. 84
    • Miyagi, T.1
  • 44
    • 0033405059 scopus 로고    scopus 로고
    • Expression of a novel human sialidase encoded by the NEU2 gene
    • Monti E, Preti A, Nesti C, Ballabio A, Borsani G. 1999a. Expression of a novel human sialidase encoded by the NEU2 gene. Glycobiology. 9:1313-1321.
    • (1999) Glycobiology , vol.9 , pp. 1313-1321
    • Monti, E.1    Preti, A.2    Nesti, C.3    Ballabio, A.4    Borsani, G.5
  • 45
    • 0033118290 scopus 로고    scopus 로고
    • Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases
    • Monti E, Preti A, Rossi E, Ballabio A, Borsani G. 1999b. Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics. 57:137-143.
    • (1999) Genomics , vol.57 , pp. 137-143
    • Monti, E.1    Preti, A.2    Rossi, E.3    Ballabio, A.4    Borsani, G.5
  • 47
    • 0036694820 scopus 로고    scopus 로고
    • Recent development in mammalian sialidase molecular biology
    • Monti E, Preti A, Venerando B, Borsani G. 2002. Recent development in mammalian sialidase molecular biology. Neurochem Res. 27:649-663.
    • (2002) Neurochem Res , vol.27 , pp. 649-663
    • Monti, E.1    Preti, A.2    Venerando, B.3    Borsani, G.4
  • 49
    • 2942716748 scopus 로고    scopus 로고
    • Increased levels of insulin and insulin-like growth factor-1 hybrid receptors and decreased glycosylation of the insulin receptor alph and beta-subunits in scrapie-infected neuroblastoma N2a cells
    • Neilsen D, Gyllberg H, Ostlund P, Bergman T, Bedecs K. 2004. Increased levels of insulin and insulin-like growth factor-1 hybrid receptors and decreased glycosylation of the insulin receptor alph and beta-subunits in scrapie-infected neuroblastoma N2a cells. Biochem J. 380:571-579.
    • (2004) Biochem J , vol.380 , pp. 571-579
    • Neilsen, D.1    Gyllberg, H.2    Ostlund, P.3    Bergman, T.4    Bedecs, K.5
  • 51
    • 61649096363 scopus 로고    scopus 로고
    • Insulin-like growth factor I (IGF-I) is a more potent regulator of gene expression than insulin in primary human myoblasts and myotubes
    • Palsgaard J, Brown AE, Jensen M, Borup R, Walker M, De Meyts P. 2009. Insulin-like growth factor I (IGF-I) is a more potent regulator of gene expression than insulin in primary human myoblasts and myotubes. Growth Horm IGF Res. 19:168-178.
    • (2009) Growth Horm IGF Res , vol.19 , pp. 168-178
    • Palsgaard, J.1    Brown, A.E.2    Jensen, M.3    Borup, R.4    Walker, M.5    De Meyts, P.6
  • 53
    • 0346727381 scopus 로고    scopus 로고
    • Five novel mutations in the lysosomal sialidase gene (NEU1) in type II sialidosis patients and assessment of their impact on enzyme activity and intracellular targeting using adenovirus-mediated expression
    • Pattison S, Pankarican M, Rupar CA, Graham FL, Igdoura SA. 2004. Five novel mutations in the lysosomal sialidase gene (NEU1) in type II sialidosis patients and assessment of their impact on enzyme activity and intracellular targeting using adenovirus-mediated expression. Hum Mutat. 23:32-39.
    • (2004) Hum Mutat , vol.23 , pp. 32-39
    • Pattison, S.1    Pankarican, M.2    Rupar, C.A.3    Graham, F.L.4    Igdoura, S.A.5
  • 54
    • 0032513204 scopus 로고    scopus 로고
    • The 67-kDa enzymatically inactive alternatively spliced variant of beta-galactosidase is identical to the elastin/laminin-binding protein
    • Privitera S, Prody CA, Callahan JW, Hinek A. 1998. The 67-kDa enzymatically inactive alternatively spliced variant of beta-galactosidase is identical to the elastin/laminin-binding protein. J Biol Chem. 273:6319-6326.
    • (1998) J Biol Chem , vol.273 , pp. 6319-6326
    • Privitera, S.1    Prody, C.A.2    Callahan, J.W.3    Hinek, A.4
  • 55
    • 0029904847 scopus 로고    scopus 로고
    • Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase Possible implication for intralysosomal catabolism of keratan sulfate
    • Pshezhetsky AV, Potier M. 1996. Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate. J Biol Chem. 271:28359-28365.
    • (1996) J Biol Chem , vol.271 , pp. 28359-28365
    • Pshezhetsky, A.V.1    Potier, M.2
  • 59
    • 0029920035 scopus 로고    scopus 로고
    • Involvement of an endogenous sialidase in skeletal muscle cell differentiation
    • Sato K, Miyagi T. 1996. Involvement of an endogenous sialidase in skeletal muscle cell differentiation. Biochem Biophys Res Commun. 221:826-830.
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 826-830
    • Sato, K.1    Miyagi, T.2
  • 60
    • 0034082628 scopus 로고    scopus 로고
    • Dynamics of nuclei of muscle fibers and connective tissue cells in normal and denervated rat muscles
    • Schmalbruch H, Lewis DM. 2000. Dynamics of nuclei of muscle fibers and connective tissue cells in normal and denervated rat muscles. Muscle Nerve. 23:617-626.
    • (2000) Muscle Nerve , vol.23 , pp. 617-626
    • Schmalbruch, H.1    Lewis, D.M.2
  • 62
    • 0022271052 scopus 로고
    • Response of satellite cells to focal skeletal muscle injury
    • Schultz E, Jaryszak DL, Valliere CR. 1985. Response of satellite cells to focal skeletal muscle injury. Muscle Nerve. 8:217-222.
    • (1985) Muscle Nerve , vol.8 , pp. 217-222
    • Schultz, E.1    Jaryszak, D.L.2    Valliere, C.R.3
  • 63
    • 42149140537 scopus 로고    scopus 로고
    • Enzymatic activity of lysosomal carboxypeptidase (cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1
    • Seyrantepe V, Hinek A, Peng J, Fedjaev M, Ernest S, Kadota Y, Canuel M, Itoh K, Morales CR, Lavoie J, et al. 2008. Enzymatic activity of lysosomal carboxypeptidase (cathepsin) A is required for proper elastic fiber formation and inactivation of endothelin-1. Circulation. 117:1973-1981.
    • (2008) Circulation , vol.117 , pp. 1973-1981
    • Seyrantepe, V.1    Hinek, A.2    Peng, J.3    Fedjaev, M.4    Ernest, S.5    Kadota, Y.6    Canuel, M.7    Itoh, K.8    Morales, C.R.9    Lavoie, J.10
  • 65
    • 0035139227 scopus 로고    scopus 로고
    • Physiology of nitric oxide in skeletal muscle
    • Stamler JS, Meissner G. 2001. Physiology of nitric oxide in skeletal muscle. Physiol Rev. 81:209-237.
    • (2001) Physiol Rev , vol.81 , pp. 209-237
    • Stamler, J.S.1    Meissner, G.2
  • 67
    • 0029122720 scopus 로고
    • Multiple roles of phosphatidylinositol 3-kinase in regulation of glucose transport, amino acid transport, and glucose transporters in L6 skeletal muscle cells
    • Tsakiridis T, McDowell HE, Walker T, Downes CP, Hundal HS, Vranic M, Klip A. 1995. Multiple roles of phosphatidylinositol 3-kinase in regulation of glucose transport, amino acid transport, and glucose transporters in L6 skeletal muscle cells. Endocrinology. 136:4315-4322.
    • (1995) Endocrinology , vol.136 , pp. 4315-4322
    • Tsakiridis, T.1    McDowell, H.E.2    Walker, T.3    Downes, C.P.4    Hundal, H.S.5    Vranic, M.6    Klip, A.7
  • 68
    • 62049084618 scopus 로고    scopus 로고
    • Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4
    • Uemura T, Shiozaki K, Yamaguchi K, Miyazaki S, Satomi S, Kato K, Sakuraba H, Miyagi T. 2009. Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4. Oncogene. 28:1218-1229.
    • (2009) Oncogene , vol.28 , pp. 1218-1229
    • Uemura, T.1    Shiozaki, K.2    Yamaguchi, K.3    Miyazaki, S.4    Satomi, S.5    Kato, K.6    Sakuraba, H.7    Miyagi, T.8


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