메뉴 건너뛰기




Volumn 1802, Issue 7-8, 2010, Pages 659-672

Muscle degeneration in neuraminidase 1-deficient mice results from infiltration of the muscle fibers by expanded connective tissue

Author keywords

ECM; Lysosome; Metalloproteinase; Muscle biopsy; NEU1; Sialidosis

Indexed keywords

CATHEPSIN; CELL MARKER; COLLAGEN; GLYCOSIDASE; METALLOPROTEINASE; NEUROMINIDASE 1; UNCLASSIFIED DRUG;

EID: 77953812943     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.04.002     Document Type: Article
Times cited : (42)

References (38)
  • 1
    • 0030451974 scopus 로고    scopus 로고
    • Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis
    • Bonten E., van der Spoel A., Fornerod M., Grosveld G., d'Azzo A. Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. Genes Dev. 1996, 10:3156-3169.
    • (1996) Genes Dev. , vol.10 , pp. 3156-3169
    • Bonten, E.1    van der Spoel, A.2    Fornerod, M.3    Grosveld, G.4    d'Azzo, A.5
  • 2
    • 0032536852 scopus 로고    scopus 로고
    • Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A
    • van der Spoel A., Bonten E., d'Azzo A. Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A. EMBO J. 1998, 17:1588-1597.
    • (1998) EMBO J. , vol.17 , pp. 1588-1597
    • van der Spoel, A.1    Bonten, E.2    d'Azzo, A.3
  • 3
    • 0001437175 scopus 로고    scopus 로고
    • Disorders of glycoprotein degradation and structure: a-mannosidosis, b-mannosidosis, fucosidosis, and sialidosis
    • 3s, McGraw Hill, Inc., New York
    • Thomas G.H. Disorders of glycoprotein degradation and structure: a-mannosidosis, b-mannosidosis, fucosidosis, and sialidosis. The Metabolic and Molecular Bases of Inherited Disease 2001, vol. III:3507-3534. McGraw Hill, Inc., New York.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3507-3534
    • Thomas, G.H.1
  • 4
    • 0000188386 scopus 로고    scopus 로고
    • Galactosialidosis
    • s3, McGraw-Hill Publishing Co., New York, C. Scriver, A. Beaudet, W. Sly, D. Valle (Eds.)
    • DAzzo A., Andria G., Strisciuglio P. Galactosialidosis. The Metabolic and Molecular Bases of Inherited Disease 2001, vol. 3:3811-3826. McGraw-Hill Publishing Co., New York. C. Scriver, A. Beaudet, W. Sly, D. Valle (Eds.).
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3811-3826
    • DAzzo, A.1    Andria, G.2    Strisciuglio, P.3
  • 5
    • 0034326899 scopus 로고    scopus 로고
    • Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis
    • Bonten E.J., Arts W.F., Beck M., Covanis A., Donati M.A., Parini R., Zammarchi E., d'Azzo A. Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis. Hum. Mol. Genet. 2000, 9:2715-2725.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2715-2725
    • Bonten, E.J.1    Arts, W.F.2    Beck, M.3    Covanis, A.4    Donati, M.A.5    Parini, R.6    Zammarchi, E.7    d'Azzo, A.8
  • 6
    • 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. Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice. Hum. Mol. Genet. 2002, 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
  • 8
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews N.W. Regulated secretion of conventional lysosomes. Trends Cell Biol. 2000, 10:316-321.
    • (2000) Trends Cell Biol. , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 9
    • 28244441019 scopus 로고    scopus 로고
    • Primary and secondary elastin-binding protein defect leads to impaired elastogenesis in fibroblasts from GM1-gangliosidosis patients
    • Caciotti A., Donati M.A., Bardelli T., d'Azzo A., Massai G., Luciani L., Zammarchi E., Morrone A. Primary and secondary elastin-binding protein defect leads to impaired elastogenesis in fibroblasts from GM1-gangliosidosis patients. Am. J. Pathol. 2005, 167:1689-1698.
    • (2005) Am. J. Pathol. , vol.167 , pp. 1689-1698
    • Caciotti, A.1    Donati, M.A.2    Bardelli, T.3    d'Azzo, A.4    Massai, G.5    Luciani, L.6    Zammarchi, E.7    Morrone, A.8
  • 10
    • 1942425113 scopus 로고    scopus 로고
    • New mutations in the PPBG gene lead to loss of PPCA protein which affects the level of the beta-galactosidase/neuraminidase complex and the EBP-receptor
    • Malvagia S., Morrone A., Caciotti A., Bardelli T., d'Azzo A., Ancora G., Zammarchi E., Donati M.A. New mutations in the PPBG gene lead to loss of PPCA protein which affects the level of the beta-galactosidase/neuraminidase complex and the EBP-receptor. Mol. Genet. Metab. 2004, 82:48-55.
    • (2004) Mol. Genet. Metab. , vol.82 , pp. 48-55
    • Malvagia, S.1    Morrone, A.2    Caciotti, A.3    Bardelli, T.4    d'Azzo, A.5    Ancora, G.6    Zammarchi, E.7    Donati, M.A.8
  • 11
    • 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 A.V., von Itzstein M., Starcher B. Lysosomal sialidase (neuraminidase-1) is targeted to the cell surface in a multiprotein complex that facilitates elastic fiber assembly. J. Biol. Chem. 2006, 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
  • 13
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty E.G., Kadler K.E. Procollagen trafficking, processing and fibrillogenesis. J. Cell. Sci. 2005, 118:1341-1353.
    • (2005) J. Cell. Sci. , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 14
    • 0037832412 scopus 로고    scopus 로고
    • The basement membrane/basal lamina of skeletal muscle
    • Sanes J.R. The basement membrane/basal lamina of skeletal muscle. J. Biol. Chem. 2003, 278:12601-12604.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12601-12604
    • Sanes, J.R.1
  • 15
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder S.J. The complexities of dystroglycan. Trends Biochem. Sci. 2001, 26:118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 16
    • 0346783321 scopus 로고    scopus 로고
    • A Tcf4-positive mesodermal population provides a prepattern for vertebrate limb muscle patterning
    • Kardon G., Harfe B.D., Tabin C.J. A Tcf4-positive mesodermal population provides a prepattern for vertebrate limb muscle patterning. Dev. Cell 2003, 5:937-944.
    • (2003) Dev. Cell , vol.5 , pp. 937-944
    • Kardon, G.1    Harfe, B.D.2    Tabin, C.J.3
  • 17
    • 0029294613 scopus 로고
    • In situ detection of fragmented DNA (TUNEL assay) fails to discriminate among apoptosis, necrosis, and autolytic cell death: a cautionary note
    • Grasl-Kraupp B., Ruttkay-Nedecky B., Koudelka H., Bukowska K., Bursch W., Schulte-Hermann R. In situ detection of fragmented DNA (TUNEL assay) fails to discriminate among apoptosis, necrosis, and autolytic cell death: a cautionary note. Hepatology 1995, 21:1465-1468.
    • (1995) Hepatology , vol.21 , pp. 1465-1468
    • Grasl-Kraupp, B.1    Ruttkay-Nedecky, B.2    Koudelka, H.3    Bukowska, K.4    Bursch, W.5    Schulte-Hermann, R.6
  • 19
    • 0036205065 scopus 로고    scopus 로고
    • Evans Blue Dye as an in vivo marker of myofibre damage: optimising parameters for detecting initial myofibre membrane permeability
    • Hamer P.W., McGeachie J.M., Davies M.J., Grounds M.D. Evans Blue Dye as an in vivo marker of myofibre damage: optimising parameters for detecting initial myofibre membrane permeability. J Anat 2002, 200:69-79.
    • (2002) J Anat , vol.200 , pp. 69-79
    • Hamer, P.W.1    McGeachie, J.M.2    Davies, M.J.3    Grounds, M.D.4
  • 20
    • 74149087076 scopus 로고    scopus 로고
    • Vacuolization and alterations of lysosomal membrane proteins in cochlear marginal cells contribute to hearing loss in neuraminidase 1-deficient mice
    • Wu X., Steigelman K.A., Bonten E., Hu H., He W., Ren T., Zuo J., d'Azzo A. Vacuolization and alterations of lysosomal membrane proteins in cochlear marginal cells contribute to hearing loss in neuraminidase 1-deficient mice. Biochim. Biophys. Acta 2010, 1802:259-268.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 259-268
    • Wu, X.1    Steigelman, K.A.2    Bonten, E.3    Hu, H.4    He, W.5    Ren, T.6    Zuo, J.7    d'Azzo, A.8
  • 21
    • 33749261091 scopus 로고    scopus 로고
    • Autophagic vacuolar myopathy
    • Nishino I. Autophagic vacuolar myopathy. Semin. Pediatr. Neurol. 2006, 13:90-95.
    • (2006) Semin. Pediatr. Neurol. , vol.13 , pp. 90-95
    • Nishino, I.1
  • 23
    • 34548613865 scopus 로고    scopus 로고
    • Role of autophagy in the pathogenesis of Pompe disease
    • Raben N., Roberts A., Plotz P.H. Role of autophagy in the pathogenesis of Pompe disease. Acta Myol. 2007, 26:45-48.
    • (2007) Acta Myol. , vol.26 , pp. 45-48
    • Raben, N.1    Roberts, A.2    Plotz, P.H.3
  • 25
    • 27744471928 scopus 로고    scopus 로고
    • There's more to life than neurotransmission: the regulation of exocytosis by synaptotagmin VII
    • Andrews N.W., Chakrabarti S. There's more to life than neurotransmission: the regulation of exocytosis by synaptotagmin VII. Trends Cell Biol. 2005, 15:626-631.
    • (2005) Trends Cell Biol. , vol.15 , pp. 626-631
    • Andrews, N.W.1    Chakrabarti, S.2
  • 27
    • 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-2
    • Hinek A., Bodnaruk T.D., Bunda S., Wang Y., Liu K. 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-2. Am. J. Pathol. 2008, 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
  • 29
    • 0033582517 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides
    • Miyagi T., Wada T., Iwamatsu A., Hata K., Yoshikawa Y., Tokuyama S., Sawada M. Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J. Biol. Chem. 1999, 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
  • 31
    • 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. Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4. Oncogene 2009, 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
  • 32
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: they're not just for matrix anymore
    • McCawley L.J., Matrisian L.M. Matrix metalloproteinases: they're not just for matrix anymore. Curr. Opin. Cell Biol. 2001, 13:534-540.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 33
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A.F., Matrisian L.M. Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 1997, 89:1260-1270.
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 34
    • 0032959030 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors
    • Nakada M., Nakamura H., Ikeda E., Fujimoto N., Yamashita J., Sato H., Seiki M., Okada Y. Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors. Am. J. Pathol. 1999, 154:417-428.
    • (1999) Am. J. Pathol. , vol.154 , pp. 417-428
    • Nakada, M.1    Nakamura, H.2    Ikeda, E.3    Fujimoto, N.4    Yamashita, J.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 36
    • 0033981058 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies
    • Choi Y.C., Dalakas M.C. Expression of matrix metalloproteinases in the muscle of patients with inflammatory myopathies. Neurology 2000, 54:65-71.
    • (2000) Neurology , vol.54 , pp. 65-71
    • Choi, Y.C.1    Dalakas, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.