메뉴 건너뛰기




Volumn 1802, Issue 2, 2010, Pages 259-268

Vacuolization and alterations of lysosomal membrane proteins in cochlear marginal cells contribute to hearing loss in neuraminidase 1-deficient mice

Author keywords

Cochlea; Endolymphatic potential; Hearing loss; Lysosomes; Sialidosis

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; POTASSIUM CHANNEL KCNQ1; SIALIDASE; VANILLOID RECEPTOR 5; VANILLOID RECEPTOR 6;

EID: 74149087076     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2009.10.008     Document Type: Article
Times cited : (39)

References (32)
  • 2
    • 0034615927 scopus 로고    scopus 로고
    • Processing of lysosomal β-galactosidase: the C-terminal precursor fragment is an essential domain of the mature enzyme.
    • van der Spoel A.C., Bonten E.J., and d'Azzo A. Processing of lysosomal β-galactosidase: the C-terminal precursor fragment is an essential domain of the mature enzyme. J. Biol. Chem. 275 (2000) 10035-10040
    • (2000) J. Biol. Chem. , vol.275 , pp. 10035-10040
    • van der Spoel, A.C.1    Bonten, E.J.2    d'Azzo, A.3
  • 3
    • 0001437175 scopus 로고    scopus 로고
    • Disorders of glycoprotein degradation and structure: α-mannosidosis, β-mannosidosis, fucosidosis, and sialidosis
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw Hill, Inc., New York
    • Thomas G.H. Disorders of glycoprotein degradation and structure: α-mannosidosis, β-mannosidosis, fucosidosis, and sialidosis. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases of Inherited Disease vol. III (2001), McGraw Hill, Inc., New York 3507-3534
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , vol.III , pp. 3507-3534
    • Thomas, G.H.1
  • 4
    • 0034535503 scopus 로고    scopus 로고
    • Lysosomal neuraminidase. Catalytic activation in insect cells is controlled by the protective protein/cathepsin A
    • Bonten E.J., and d'Azzo A. Lysosomal neuraminidase. Catalytic activation in insect cells is controlled by the protective protein/cathepsin A. J. Biol. Chem. 275 (2000) 37657-37663
    • (2000) J. Biol. Chem. , vol.275 , pp. 37657-37663
    • Bonten, E.J.1    d'Azzo, A.2
  • 5
    • 0018346760 scopus 로고
    • Sialidosis: a review of human neuraminidase deficiency
    • Lowden J., and O'Brien J. Sialidosis: a review of human neuraminidase deficiency. Am. J. Hum. Genet. 31 (1979) 1
    • (1979) Am. J. Hum. Genet. , vol.31 , pp. 1
    • Lowden, J.1    O'Brien, J.2
  • 6
    • 0020659404 scopus 로고
    • Sialidosis type 2 in Japan. Clinical study in two siblings cases and review of literature
    • Matsuo T., Egawa I., Okada S., Suhtsugui M., Yamamoto K., and Watanabe M. Sialidosis type 2 in Japan. Clinical study in two siblings cases and review of literature. J. Neurol. Sci. 58 (1983) 45-55
    • (1983) J. Neurol. Sci. , vol.58 , pp. 45-55
    • Matsuo, T.1    Egawa, I.2    Okada, S.3    Suhtsugui, M.4    Yamamoto, K.5    Watanabe, M.6
  • 13
    • 33748910482 scopus 로고    scopus 로고
    • Supporting sensory transduction: cochlear fluid homeostasis and the endocochlear potential
    • Wangemann P. Supporting sensory transduction: cochlear fluid homeostasis and the endocochlear potential. J. Physiol. 576 (2006) 11-21
    • (2006) J. Physiol. , vol.576 , pp. 11-21
    • Wangemann, P.1
  • 14
    • 36048955489 scopus 로고    scopus 로고
    • Mouse models to study inner ear development and hereditary hearing loss
    • Friedman L.M., Dror A.A., and Avraham K.B. Mouse models to study inner ear development and hereditary hearing loss. Int. J. Dev. Biol. 51 (2007) 609-631
    • (2007) Int. J. Dev. Biol. , vol.51 , pp. 609-631
    • Friedman, L.M.1    Dror, A.A.2    Avraham, K.B.3
  • 16
    • 0021296004 scopus 로고
    • Electrochemical heterogeneity of the cochlear endolymph: effect of acetazolamide
    • Sterkers O., Saumon G., Tran Ba Huy P., Ferrary E., and Amiel C. Electrochemical heterogeneity of the cochlear endolymph: effect of acetazolamide. Am. J. Physiol. 246 (1984) F47-F53
    • (1984) Am. J. Physiol. , vol.246
    • Sterkers, O.1    Saumon, G.2    Tran Ba Huy, P.3    Ferrary, E.4    Amiel, C.5
  • 17
    • 0023583084 scopus 로고
    • Early effects of acetazolamide on anionic activities of the guinea pig endolymph: evidence for active function of carbonic anhydrase in the cochlea
    • Ikeda K., Kusakari J., Takasaka T., and Saito Y. Early effects of acetazolamide on anionic activities of the guinea pig endolymph: evidence for active function of carbonic anhydrase in the cochlea. Hear. Res. 31 (1987) 211-216
    • (1987) Hear. Res. , vol.31 , pp. 211-216
    • Ikeda, K.1    Kusakari, J.2    Takasaka, T.3    Saito, Y.4
  • 18
    • 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., and d'Azzo A. Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice. Hum. Mol. Genet. 11 (2002) 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
  • 21
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases-nature's most versatile proton pumps
    • Nishi T., and Forgac M. The vacuolar (H+)-ATPases-nature's most versatile proton pumps. Nat. Rev. 3 (2002) 94-103
    • (2002) Nat. Rev. , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 22
    • 0032879483 scopus 로고    scopus 로고
    • Cochlear fluid space dimensions for six species derived from reconstructions of three-dimensional magnetic resonance images
    • Thorne M., Salt A.N., DeMott J.E., Henson M.M., Henson Jr. O.W., and Gewalt S.L. Cochlear fluid space dimensions for six species derived from reconstructions of three-dimensional magnetic resonance images. Laryngoscope 109 (1999) 1661-1668
    • (1999) Laryngoscope , vol.109 , pp. 1661-1668
    • Thorne, M.1    Salt, A.N.2    DeMott, J.E.3    Henson, M.M.4    Henson Jr., O.W.5    Gewalt, S.L.6
  • 23
    • 0034957276 scopus 로고    scopus 로고
    • Morphological alterations in the inner ear of the arylsulfatase A-deficient mouse
    • Coenen R., Gieselmann V., and Lullmann-Rauch R. Morphological alterations in the inner ear of the arylsulfatase A-deficient mouse. Acta neuropathologica 101 (2001) 491-498
    • (2001) Acta neuropathologica , vol.101 , pp. 491-498
    • Coenen, R.1    Gieselmann, V.2    Lullmann-Rauch, R.3
  • 29
    • 0038361002 scopus 로고    scopus 로고
    • Mice lacking the B1 subunit of H+ -ATPase have normal hearing
    • Dou H., Finberg K., Cardell E.L., Lifton R., and Choo D. Mice lacking the B1 subunit of H+ -ATPase have normal hearing. Hear. Res. 180 (2003) 76-84
    • (2003) Hear. Res. , vol.180 , pp. 76-84
    • Dou, H.1    Finberg, K.2    Cardell, E.L.3    Lifton, R.4    Choo, D.5
  • 31
    • 2942648144 scopus 로고    scopus 로고
    • Hearing threshold elevation precedes hair-cell loss in prestin knockout mice
    • Wu X., Gao J., Guo Y., and Zuo J. Hearing threshold elevation precedes hair-cell loss in prestin knockout mice. Brain Res. 126 (2004) 30-37
    • (2004) Brain Res. , vol.126 , pp. 30-37
    • Wu, X.1    Gao, J.2    Guo, Y.3    Zuo, J.4
  • 32
    • 6944226811 scopus 로고    scopus 로고
    • Targeting macrophages with baculovirus-produced lysosomal enzymes: implications for enzyme replacement therapy of the glycoprotein storage disorder galactosialidosis
    • Bonten E.J., Wang D., Toy J.N., Mann L., Mignardot A., Yogalingam G., and D'Azzo A. Targeting macrophages with baculovirus-produced lysosomal enzymes: implications for enzyme replacement therapy of the glycoprotein storage disorder galactosialidosis. FASEB J. 18 (2004) 971-973
    • (2004) FASEB J. , vol.18 , pp. 971-973
    • Bonten, E.J.1    Wang, D.2    Toy, J.N.3    Mann, L.4    Mignardot, A.5    Yogalingam, G.6    D'Azzo, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.