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Volumn 244, Issue 2, 1997, Pages 279-285

Synthesis, sorting, and processing into distinct isoforms of human macrophage chitotriosidase

Author keywords

Chitinase; Chitotriosidase; Macrophage; Processing; Sorting

Indexed keywords

CHITINASE;

EID: 0031039858     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00279.x     Document Type: Article
Times cited : (155)

References (26)
  • 1
    • 0000502209 scopus 로고
    • Glucosylceramide lipidoses: Gaucher disease
    • Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds McGraw-Hill, New York
    • Barranger, J. A. & Ginns, E. I. (1989) Glucosylceramide lipidoses: Gaucher disease, in The metabolic basis of inherited disease (Scriver, C. R., Beaudet, A. L., Sly, W. S. & Valle, D., eds) pp. 1677-1698, McGraw-Hill, New York.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 1677-1698
    • Barranger, J.A.1    Ginns, E.I.2
  • 3
    • 0028911536 scopus 로고
    • Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins
    • Renkema, G. H., Boot, R. G., Muijsers, A. O., Donker-Koopman, W. E. & Aerts, J. M. F. G. (1995) Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins, J. Biol. Chem. 270, 2198-2202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2198-2202
    • Renkema, G.H.1    Boot, R.G.2    Muijsers, A.O.3    Donker-Koopman, W.E.4    Aerts, J.M.F.G.5
  • 4
    • 0027505001 scopus 로고
    • Human cartilage gp-39, A major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family
    • Hakala, B. E., White, C. & Recklies, A. D. (1993) Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family, J. Biol. Chem. 268, 25803-25810.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25803-25810
    • Hakala, B.E.1    White, C.2    Recklies, A.D.3
  • 5
    • 0028799896 scopus 로고
    • Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages
    • Boot, R. G., Renkema, G. H., Strijland, A., van Zonneveld, A. J. & Aerts, J. M. F. G. (1995) Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages, J. Biol. Chem. 270, 26252-26256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26252-26256
    • Boot, R.G.1    Renkema, G.H.2    Strijland, A.3    Van Zonneveld, A.J.4    Aerts, J.M.F.G.5
  • 9
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda, M. J. & Robbins, P. W. (1991) Chitinase is required for cell separation during growth of Saccharomyces cerevisiae, J. Biol. Chem. 266, 19758-19767.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19758-19767
    • Kuranda, M.J.1    Robbins, P.W.2
  • 10
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts
    • Hasilik, A. & Neufeld, E. F. (1980) Biosynthesis of lysosomal enzymes in fibroblasts, J. Biol. Chem. 255, 4937-4945.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 11
    • 0025640959 scopus 로고
    • Role of lysosomal and cytosolic pH in the regulation of macrophage enzyme secretion
    • Tapper, H. & Sundler, R. (1990) Role of lysosomal and cytosolic pH in the regulation of macrophage enzyme secretion, Biochem. J. 272, 407-414.
    • (1990) Biochem. J. , vol.272 , pp. 407-414
    • Tapper, H.1    Sundler, R.2
  • 12
    • 0029039148 scopus 로고
    • Structure and function of a family of chitinase isozymes from Brugian microfilariae
    • Fuhrman, J. A., Lee, J. & Dalamagas, D. (1995) Structure and function of a family of chitinase isozymes from Brugian microfilariae, Exp. Parasitol. 80, 672-680.
    • (1995) Exp. Parasitol. , vol.80 , pp. 672-680
    • Fuhrman, J.A.1    Lee, J.2    Dalamagas, D.3
  • 13
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi, Y., Misumi, Y., Takatsuki, A., Tamura, G., Miki, K. & Ikehara, Y. (1986) Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes, J. Biol. Chem. 261, 11398-11403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Misumi, Y.2    Takatsuki, A.3    Tamura, G.4    Miki, K.5    Ikehara, Y.6
  • 15
    • 0023019126 scopus 로고
    • Comparison of the properties of a soluble form of glucocerebrosidase from human urine with those of the membrane-associated tissue enzyme
    • Aerts, J. M. F. G., Donker-Koopman, W. E., Koot, M., Murray, G. J., Barranger, J. A., Tager, J. M. & Schram, A. W. (1986) Comparison of the properties of a soluble form of glucocerebrosidase from human urine with those of the membrane-associated tissue enzyme, Biochim. Biophys. Acta 863, 63-70.
    • (1986) Biochim. Biophys. Acta , vol.863 , pp. 63-70
    • Aerts, J.M.F.G.1    Donker-Koopman, W.E.2    Koot, M.3    Murray, G.J.4    Barranger, J.A.5    Tager, J.M.6    Schram, A.W.7
  • 17
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors
    • Kornfeld, S. (1992) Structure and function of the mannose 6-phosphate/insulin-like growth factor II receptors, Annu. Rev. Biochem. 61, 307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 18
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 280, 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 19
    • 0028170801 scopus 로고
    • Crystal structure of endo-beta-N-acetylglucosaminidase F-1, an alpha/beta-barrel enzyme adapted for a complex substrate
    • Vanroey, P., Rao, V., Plummer, T. H. & Tarentino, A. L. (1994) Crystal structure of endo-beta-N-acetylglucosaminidase F-1, an alpha/beta-barrel enzyme adapted for a complex substrate, Biochemistry 33, 13989-13996.
    • (1994) Biochemistry , vol.33 , pp. 13989-13996
    • Vanroey, P.1    Rao, V.2    Plummer, T.H.3    Tarentino, A.L.4
  • 21
    • 0028033747 scopus 로고
    • A proposed structure for 'Family 18' chitinases - A possible function for narbonin
    • Coulson, A. F. W. (1994) A proposed structure for 'Family 18' chitinases - A possible function for narbonin, FEBS Lett. 354, 41-44.
    • (1994) FEBS Lett. , vol.354 , pp. 41-44
    • Coulson, A.F.W.1
  • 22
    • 0026565262 scopus 로고
    • Transmission-blocking antibodies recognize microfilarial chitinase in Brugian lymphatic filariasis
    • Fuhrman, J. A., Lane, W. S., Smith, R. F., Piessens, W. F. & Perler, F. B. (1992) Transmission-blocking antibodies recognize microfilarial chitinase in Brugian lymphatic filariasis, Proc. Natl Acad. Sci. USA 89, 1548-1552.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1548-1552
    • Fuhrman, J.A.1    Lane, W.S.2    Smith, R.F.3    Piessens, W.F.4    Perler, F.B.5
  • 23
    • 0027668880 scopus 로고
    • Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta
    • Kramer, K. J., Corpuz, L., Choi, H. K. & Mathukrishnan, S. (1993) Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta, Insect Biochem. Mol. Biol. 23, 691-701
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 691-701
    • Kramer, K.J.1    Corpuz, L.2    Choi, H.K.3    Mathukrishnan, S.4
  • 24
    • 0028145771 scopus 로고
    • The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulons WL-12 in chitin degradation
    • Watanabe, T., Ito, Y., Yamada, T., Hashimoto, M., Sekine, S. & Tanaka, H. (1994) The roles of the C-terminal domain and type III domains of chitinase A1 from Bacillus circulons WL-12 in chitin degradation, J. Bacteriol. 176, 4465-4472.
    • (1994) J. Bacteriol. , vol.176 , pp. 4465-4472
    • Watanabe, T.1    Ito, Y.2    Yamada, T.3    Hashimoto, M.4    Sekine, S.5    Tanaka, H.6
  • 25
    • 0028925347 scopus 로고
    • Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytic processed form
    • Blaak, H. & Schrempf, H. (1995) Binding and substrate specificities of a Streptomyces olivaceoviridis chitinase in comparison with its proteolytic processed form, Eur. J. Biochem. 229, 132-139.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 132-139
    • Blaak, H.1    Schrempf, H.2
  • 26
    • 0026499523 scopus 로고
    • The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase
    • Lerner, D. R. & Raikhel, N. V. (1992) The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase, J. Biol. Chem. 267, 11085-11091.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11085-11091
    • Lerner, D.R.1    Raikhel, N.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.