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Volumn 244, Issue 1, 1997, Pages 21-30

Production and characterization of recombinant active mouse gelatinase B from eukaryotic cells and in vivo effects after intravenous administration

Author keywords

Expression; Gelatinase B; Leukocytosis; Matrix metalloproteinase; Pichia pastoris

Indexed keywords

GELATINASE B; MATRIX METALLOPROTEINASE; RECOMBINANT ENZYME;

EID: 0031049458     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00021.x     Document Type: Article
Times cited : (37)

References (39)
  • 1
    • 0028346025 scopus 로고
    • Direct evidence linking expression of matrix metalloproteinase 9 (92-kDa gelatinase/ collagenase) to the metastatic phenotype in transformed rat embryo cells
    • Bernhard, E. J., Gruber, S. B. & Muschel, R. J. (1994) Direct evidence linking expression of matrix metalloproteinase 9 (92-kDa gelatinase/ collagenase) to the metastatic phenotype in transformed rat embryo cells, Proc. Natl Acad. Sci. USA 91, 4293-4297.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4293-4297
    • Bernhard, E.J.1    Gruber, S.B.2    Muschel, R.J.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0023650538 scopus 로고
    • Electroporation for the efficient transfection of mammalian cells with DNA
    • Chu, G., Hayakawa, H. & Berg, P. (1987) Electroporation for the efficient transfection of mammalian cells with DNA. Nucleic Acids Res. 15, 1311-1326.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1311-1326
    • Chu, G.1    Hayakawa, H.2    Berg, P.3
  • 5
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg, J. M., Vedvick, T. S. & Raschke, W. C. (1993) Recent advances in the expression of foreign genes in Pichia pastoris, Biotechnology 11, 905-910.
    • (1993) Biotechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 6
    • 0027435065 scopus 로고
    • Tissue inhibitor of metalloproteinases (TIMP, aka EPA): Structure, control of expression and biological functions
    • Denhardt, D. T., Feng, B., Edwards, D. R., Cocuzzi, E. T. & Malyankar, U. M. (1993) Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions, Pharmac. Ther. 59, 329-341.
    • (1993) Pharmac. Ther. , vol.59 , pp. 329-341
    • Denhardt, D.T.1    Feng, B.2    Edwards, D.R.3    Cocuzzi, E.T.4    Malyankar, U.M.5
  • 7
    • 0026721062 scopus 로고
    • The matrix metalloproteinases and their natural inhibitors: Prospects for treating degenerative tissue diseases
    • Docherty, A. J. P., O'Connell, J., Crabbe, T., Angal, S. & Murphy, G. (1992) The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases, Trends Biotechnol. 10, 200-207.
    • (1992) Trends Biotechnol. , vol.10 , pp. 200-207
    • Docherty, A.J.P.1    O'Connell, J.2    Crabbe, T.3    Angal, S.4    Murphy, G.5
  • 8
    • 0026442957 scopus 로고
    • Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders
    • Gijbels, K., Masure, S., Carton, H. & Opdenakker, G. (1992) Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders, J. Neuroimmunol. 41, 29-34.
    • (1992) J. Neuroimmunol. , vol.41 , pp. 29-34
    • Gijbels, K.1    Masure, S.2    Carton, H.3    Opdenakker, G.4
  • 9
    • 0027368518 scopus 로고
    • Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein
    • Gijbels, K., Proost, P., Masure, S., Carton, H., Billiau, A. & Opdenakker, G. (1993) Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein, J. Neurosci. Res. 36, 432-440.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 432-440
    • Gijbels, K.1    Proost, P.2    Masure, S.3    Carton, H.4    Billiau, A.5    Opdenakker, G.6
  • 10
    • 0027366465 scopus 로고
    • Cloning and expression of the cDNA encoding mouse neutrophil gelatinase: Demonstration of coordinate secondary granule protein gene expression during terminal neutrophil maturation
    • Graubert, T., Johnston, J. & Berliner, N. (1993) Cloning and expression of the cDNA encoding mouse neutrophil gelatinase: demonstration of coordinate secondary granule protein gene expression during terminal neutrophil maturation, Blood 82, 3192-3197.
    • (1993) Blood , vol.82 , pp. 3192-3197
    • Graubert, T.1    Johnston, J.2    Berliner, N.3
  • 13
    • 0029594498 scopus 로고
    • Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis
    • MacDougall, J. R. & Matrisian, L. M. (1995) Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis, Cancer Metastasis Rev. 14, 351-362.
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 351-362
    • MacDougall, J.R.1    Matrisian, L.M.2
  • 14
    • 0025102477 scopus 로고
    • Human hepatoma cells produce an 85 kDa gelatinase regulated by phorbol 12-myristate 13-acetate
    • Masure, S., Billiau, A., Van Damme, J. & Opdenakker, G. (1990) Human hepatoma cells produce an 85 kDa gelatinase regulated by phorbol 12-myristate 13-acetate, Biochim. Biophys. Acta 1054, 317-325.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 317-325
    • Masure, S.1    Billiau, A.2    Van Damme, J.3    Opdenakker, G.4
  • 15
    • 0025808816 scopus 로고
    • Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8
    • Masure, S., Proost, P., Van Damme, J. & Opdenakker, G. (1991) Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8, Eur. J. Biochem. 198, 391-398.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 391-398
    • Masure, S.1    Proost, P.2    Van Damme, J.3    Opdenakker, G.4
  • 16
    • 0027426024 scopus 로고
    • Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation
    • Masure, S., Nys, G., Fiten, P., Van Damme, J. & Opdenakker, G. (1993) Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation, Eur. J. Biochem. 218, 129-141.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 129-141
    • Masure, S.1    Nys, G.2    Fiten, P.3    Van Damme, J.4    Opdenakker, G.5
  • 18
  • 19
    • 0030052834 scopus 로고    scopus 로고
    • Human gelatinase B, a marker enzyme in rheumatoid arthritis, is inhibited by D-penicillamine: Anti-rheumatic activity by protease inhibition
    • Norga, K., Grillet, B., Masure, S., Paemen, L. & Opdenakker, G. (1996) Human gelatinase B, a marker enzyme in rheumatoid arthritis, is inhibited by D-penicillamine: anti-rheumatic activity by protease inhibition, Clin. Rheumatol. 15, 31-34.
    • (1996) Clin. Rheumatol. , vol.15 , pp. 31-34
    • Norga, K.1    Grillet, B.2    Masure, S.3    Paemen, L.4    Opdenakker, G.5
  • 20
    • 0028957812 scopus 로고
    • Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase = gelatinase B) in osteoclasts: Implications for bone resorption
    • Okada, Y., Naka, K., Kawamura, K., Matsumoto, T., Nakanishi, I., Fujimoto, N., Sato, H. & Seiki, M. (1995) Localization of matrix metalloproteinase 9 (92-kilodalton gelatinase/type IV collagenase = gelatinase B) in osteoclasts: implications for bone resorption, Lab. Invest. 72, 311-322.
    • (1995) Lab. Invest. , vol.72 , pp. 311-322
    • Okada, Y.1    Naka, K.2    Kawamura, K.3    Matsumoto, T.4    Nakanishi, I.5    Fujimoto, N.6    Sato, H.7    Seiki, M.8
  • 22
    • 0025883322 scopus 로고
    • Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis
    • Opdenakker, G., Masure, S., Grillet, B. & Van Damme, J. (1991 b) Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis, Lymphokine Cytokine Res. 10, 317-324.
    • (1991) Lymphokine Cytokine Res. , vol.10 , pp. 317-324
    • Opdenakker, G.1    Masure, S.2    Grillet, B.3    Van Damme, J.4
  • 23
    • 0026890915 scopus 로고
    • Cytokines and proteases in invasive processes: Molecular similarities between inflammation and cancer
    • Opdenakker, G. & Van Damme, J. (1992) Cytokines and proteases in invasive processes: molecular similarities between inflammation and cancer, Cytokine 4, 251-258.
    • (1992) Cytokine , vol.4 , pp. 251-258
    • Opdenakker, G.1    Van Damme, J.2
  • 24
    • 0028328881 scopus 로고
    • Cytokine-regulated proteases in autoimmune diseases
    • Opdenakker, G. & Van Damme, J. (1994) Cytokine-regulated proteases in autoimmune diseases, Immunol. Today 15, 103-107.
    • (1994) Immunol. Today , vol.15 , pp. 103-107
    • Opdenakker, G.1    Van Damme, J.2
  • 25
    • 0028005697 scopus 로고
    • Evaluation of gelatinases and IL-6 in the cerebrospinal fluid of patients with optic neuritis, multiple sclerosis and other inflammatory neurological diseases
    • Paemen, L., Olsson, T., Söderström, M., Van Damme, J. & Opdenakker, G. (1994) Evaluation of gelatinases and IL-6 in the cerebrospinal fluid of patients with optic neuritis, multiple sclerosis and other inflammatory neurological diseases, Eur. J. Neurol. 1, 55-63.
    • (1994) Eur. J. Neurol. , vol.1 , pp. 55-63
    • Paemen, L.1    Olsson, T.2    Söderström, M.3    Van Damme, J.4    Opdenakker, G.5
  • 26
    • 0029888573 scopus 로고    scopus 로고
    • The gelatinase inhibitory activity of tetracyclines and chemically modified tetracycline analogues as measured by a novel microtiter assay for inhibitors
    • Paemen, L., Martens, E., Norga, K., Masure, S., Roets, E., Hoogmartens, J. & Opdenakker, G. (1996) The gelatinase inhibitory activity of tetracyclines and chemically modified tetracycline analogues as measured by a novel microtiter assay for inhibitors, Biochem. Pharmacol. 52, 105-111.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 105-111
    • Paemen, L.1    Martens, E.2    Norga, K.3    Masure, S.4    Roets, E.5    Hoogmartens, J.6    Opdenakker, G.7
  • 27
    • 0028069617 scopus 로고
    • Characteristics of 92 kDa type IV collagenase/gelatinase produced by granulocytic leukemia cells: Structure, expression of cDNA in E. Coli and enzymic properties
    • Pourmotabbed, T., Solomon, T. L., Hasty, K. A. & Mainardi, C. L. (1994) Characteristics of 92 kDa type IV collagenase/gelatinase produced by granulocytic leukemia cells: structure, expression of cDNA in E. Coli and enzymic properties, Biochim. Biophys. Acta 1204, 97-107.
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 97-107
    • Pourmotabbed, T.1    Solomon, T.L.2    Hasty, K.A.3    Mainardi, C.L.4
  • 28
    • 0028223234 scopus 로고
    • High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development
    • Reponen, P., Sahlberg, C., Munaut, C., Thesleff, I. & Tryggvason, K. (1994) High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development. J. Cell Biol. 124, 1091-1102.
    • (1994) J. Cell Biol. , vol.124 , pp. 1091-1102
    • Reponen, P.1    Sahlberg, C.2    Munaut, C.3    Thesleff, I.4    Tryggvason, K.5
  • 31
    • 0030019731 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis
    • Sato, H. & Seiki, M. (1996) Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis, J. Biochem. 119, 209-215.
    • (1996) J. Biochem. , vol.119 , pp. 209-215
    • Sato, H.1    Seiki, M.2
  • 32
    • 14744304041 scopus 로고
    • Rapid selection using G-418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression
    • Scorer, C. A., Clare, J. J., McCombie, W. R., Romanos, M. A. & Sreekrishna, K. (1994) Rapid selection using G-418 of high copy number transformants of Pichia pastoris for high-level foreign gene expression, Biotechnology 12, 181-184.
    • (1994) Biotechnology , vol.12 , pp. 181-184
    • Scorer, C.A.1    Clare, J.J.2    McCombie, W.R.3    Romanos, M.A.4    Sreekrishna, K.5
  • 35
    • 0025782511 scopus 로고
    • Production and identification of natural monocyte chemotactic protein from virally infected murine fibroblasts. Relationship with the product of the mouse competence (JE) gene
    • Van Damme, J., Decock, B., Bertini, R., Conings, R., Lenaerts, J.-P., Put, W., Opdenakker, G. & Mantovani, A. (1991) Production and identification of natural monocyte chemotactic protein from virally infected murine fibroblasts. Relationship with the product of the mouse competence (JE) gene, Eur. J. Biochem. 199, 223-229.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 223-229
    • Van Damme, J.1    Decock, B.2    Bertini, R.3    Conings, R.4    Lenaerts, J.-P.5    Put, W.6    Opdenakker, G.7    Mantovani, A.8
  • 36
    • 0026161901 scopus 로고
    • The cytokineprotease connection: Identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers
    • Van Ranst, M., Norga, K., Masure, S., Proost, P., Vandekerckhove, F., Auwerx, J., Van Damme, J. & Opdenakker, G. (1991) The cytokineprotease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers, Cytokine 3, 231-239.
    • (1991) Cytokine , vol.3 , pp. 231-239
    • Van Ranst, M.1    Norga, K.2    Masure, S.3    Proost, P.4    Vandekerckhove, F.5    Auwerx, J.6    Van Damme, J.7    Opdenakker, G.8
  • 37
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H. E. & Birkedal-Hansen, H. (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family, Proc. Natl Acad. Sci. USA 87, 5578-5582.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 38
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, G. A. & Goldberg, G. I. (1989) SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages, J. Biol. Chem. 264, 17 213-17 221.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 39
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J. F. (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling, FASEB J. 5, 2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.