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Volumn 5, Issue 5, 1999, Pages 1115-1124

Matrix metalloproteinase production by bone marrow mononuclear cells from normal individuals and patients with acute and chronic myeloid leukemia or myelodysplastic syndromes

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE A; MATRIX METALLOPROTEINASE; MESSENGER RNA; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 0032937216     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (104)

References (50)
  • 1
    • 0026017392 scopus 로고
    • Leukemia and the disruption of normal hematopoiesis
    • Sawyers, C. L., Denny, C. T., and Witte, O. N. Leukemia and the disruption of normal hematopoiesis. Cell, 64: 337-350, 1991.
    • (1991) Cell , vol.64 , pp. 337-350
    • Sawyers, C.L.1    Denny, C.T.2    Witte, O.N.3
  • 2
    • 0029310597 scopus 로고
    • Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease
    • Ries, C., and Petrides, P. E. Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease. Biol. Chem. Hoppe-Seyler, 376: 345-355, 1995.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 345-355
    • Ries, C.1    Petrides, P.E.2
  • 3
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. Activation mechanisms of matrix metalloproteinases. Biol. Chem., 378: 151-160, 1997.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 5
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation
    • Liotta, L. A., Steeg, P. S., and Stetler-Stevenson, W. G. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell, 64: 327-336, 1991.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 6
    • 0027140406 scopus 로고
    • Extracellular matrix 6: Role of matrix metalloproteinases in tumor invasion and metastasis
    • Stetler-Stevenson, W. G., Liotta, L. A., and Kleiner, D. E. J. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J., 7: 1434-1441, 1993.
    • (1993) FASEB J. , vol.7 , pp. 1434-1441
    • Stetler-Stevenson, W.G.1    Liotta, L.A.2    Kleiner, D.E.J.3
  • 7
    • 0025262040 scopus 로고
    • Immunohistochemical distribution of type IV collagenase in normal, benign, and malignant breast tissue
    • Monteagudo, C., Merino, M. J., San Juan, J., Liotta, L. A., and Stetler Stevenson, W. G. Immunohistochemical distribution of type IV collagenase in normal, benign, and malignant breast tissue. Am. J. Pathol., 136: 585-592, 1990.
    • (1990) Am. J. Pathol. , vol.136 , pp. 585-592
    • Monteagudo, C.1    Merino, M.J.2    San Juan, J.3    Liotta, L.A.4    Stetler Stevenson, W.G.5
  • 9
    • 0023696675 scopus 로고
    • Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B 16-F10 melanoma cells
    • Schultz, R. M., Silberman, S., Persky, B., Bajkowski, A. S., and Carmichael, D. F. Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B 16-F10 melanoma cells. Cancer Res., 48: 5539-5545, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3    Bajkowski, A.S.4    Carmichael, D.F.5
  • 10
    • 0027285775 scopus 로고
    • In vitro invasive potential and type IV collagenolytic activity of human renal cell carcinoma cells derived from primary and metastatic lesions
    • Otani, N., Tsukamoto, T., Saiki, I., Yoneda, J., Mitaka, T., and Kumamoto, Y. In vitro invasive potential and type IV collagenolytic activity of human renal cell carcinoma cells derived from primary and metastatic lesions. J. Urol., 149: 1182-1185, 1993.
    • (1993) J. Urol. , vol.149 , pp. 1182-1185
    • Otani, N.1    Tsukamoto, T.2    Saiki, I.3    Yoneda, J.4    Mitaka, T.5    Kumamoto, Y.6
  • 11
    • 0026515761 scopus 로고
    • Expression of genes encoding type IV collagen-degrading metalloproteinases and tissue inhibitors of metalloproteinases in various human tumor cells
    • Sato, H., Kida, Y., Mai, M., Endo, Y., Sasaki, T., Tanaka, J., and Seiki, M. Expression of genes encoding type IV collagen-degrading metalloproteinases and tissue inhibitors of metalloproteinases in various human tumor cells. Oncogene, 7: 77-83, 1992.
    • (1992) Oncogene , vol.7 , pp. 77-83
    • Sato, H.1    Kida, Y.2    Mai, M.3    Endo, Y.4    Sasaki, T.5    Tanaka, J.6    Seiki, M.7
  • 14
    • 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., and Muschel, R. J. 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.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4293-4297
    • Bernhard, E.J.1    Gruber, S.B.2    Muschel, R.J.3
  • 16
    • 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., and Opdenakker, G. Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8. Eur. J. Biochem., 198: 391-398, 1991.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 391-398
    • Masure, S.1    Proost, P.2    Van Damme, J.A.3    Opdenakker, G.4
  • 17
    • 0029041446 scopus 로고
    • T cell gelatinases mediate basement membrane transmigration in vitro
    • Leppert, D., Waubant, E., Galardy, R., Bunnett, N. W., and Hauser, S. L. T cell gelatinases mediate basement membrane transmigration in vitro. J. Immunol., 154: 4379-4389, 1995.
    • (1995) J. Immunol. , vol.154 , pp. 4379-4389
    • Leppert, D.1    Waubant, E.2    Galardy, R.3    Bunnett, N.W.4    Hauser, S.L.5
  • 18
    • 0026033779 scopus 로고
    • Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and tissue inhibitor of metalloproteinases
    • Campbell, E. J., Cury, J. D., Shapiro, S. D., Goldberg, G. I., and Welgus, H. G. Neutral proteinases of human mononuclear phagocytes. Cellular differentiation markedly alters cell phenotype for serine proteinases, metalloproteinases, and tissue inhibitor of metalloproteinases. J. Immunol., 146: 1286-1293, 1991.
    • (1991) J. Immunol. , vol.146 , pp. 1286-1293
    • Campbell, E.J.1    Cury, J.D.2    Shapiro, S.D.3    Goldberg, G.I.4    Welgus, H.G.5
  • 19
    • 0025059594 scopus 로고
    • Neutral metalloproteinases produced by human mononuclear phagocytes. Enzyme profile, regulation, and expression during cellular development
    • Welgus, H. G., Campbell, E. J., Cury, J. D., Eisen, A. Z., Senior, R. M., Wilhelm, S. M., and Goldberg, G. I. Neutral metalloproteinases produced by human mononuclear phagocytes. Enzyme profile, regulation, and expression during cellular development. J. Clin. Invest., 86: 1496-1502, 1990.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1496-1502
    • Welgus, H.G.1    Campbell, E.J.2    Cury, J.D.3    Eisen, A.Z.4    Senior, R.M.5    Wilhelm, S.M.6    Goldberg, G.I.7
  • 20
    • 0030028043 scopus 로고    scopus 로고
    • Matrix metalloproteinases in immunity
    • Goetzl, E. J., Banda, M. J., and Leppert, D. Matrix metalloproteinases in immunity. J. Immunol., 156: 1-4, 1996.
    • (1996) J. Immunol. , vol.156 , pp. 1-4
    • Goetzl, E.J.1    Banda, M.J.2    Leppert, D.3
  • 22
    • 0026970047 scopus 로고
    • Relationship between the clinical aggressiveness of large cell immunoblastic lymphomas and expression of 92 kDa gelatinase (type IV collagenase) and tissue inhibitor of metalloproteinases-1 (TIMP-1) RNAs
    • Kossakowska, A. E., Urbanski, S. J., Huchcroft, S. A., and Edwards, D. R. Relationship between the clinical aggressiveness of large cell immunoblastic lymphomas and expression of 92 kDa gelatinase (type IV collagenase) and tissue inhibitor of metalloproteinases-1 (TIMP-1) RNAs. Oncol. Res., 4: 233-240, 1992.
    • (1992) Oncol. Res. , vol.4 , pp. 233-240
    • Kossakowska, A.E.1    Urbanski, S.J.2    Huchcroft, S.A.3    Edwards, D.R.4
  • 23
    • 0027300274 scopus 로고
    • Patterns of expression of metalloproteinases and their inhibitors in human malignant lymphomas
    • Kossakowska, A. E., Urbanski, S. J., Watson, A., Hayden, L. J., and Edwards, D. R. Patterns of expression of metalloproteinases and their inhibitors in human malignant lymphomas. Oncol. Res., 5: 19-28, 1993.
    • (1993) Oncol. Res. , vol.5 , pp. 19-28
    • Kossakowska, A.E.1    Urbanski, S.J.2    Watson, A.3    Hayden, L.J.4    Edwards, D.R.5
  • 24
    • 1842331535 scopus 로고    scopus 로고
    • Altered tumor growth and metastasis of a T-cell lymphoma in TIMP-1 transgenic mice
    • Krüger, A., Fata, J. E., and Khokha, R. Altered tumor growth and metastasis of a T-cell lymphoma in TIMP-1 transgenic mice. Blood, 90: 1993-2000, 1997.
    • (1997) Blood , vol.90 , pp. 1993-2000
    • Krüger, A.1    Fata, J.E.2    Khokha, R.3
  • 25
    • 0030405381 scopus 로고    scopus 로고
    • The role of metalloproteinases and their inhibitors in hematological disorders
    • Guedez, L., Lim, M. S., and Stetler-Stevenson, W. G. The role of metalloproteinases and their inhibitors in hematological disorders. Crit. Rev. Oncogenesis, 7: 205-225, 1996.
    • (1996) Crit. Rev. Oncogenesis , vol.7 , pp. 205-225
    • Guedez, L.1    Lim, M.S.2    Stetler-Stevenson, W.G.3
  • 26
    • 0025142646 scopus 로고
    • How do normal and leukemic white blood cells egress from the bone marrow? Morphological facts and biochemical riddles
    • Petrides, P. E., and Dittmann, K. H. How do normal and leukemic white blood cells egress from the bone marrow? Morphological facts and biochemical riddles. Ann. Hematol., 61: 3-13, 1990.
    • (1990) Ann. Hematol. , vol.61 , pp. 3-13
    • Petrides, P.E.1    Dittmann, K.H.2
  • 27
    • 0028338449 scopus 로고
    • Regulation of 92-kD gelatinase release in HL-60 leukemia cells: Tumor necrosis factor-α as an autocrine stimulus for basal-and phorbol ester-induced secretion
    • Ries, C., Kolb, H., and Petrides, P. E. Regulation of 92-kD gelatinase release in HL-60 leukemia cells: tumor necrosis factor-α as an autocrine stimulus for basal-and phorbol ester-induced secretion. Blood, 83: 3638-3646, 1994.
    • (1994) Blood , vol.83 , pp. 3638-3646
    • Ries, C.1    Kolb, H.2    Petrides, P.E.3
  • 28
    • 0029761280 scopus 로고    scopus 로고
    • HL-60 leukemia cells produce an autocatalytically truncated form of matrix metalloproteinase-9 with impaired sensitivity to inhibition by tissue inhibitors of metalloproteinases
    • Ries, C., Lottspeich, F., Dittmann, K. H., and Petrides, P. E. HL-60 leukemia cells produce an autocatalytically truncated form of matrix metalloproteinase-9 with impaired sensitivity to inhibition by tissue inhibitors of metalloproteinases. Leukemia (Baltimore), 10: 1520-1526, 1996.
    • (1996) Leukemia (Baltimore) , vol.10 , pp. 1520-1526
    • Ries, C.1    Lottspeich, F.2    Dittmann, K.H.3    Petrides, P.E.4
  • 29
    • 0031851423 scopus 로고    scopus 로고
    • Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-α (TNF-α) in NB4 leukemic cells: Specific involvement of TNF receptor type I
    • Ismair, M. G., Ries, C., Lottspeich, F., Zang, C., Kolb, H., and Petrides, P. E. Autocrine regulation of matrix metalloproteinase-9 gene expression and secretion by tumor necrosis factor-α (TNF-α) in NB4 leukemic cells: specific involvement of TNF receptor type I. Leukemia (Baltimore), 12: 1136-1143, 1998.
    • (1998) Leukemia (Baltimore) , vol.12 , pp. 1136-1143
    • Ismair, M.G.1    Ries, C.2    Lottspeich, F.3    Zang, C.4    Kolb, H.5    Petrides, P.E.6
  • 30
    • 0031058431 scopus 로고    scopus 로고
    • Unstimulated human acute myelogenous leukemia blasts secrete matrix metalloproteinases
    • Matsuzaki, A., and Janowska-Wieczorek, A. Unstimulated human acute myelogenous leukemia blasts secrete matrix metalloproteinases. J. Cancer Res. Clin. Oncol., 123: 100-106, 1997.
    • (1997) J. Cancer Res. Clin. Oncol. , vol.123 , pp. 100-106
    • Matsuzaki, A.1    Janowska-Wieczorek, A.2
  • 32
    • 9044246674 scopus 로고    scopus 로고
    • Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro
    • Yamamoto, M., Mohanam, S., Sawaya, R., Fuller, G. N., Seiki, M., Sato, H., Gokaslan, Z. L., Liotta, L. A., Nicolson, G. L., and Rao, J. S. Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro. Cancer Res., 56: 384-392, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 384-392
    • Yamamoto, M.1    Mohanam, S.2    Sawaya, R.3    Fuller, G.N.4    Seiki, M.5    Sato, H.6    Gokaslan, Z.L.7    Liotta, L.A.8    Nicolson, G.L.9    Rao, J.S.10
  • 33
    • 0030744830 scopus 로고    scopus 로고
    • Metalloproteinases in multiple myeloma: Production of matrix metalloproteinase-9 (MMP-9), activation of proMMP-2, and induction of MMP-1 by myeloma cells
    • Barille, S., Akhoundi, C., Collette, M., Mellerin, M. P., Rapp, M. J., Harousseau, J. L., Bateille, R., and Amiot, M. Metalloproteinases in multiple myeloma: production of matrix metalloproteinase-9 (MMP-9), activation of proMMP-2, and induction of MMP-1 by myeloma cells. Blood, 90: 1649-1655, 1997.
    • (1997) Blood , vol.90 , pp. 1649-1655
    • Barille, S.1    Akhoundi, C.2    Collette, M.3    Mellerin, M.P.4    Rapp, M.J.5    Harousseau, J.L.6    Bateille, R.7    Amiot, M.8
  • 34
    • 0028921518 scopus 로고
    • Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation
    • Borregaard, N., Sehested, M., Nielsen, B. S., Sengelov, H., and Kjeldsen, L. Biosynthesis of granule proteins in normal human bone marrow cells. Gelatinase is a marker of terminal neutrophil differentiation. Blood, 85: 812-817, 1995.
    • (1995) Blood , vol.85 , pp. 812-817
    • Borregaard, N.1    Sehested, M.2    Nielsen, B.S.3    Sengelov, H.4    Kjeldsen, L.5
  • 35
    • 0027219989 scopus 로고
    • Distinct mechanisms regulate interstitial collagenase and 92-kDa gelatinase expression in human monocytic-like cells exposed to bacterial endotoxin
    • Saarialho Kere, U. K., Welgus, H. G., and Parks, W. C. Distinct mechanisms regulate interstitial collagenase and 92-kDa gelatinase expression in human monocytic-like cells exposed to bacterial endotoxin. J. Biol. Chem., 268: 17354-17361, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17354-17361
    • Saarialho Kere, U.K.1    Welgus, H.G.2    Parks, W.C.3
  • 36
    • 0026161901 scopus 로고
    • The cytokine-protease 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., and Opdenakker, G. The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers. Cytokine, 3: 231-239, 1991.
    • (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
    • 0002282923 scopus 로고
    • Neutrophil proteases: Their physiological and pathological roles
    • P. G. Hellewell and T. J. Williams (eds.), London: Academic Press
    • Doherty, N. S., and Janusz, M. J. Neutrophil proteases: their physiological and pathological roles. In: P. G. Hellewell and T. J. Williams (eds.), Immunopharmacology of Neutrophils, pp. 55-94. London: Academic Press, 1994.
    • (1994) Immunopharmacology of Neutrophils , pp. 55-94
    • Doherty, N.S.1    Janusz, M.J.2
  • 38
    • 0030094287 scopus 로고    scopus 로고
    • Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration across basement membrane
    • Delclaux, C., Delacourt, C., D'Ortho, M. P., Boyer, V., Lafuma, C., and Harf, A. Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration across basement membrane. Am. J. Respir. Cell Mol. Biol., 14: 288-295, 1996.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.14 , pp. 288-295
    • Delclaux, C.1    Delacourt, C.2    D'Ortho, M.P.3    Boyer, V.4    Lafuma, C.5    Harf, A.6
  • 39
    • 0030048296 scopus 로고    scopus 로고
    • Rapid mobilization of hematopoietic progenitor cells in rhesus monkeys by a single intravenous injection of interleukin-8
    • Laterveer, L., Lindley, I. J., Heemskerk, D. P., Camps, J. A., Pauwels, E. K., Willemze, R., and Fibbe, W. E. Rapid mobilization of hematopoietic progenitor cells in rhesus monkeys by a single intravenous injection of interleukin-8. Blood, 87: 781-788, 1996.
    • (1996) Blood , vol.87 , pp. 781-788
    • Laterveer, L.1    Lindley, I.J.2    Heemskerk, D.P.3    Camps, J.A.4    Pauwels, E.K.5    Willemze, R.6    Fibbe, W.E.7
  • 40
    • 0003213524 scopus 로고    scopus 로고
    • Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by antibodies to the metalloproteinase gelatinase-B
    • Pruijt, J. F. M., Fibbe, W. E., Laterveer, L., Willemze, R., Masure, S., Paemen, L., and Opdenakker, G. Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by antibodies to the metalloproteinase gelatinase-B. Blood, 88: 455a, 1996.
    • (1996) Blood , vol.88
    • Pruijt, J.F.M.1    Fibbe, W.E.2    Laterveer, L.3    Willemze, R.4    Masure, S.5    Paemen, L.6    Opdenakker, G.7
  • 43
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. Activation mechanisms of matrix metalloproteinases. Biol. Chem., 378: 151-160, 1997.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 44
    • 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., and Goldberg, G. I. 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: 17213-17221, 1989.
    • (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
  • 46
  • 47
    • 0026568011 scopus 로고
    • Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum
    • Hayakawa, T., Yamashita, K., Tanzawa, K., Uchijima, E., and Iwata, K. Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum. FEBS Lett., 298: 29-32, 1992.
    • (1992) FEBS Lett. , vol.298 , pp. 29-32
    • Hayakawa, T.1    Yamashita, K.2    Tanzawa, K.3    Uchijima, E.4    Iwata, K.5
  • 48
    • 0028944106 scopus 로고
    • Molecular insights into cancer invasion: Strategies for prevention and intervention
    • Kohn, E. C., and Liotta, L. A. Molecular insights into cancer invasion: strategies for prevention and intervention. Cancer Res., 55: 1856-1862, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 1856-1862
    • Kohn, E.C.1    Liotta, L.A.2
  • 49
    • 0029586589 scopus 로고
    • Matrix metalloproteinase inhibition: A review of anti-tumour activity
    • Brown, P. D., and Giavazzi, R. Matrix metalloproteinase inhibition: a review of anti-tumour activity. Ann. Oncol., 6: 967-974, 1995.
    • (1995) Ann. Oncol. , vol.6 , pp. 967-974
    • Brown, P.D.1    Giavazzi, R.2


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