메뉴 건너뛰기




Volumn 349, Issue 1, 2006, Pages 426-431

Apparent suppression of MMP-9 activity by GD1a as determined by gelatin zymography

Author keywords

Ganglioside; GD1a; Metastasis; MMP 2; MMP 9; Zymography

Indexed keywords

GANGLIOSIDE GD 1A; GELATINASE B; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B;

EID: 33748291573     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.08.062     Document Type: Article
Times cited : (7)

References (18)
  • 1
    • 0033624445 scopus 로고    scopus 로고
    • Matrix metalloproteinases: molecular aspects of their roles in tumour invasion and metastasis
    • Curran S., and Murray G.I. Matrix metalloproteinases: molecular aspects of their roles in tumour invasion and metastasis. Eur. J. Cancer 36 (2000) 1621-1630
    • (2000) Eur. J. Cancer , vol.36 , pp. 1621-1630
    • Curran, S.1    Murray, G.I.2
  • 3
    • 24044459285 scopus 로고    scopus 로고
    • Matrix metalloproteinases and angiogenesis
    • Rundhaug J.E. Matrix metalloproteinases and angiogenesis. J. Cell. Mol. Med. 9 (2005) 267-285
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 267-285
    • Rundhaug, J.E.1
  • 4
    • 0026425631 scopus 로고
    • Tumor invasion and metastasis: an importance of positive and negative regulation
    • Liotta L.A., and Stetler-Stevenson W.G. Tumor invasion and metastasis: an importance of positive and negative regulation. Cancer Res. 51 (1991) 5054-5059
    • (1991) Cancer Res. , vol.51 , pp. 5054-5059
    • Liotta, L.A.1    Stetler-Stevenson, W.G.2
  • 5
    • 33748287865 scopus 로고    scopus 로고
    • D. Hu, Z. Man, T. Xuan, P. Wang, T. Takaku, S. Hyuga, X.S. Yao, T. Sato, S. Yamagata, T. Yamagata, Ganglioside GD1a regulation of matrix metalloproteinase-9 (MMP-9) expression in mouse FBJ cell Lines: GD1a suppression of MMP-9 expression stimulated by PI3K-Akt and p38 though not by the Erk signaling pathway, 2006, Submitted for publication.
  • 8
    • 0025741831 scopus 로고
    • Occurrence of an active form of gelatinase in human gastric and colorectal carcinoma tissues
    • Yamagata S., Yoshii Y., Suh J.G., Tanaka R., and Shimizu S. Occurrence of an active form of gelatinase in human gastric and colorectal carcinoma tissues. Cancer Lett. 59 (1991) 51-55
    • (1991) Cancer Lett. , vol.59 , pp. 51-55
    • Yamagata, S.1    Yoshii, Y.2    Suh, J.G.3    Tanaka, R.4    Shimizu, S.5
  • 9
    • 0028827415 scopus 로고
    • Characterization of extracellular matrix-degrading proteinase and its inhibitor in gynecologic cancer tissues with clinically different metastatic form
    • Tamakoshi K., Kikkawa F., Nawa A., Ishikawa H., Mizuno K., Tamakoshi A., Yamagata S., Suganuma N., and Tomoda Y. Characterization of extracellular matrix-degrading proteinase and its inhibitor in gynecologic cancer tissues with clinically different metastatic form. Cancer 76 (1995) 2565-2571
    • (1995) Cancer , vol.76 , pp. 2565-2571
    • Tamakoshi, K.1    Kikkawa, F.2    Nawa, A.3    Ishikawa, H.4    Mizuno, K.5    Tamakoshi, A.6    Yamagata, S.7    Suganuma, N.8    Tomoda, Y.9
  • 10
    • 0028903083 scopus 로고
    • Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src
    • Hamaguchi M., Yamagata S., Thant A.A., Xiao H., Iwata H., Mazaki T., and Hanafusa H. Augmentation of metalloproteinase (gelatinase) activity secreted from Rous sarcoma virus-infected cells correlates with transforming activity of src. Oncogene 10 (1995) 1037-1043
    • (1995) Oncogene , vol.10 , pp. 1037-1043
    • Hamaguchi, M.1    Yamagata, S.2    Thant, A.A.3    Xiao, H.4    Iwata, H.5    Mazaki, T.6    Hanafusa, H.7
  • 11
    • 0028934954 scopus 로고
    • Analysis of glycosaminoglycan-degrading enzymes by substrate gel electrophoresis (zymography)
    • Miura R.O., Yamagata S., Miura Y., Harada T., and Yamagata T. Analysis of glycosaminoglycan-degrading enzymes by substrate gel electrophoresis (zymography). Anal. Biochem. 225 (1995) 333-340
    • (1995) Anal. Biochem. , vol.225 , pp. 333-340
    • Miura, R.O.1    Yamagata, S.2    Miura, Y.3    Harada, T.4    Yamagata, T.5
  • 12
    • 4243180411 scopus 로고    scopus 로고
    • Plasminogen activator and serine protease inhibitor-E2 (protease nexin-1) expression by bovine granulosa cells in vitro
    • Cao M., Sahmi M., Lussier J.G., and Price C.A. Plasminogen activator and serine protease inhibitor-E2 (protease nexin-1) expression by bovine granulosa cells in vitro. Biol. Reprod. 71 (2004) 887-893
    • (2004) Biol. Reprod. , vol.71 , pp. 887-893
    • Cao, M.1    Sahmi, M.2    Lussier, J.G.3    Price, C.A.4
  • 13
    • 0036467706 scopus 로고    scopus 로고
    • Real-time zymography and reverse zymography: a method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates
    • Hattori S., Fujisaki H., Kiriyama T., Yokoyama T., and Irie S. Real-time zymography and reverse zymography: a method for detecting activities of matrix metalloproteinases and their inhibitors using FITC-labeled collagen and casein as substrates. Anal. Biochem. 301 (2002) 27-34
    • (2002) Anal. Biochem. , vol.301 , pp. 27-34
    • Hattori, S.1    Fujisaki, H.2    Kiriyama, T.3    Yokoyama, T.4    Irie, S.5
  • 14
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen L., Johnsen A.H., Sengeløv H., and Borregaard N. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J. Biol. Chem. 268 (1993) 10425-10432
    • (1993) J. Biol. Chem. , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengeløv, H.3    Borregaard, N.4
  • 15
    • 0037364403 scopus 로고    scopus 로고
    • Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: correlation to polymorphonuclear leukocyte infiltration and in response to infection
    • Makowskia G.S., and Ramsby M.L. Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: correlation to polymorphonuclear leukocyte infiltration and in response to infection. Clin. Chim. Acta 329 (2003) 77-81
    • (2003) Clin. Chim. Acta , vol.329 , pp. 77-81
    • Makowskia, G.S.1    Ramsby, M.L.2
  • 16
    • 6344221921 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors in the developing neonatal mouse uterus
    • Hu J., Zhang X., Nothnick W.B., and Spencer T.E. Matrix metalloproteinases and their tissue inhibitors in the developing neonatal mouse uterus. Biol. Reprod. 71 (2004) 1598-1604
    • (2004) Biol. Reprod. , vol.71 , pp. 1598-1604
    • Hu, J.1    Zhang, X.2    Nothnick, W.B.3    Spencer, T.E.4
  • 17
    • 0034472617 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion and metastasis
    • Stamenkovic I. Matrix metalloproteinases in tumor invasion and metastasis. Cancer Biol. 10 (2000) 415-433
    • (2000) Cancer Biol. , vol.10 , pp. 415-433
    • Stamenkovic, I.1
  • 18
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: evolution, structure and function
    • Brew K., Dinakarpandian D., and Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim. Biophys. Acta 1477 (2000) 267-283
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.