메뉴 건너뛰기




Volumn 51, Issue 6, 2003, Pages 821-829

In situ localization of gelatinolytic activity in the extracellular matrix of metastases of colon cancer in rat liver using quenched fluorogenic DQ-gelatin

Author keywords

DQ gelatin; Extracellular matrix; Gelatinase activity; In situ zymograpy; Matrix metalloproteinase; Metastasis

Indexed keywords

DQ GELATIN; GELATIN; GELATINASE; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 0037675000     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/002215540305100613     Document Type: Article
Times cited : (91)

References (42)
  • 1
    • 0033831933 scopus 로고    scopus 로고
    • Matrix metalloproteinases, their tissue inhibitors and colorectal cancer staging
    • Baker EA, Bergin FG, Leaper DJ (2000) Matrix metalloproteinases, their tissue inhibitors and colorectal cancer staging. Br J Surg 87:1215-1221
    • (2000) Br J Surg , vol.87 , pp. 1215-1221
    • Baker, E.A.1    Bergin, F.G.2    Leaper, D.J.3
  • 2
    • 0035920182 scopus 로고    scopus 로고
    • Gelatin-binding region of human matrix metalloproteinase-2: Solution structure, dynamics, and function of the COL-23 two-domain construct
    • Briknarova K, Gehrmann M, Banyai L, Tordai H, Patthy L, Llinas M (2001) Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct. J Biol Chem 276:27613-27621
    • (2001) J Biol Chem , vol.276 , pp. 27613-27621
    • Briknarova, K.1    Gehrmann, M.2    Banyai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 3
    • 0026656315 scopus 로고
    • Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kDa type IV collagenase
    • Collier IE, Krasnov PA, Strongin AY, Birkedal-Hansen H, Goldberg GI (1992) Alanine scanning mutagenesis and functional analysis of the fibronectin-like collagen-binding domain from human 92-kDa type IV collagenase. J Biol Chem 267:6776-6781
    • (1992) J Biol Chem , vol.267 , pp. 6776-6781
    • Collier, I.E.1    Krasnov, P.A.2    Strongin, A.Y.3    Birkedal-Hansen, H.4    Goldberg, G.I.5
  • 4
    • 0023919959 scopus 로고
    • H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
    • Collier IE, Wilhelm SM, Eisen AZ, Marmer BL, Grant GA, Seltzer JL, Kronberger A, et al. (1988) H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. J Biol Chem 263:6579-6587
    • (1988) J Biol Chem , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3    Marmer, B.L.4    Grant, G.A.5    Seltzer, J.L.6    Kronberger, A.7
  • 5
    • 0028675819 scopus 로고
    • Tumor and stromal expression of matrix metalloproteinases and their role in tumor progression
    • Crawford HC, Matrisian LM (1994) Tumor and stromal expression of matrix metalloproteinases and their role in tumor progression. Invas Metast 14:234-245
    • (1994) Invas Metast , vol.14 , pp. 234-245
    • Crawford, H.C.1    Matrisian, L.M.2
  • 6
    • 0031965487 scopus 로고    scopus 로고
    • Gelatinase A (MMP-2) and cysteine proteinases are essential for the degradation of collagen in soft connective tissue
    • Creemers LB, Jansen ID, Docherty AJ, Reynolds JJ, Beertsen W, Everts V (1998) Gelatinase A (MMP-2) and cysteine proteinases are essential for the degradation of collagen in soft connective tissue. Matrix Biol 17:35-46
    • (1998) Matrix Biol , vol.17 , pp. 35-46
    • Creemers, L.B.1    Jansen, I.D.2    Docherty, A.J.3    Reynolds, J.J.4    Beertsen, W.5    Everts, V.6
  • 8
    • 0032763013 scopus 로고    scopus 로고
    • Combined treatment with serine protease inhibitor aprotinin and matrix metalloproteinase inhibitor batimastat (BB-94) does not prevent invasion of human esophageal and ovarian carcinoma cells in vivo
    • Della Porta P, Soeltl R, Krell HW, Collins K, O'Donoghue M, Schmitt M, Kruger A (1999) Combined treatment with serine protease inhibitor aprotinin and matrix metalloproteinase inhibitor batimastat (BB-94) does not prevent invasion of human esophageal and ovarian carcinoma cells in vivo. Anticancer Res 19:3809-3816
    • (1999) Anticancer Res , vol.19 , pp. 3809-3816
    • Della Porta, P.1    Soeltl, R.2    Krell, H.W.3    Collins, K.4    O'Donoghue, M.5    Schmitt, M.6    Kruger, A.7
  • 10
    • 0029129597 scopus 로고
    • Microscopic localization of active proteases by in situ zymography: Detection of matrix metalloproteinase activity in vascular tissue
    • Galis ZS, Sukhova GK, Libby P (1995) Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue. FASEB J 9:974-980
    • (1995) FASEB J , vol.9 , pp. 974-980
    • Galis, Z.S.1    Sukhova, G.K.2    Libby, P.3
  • 12
  • 13
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C, Dowdle EB (1980) Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal Biochem 102:196-202
    • (1980) Anal Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 15
    • 0034108172 scopus 로고    scopus 로고
    • Inactive matrix metalloproteinase 2 is a normal constituent of human glomerular basement membrane. An immuno-electron microscopic study
    • Jalalah SM, Furness PN, Barker G, Thomas M, Hall LL, Bicknell GR, Shaw JA, et al. (2000) Inactive matrix metalloproteinase 2 is a normal constituent of human glomerular basement membrane. An immuno-electron microscopic study. J Pathol 191:61-66
    • (2000) J Pathol , vol.191 , pp. 61-66
    • Jalalah, S.M.1    Furness, P.N.2    Barker, G.3    Thomas, M.4    Hall, L.L.5    Bicknell, G.R.6    Shaw, J.A.7
  • 16
    • 0027250427 scopus 로고
    • Experimentally induced colon cancer metastases in rat liver increase the proliferation rate and capacity for purine catabolism in liver cells
    • Jonges GN, Vogels IM, Bosch KS, Dingemans KP, Van Noorden CJ (1993) Experimentally induced colon cancer metastases in rat liver increase the proliferation rate and capacity for purine catabolism in liver cells. Histochemistry 100:41-51
    • (1993) Histochemistry , vol.100 , pp. 41-51
    • Jonges, G.N.1    Vogels, I.M.2    Bosch, K.S.3    Dingemans, K.P.4    Van Noorden, C.J.5
  • 17
    • 0033921956 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors during hepatic tissue repair in the rat
    • Knittel T, Mehde M, Grundmann A, Saile B, Scharf JG, Ramadori G (2000) Expression of matrix metalloproteinases and their inhibitors during hepatic tissue repair in the rat. Histochem Cell Biol 113:443-453
    • (2000) Histochem Cell Biol , vol.113 , pp. 443-453
    • Knittel, T.1    Mehde, M.2    Grundmann, A.3    Saile, B.4    Scharf, J.G.5    Ramadori, G.6
  • 18
    • 0033815354 scopus 로고    scopus 로고
    • Gelatinolytic activity of matrix metalloproteinase-2 and -9 in oesophageal carcinoma: A study using in situ zymography
    • Koyama H, Iwata H, Kuwabara Y, Iwase H, Kobayashi S, Fujii Y (2000) Gelatinolytic activity of matrix metalloproteinase-2 and -9 in oesophageal carcinoma: a study using in situ zymography. Eur J Cancer 36:2164-2170
    • (2000) Eur J Cancer , vol.36 , pp. 2164-2170
    • Koyama, H.1    Iwata, H.2    Kuwabara, Y.3    Iwase, H.4    Kobayashi, S.5    Fujii, Y.6
  • 19
    • 0035866362 scopus 로고    scopus 로고
    • Hydroxamate-type matrix metalloproteinase inhibitor batimastat promotes liver metastasis
    • Kruger A, Soeltl R, Sopov I, Kopitz C, Arlt M, Magdolen V, Harbeck N, et al. (2001) Hydroxamate-type matrix metalloproteinase inhibitor batimastat promotes liver metastasis. Cancer Res 61:1272-1275
    • (2001) Cancer Res , vol.61 , pp. 1272-1275
    • Kruger, A.1    Soeltl, R.2    Sopov, I.3    Kopitz, C.4    Arlt, M.5    Magdolen, V.6    Harbeck, N.7
  • 20
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor I
    • Levi E, Fridman R, Miao H-Q, Ma Y-C, Yayon A, Vlodavsky I (1996) Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor I. Proc Natl Acad Sci USA 93:7069-7074
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7069-7074
    • Levi, E.1    Fridman, R.2    Miao, H.-Q.3    Ma, Y.-C.4    Yayon, A.5    Vlodavsky, I.6
  • 21
    • 0030044480 scopus 로고    scopus 로고
    • Matrix metalloprotease 2 (MMP-2) and matrix metalloprotease 9 (MMP-9) type IV collagenases in colorectal cancer
    • Liabakk NB, Talbot I, Smith RA, Wilkinson K, Balkwill F (1996) Matrix metalloprotease 2 (MMP-2) and matrix metalloprotease 9 (MMP-9) type IV collagenases in colorectal cancer. Cancer Res 56:190-196
    • (1996) Cancer Res , vol.56 , pp. 190-196
    • Liabakk, N.B.1    Talbot, I.2    Smith, R.A.3    Wilkinson, K.4    Balkwill, F.5
  • 22
    • 0032170034 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinase inhibitors and tissue inhibitor of metalloproteinase (TIMP)-2, but not TIMP-1, inhibit shedding of tumor necrosis factor-α receptors in a human colon adenocarcinoma (Colo 205) cell line
    • Lombard MA, Wallace TL, Kubicek MF, Petzold GL, Mitchell MA, Hendges SK, Wilks JW (1998) Synthetic matrix metalloproteinase inhibitors and tissue inhibitor of metalloproteinase (TIMP)-2, but not TIMP-1, inhibit shedding of tumor necrosis factor-α receptors in a human colon adenocarcinoma (Colo 205) cell line. Cancer Res 58:4001-4007
    • (1998) Cancer Res , vol.58 , pp. 4001-4007
    • Lombard, M.A.1    Wallace, T.L.2    Kubicek, M.F.3    Petzold, G.L.4    Mitchell, M.A.5    Hendges, S.K.6    Wilks, J.W.7
  • 23
    • 0021359081 scopus 로고
    • Interferon treatment of a transplantable rat colon adenocarcinoma: Importance of tumor site
    • Marquet RL, Westbroek DL, Jeekel J (1984) Interferon treatment of a transplantable rat colon adenocarcinoma: importance of tumor site. Int J Cancer 33:689-692
    • (1984) Int J Cancer , vol.33 , pp. 689-692
    • Marquet, R.L.1    Westbroek, D.L.2    Jeekel, J.3
  • 24
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 12:1075-1095
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 25
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • McCawley LJ, Matrisian LM (2000) Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol Med Today 6:149-156
    • (2000) Mol Med Today , vol.6 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 26
    • 0032512914 scopus 로고    scopus 로고
    • Mechanisms of tumour metastasis
    • Meyer T, Hart IR (1998) Mechanisms of tumour metastasis. Eur J Cancer 34:214-221
    • (1998) Eur J Cancer , vol.34 , pp. 214-221
    • Meyer, T.1    Hart, I.R.2
  • 28
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr. (1999) Matrix metalloproteinases. J Biol Chem 274:21491-21494
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner J.F., Jr.2
  • 30
    • 0032952694 scopus 로고    scopus 로고
    • Inhibition of gelatinase A (MMP-2) by batimastat and captopril reduces tumor growth and lung metastases in mice bearing Lewis lung carcinoma
    • Prontera C, Mariani B, Rossi C, Poggi A, Rotilio D (1999) Inhibition of gelatinase A (MMP-2) by batimastat and captopril reduces tumor growth and lung metastases in mice bearing Lewis lung carcinoma. Int J Cancer 81:761-766
    • (1999) Int J Cancer , vol.81 , pp. 761-766
    • Prontera, C.1    Mariani, B.2    Rossi, C.3    Poggi, A.4    Rotilio, D.5
  • 31
    • 0030839472 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition as a novel anticancer strategy: A review with special focus on batimastat and marimastat
    • Rasmussen HS, McCann PP (1997) Matrix metalloproteinase inhibition as a novel anticancer strategy: a review with special focus on batimastat and marimastat. Pharmacol Ther 75:69-75
    • (1997) Pharmacol Ther , vol.75 , pp. 69-75
    • Rasmussen, H.S.1    McCann, P.P.2
  • 33
    • 0028073883 scopus 로고
    • The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis
    • Ray JM, Stetler-Stevenson WG (1994) The role of matrix metalloproteases and their inhibitors in tumour invasion, metastasis and angiogenesis. Eur Respir J 7:2062-2072
    • (1994) Eur Respir J , vol.7 , pp. 2062-2072
    • Ray, J.M.1    Stetler-Stevenson, W.G.2
  • 34
    • 0032194115 scopus 로고    scopus 로고
    • Generation of biologically active IL-1 beta by matrix metalloproteinases: A novel caspase-1-independent pathway of IL-1 beta processing
    • Schonbeck U, Mach F, Libby P (1998) Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing. J Immunol 161:3340-3346
    • (1998) J Immunol , vol.161 , pp. 3340-3346
    • Schonbeck, U.1    Mach, F.2    Libby, P.3
  • 35
    • 0029010660 scopus 로고
    • Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen
    • Steffensen B, Wallon UM, Overall CM (1995) Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J Biol Chem 270:11555-11566
    • (1995) J Biol Chem , vol.270 , pp. 11555-11566
    • Steffensen, B.1    Wallon, U.M.2    Overall, C.M.3
  • 36
    • 0033636735 scopus 로고    scopus 로고
    • The role of up-regulated serine proteases and matrix metalloproteinases in the pathogenesis of a murine model of colitis
    • Tarlton JF, Whiting CV, Tunmore D, Bregenholt S, Reimann J, Claesson MH, Bland PW (2000) The role of up-regulated serine proteases and matrix metalloproteinases in the pathogenesis of a murine model of colitis. Am J Pathol 157:1927-1935
    • (2000) Am J Pathol , vol.157 , pp. 1927-1935
    • Tarlton, J.F.1    Whiting, C.V.2    Tunmore, D.3    Bregenholt, S.4    Reimann, J.5    Claesson, M.H.6    Bland, P.W.7
  • 37
    • 0031800093 scopus 로고    scopus 로고
    • Heterogeneous suppression of experimentally induced colon cancer metastasis in rat liver lobes by inhibition of extracellular cathepsin B
    • Van Noorden CJ, Jonges TG, Van Marle J, Bissell ER, Griffini P, Jans M, Snel J, et al. (1998) Heterogeneous suppression of experimentally induced colon cancer metastasis in rat liver lobes by inhibition of extracellular cathepsin B. Clin Exp Metast 16:159-167
    • (1998) Clin Exp Metast , vol.16 , pp. 159-167
    • Van Noorden, C.J.1    Jonges, T.G.2    Van Marle, J.3    Bissell, E.R.4    Griffini, P.5    Jans, M.6    Snel, J.7
  • 38
    • 0037125032 scopus 로고    scopus 로고
    • Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer
    • Waas ET, Lomme RMLM, DeGroot J, Wobbes Th, Hendriks T (2002) Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer. Br J Cancer 86:1876-1883
    • (2002) Br J Cancer , vol.86 , pp. 1876-1883
    • Waas, E.T.1    Lomme, R.M.L.M.2    DeGroot, J.3    Wobbes, Th.4    Hendriks, T.5
  • 39
    • 0032801504 scopus 로고    scopus 로고
    • Histochemical and ultrastructural characterization of vacuoles and spherosomes as components of the lytic system in hyphae of the fungus Botrytis cinerea
    • Weber RW, Wakley GE, Pitt D (1999) Histochemical and ultrastructural characterization of vacuoles and spherosomes as components of the lytic system in hyphae of the fungus Botrytis cinerea. Histochem J 31:293-301
    • (1999) Histochem J , vol.31 , pp. 293-301
    • Weber, R.W.1    Wakley, G.E.2    Pitt, D.3
  • 40
    • 0029001584 scopus 로고
    • Quantification of matrix metalloproteinases in tissue samples
    • Woessner JF Jr (1995) Quantification of matrix metalloproteinases in tissue samples. Methods Enzymol 248:510-528
    • (1995) Methods Enzymol , vol.248 , pp. 510-528
    • Woessner J.F., Jr.1
  • 42
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metallo-proteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I (2000) Cell surface-localized matrix metallo-proteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 14:163-176
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.