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Volumn 44, Issue 17-18, 2011, Pages 1434-1439

Potential of fluorescent metalloproteinase substrates for cancer detection

Author keywords

ADAMs; Breast cancer; Enzyme activity; FRET substrates; Invasive; Metastatic; MMPs; Urine

Indexed keywords

ADAM 12; ADAM 8; ADAM PROTEIN; FLSUB13 PROTEIN; FLSUB21 PROTEIN; GELATINASE A; GELATINASE B; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 81555219466     PISSN: 00099120     EISSN: 18732933     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2011.09.016     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 33344466450 scopus 로고    scopus 로고
    • Making the cut: protease-mediated regulation of angiogenesis
    • Roy R., Zhang B., Moses M.A. Making the cut: protease-mediated regulation of angiogenesis. Exp Cell Res 2006, 312:608-622.
    • (2006) Exp Cell Res , vol.312 , pp. 608-622
    • Roy, R.1    Zhang, B.2    Moses, M.A.3
  • 2
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A.F., Matrisian L.M. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 1997, 89:1260-1270.
    • (1997) J Natl Cancer Inst , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 4
    • 0032850365 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumour invasion and metastasis
    • Curran S., Murray G.I. Matrix metalloproteinases in tumour invasion and metastasis. J Pathol 1999, 189:300-308.
    • (1999) J Pathol , vol.189 , pp. 300-308
    • Curran, S.1    Murray, G.I.2
  • 5
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H., Woessner J.F. Matrix metalloproteinases. J Biol Chem 1999, 274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 7
    • 0033617532 scopus 로고    scopus 로고
    • Effects of angiogenesis inhibitors on multistage carcinogenesis in mice
    • Bergers G., Javaherian K., Lo K.M., Folkman J., Hanahan D. Effects of angiogenesis inhibitors on multistage carcinogenesis in mice. Science 1999, 284:808-812.
    • (1999) Science , vol.284 , pp. 808-812
    • Bergers, G.1    Javaherian, K.2    Lo, K.M.3    Folkman, J.4    Hanahan, D.5
  • 8
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002, 2:161-174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 9
    • 1542495411 scopus 로고    scopus 로고
    • Structural basis of matrix metalloproteinase function
    • Bode W. Structural basis of matrix metalloproteinase function. Biochem Soc Symp 2003, 1-14.
    • (2003) Biochem Soc Symp , pp. 1-14
    • Bode, W.1
  • 10
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: multidomain proteins with multiple functions
    • Seals D.F., Courtneidge S.A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003, 17:7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 12
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • Maretzky T., Schulte M., Ludwig A., Rose-John S., Blobel C., Hartmann D., Altevogt P., Saftig P., Reiss K. L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol Cell Biol 2005, 25:9040-9053.
    • (2005) Mol Cell Biol , vol.25 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.5    Hartmann, D.6    Altevogt, P.7    Saftig, P.8    Reiss, K.9
  • 13
    • 84863876087 scopus 로고    scopus 로고
    • Mammary gland reprogramming: metalloproteinases couple form with function
    • Khokha R., Werb Z. Mammary gland reprogramming: metalloproteinases couple form with function. Cold Spring Harb Perspect Biol 3 2010.
    • (2010) Cold Spring Harb Perspect Biol 3
    • Khokha, R.1    Werb, Z.2
  • 14
    • 33748484703 scopus 로고    scopus 로고
    • Understanding the role of tissue degrading enzymes and their inhibitors in development and disease
    • Cawston T.E., Wilson A.J. Understanding the role of tissue degrading enzymes and their inhibitors in development and disease. Best Pract Res Clin Rheumatol 2006, 20:983-1002.
    • (2006) Best Pract Res Clin Rheumatol , vol.20 , pp. 983-1002
    • Cawston, T.E.1    Wilson, A.J.2
  • 16
    • 73249114449 scopus 로고    scopus 로고
    • Extracellular and cell surface proteases in wound healing: new players are still emerging
    • Moali C., Hulmes D.J. Extracellular and cell surface proteases in wound healing: new players are still emerging. Eur J Dermatol 2009, 19:552-564.
    • (2009) Eur J Dermatol , vol.19 , pp. 552-564
    • Moali, C.1    Hulmes, D.J.2
  • 17
    • 77049128569 scopus 로고    scopus 로고
    • Unraveling metalloproteinase function in skeletal biology and disease using genetically altered mice
    • Aiken A., Khokha R. Unraveling metalloproteinase function in skeletal biology and disease using genetically altered mice. Biochim Biophys Acta 2010, 1803:121-132.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 121-132
    • Aiken, A.1    Khokha, R.2
  • 19
    • 42249085231 scopus 로고    scopus 로고
    • Urinary biomarkers predict brain tumor presence and response to therapy
    • Smith E.R., Zurakowski D., Saad A., Scott R.M., Moses M.A. Urinary biomarkers predict brain tumor presence and response to therapy. Clin Cancer Res 2008, 14:2378-2386.
    • (2008) Clin Cancer Res , vol.14 , pp. 2378-2386
    • Smith, E.R.1    Zurakowski, D.2    Saad, A.3    Scott, R.M.4    Moses, M.A.5
  • 20
    • 58049203639 scopus 로고    scopus 로고
    • Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species
    • Roy R., Louis G., Loughlin K.R., Wiederschain D., Kilroy S.M., Lamb C.C., Zurakowski D., Moses M.A. Tumor-specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clin Cancer Res 2008, 14:6610-6617.
    • (2008) Clin Cancer Res , vol.14 , pp. 6610-6617
    • Roy, R.1    Louis, G.2    Loughlin, K.R.3    Wiederschain, D.4    Kilroy, S.M.5    Lamb, C.C.6    Zurakowski, D.7    Moses, M.A.8
  • 21
    • 1442339457 scopus 로고    scopus 로고
    • Urinary VEGF and MMP levels as predictive markers of 1-year progression-free survival in cancer patients treated with radiation therapy: a longitudinal study of protein kinetics throughout tumor progression and therapy
    • Chan L.W., Moses M.A., Goley E., Sproull M., Muanza T., Coleman C.N., Figg W.D., Albert P.S., Menard C., Camphausen K. Urinary VEGF and MMP levels as predictive markers of 1-year progression-free survival in cancer patients treated with radiation therapy: a longitudinal study of protein kinetics throughout tumor progression and therapy. J Clin Oncol 2004, 22:499-506.
    • (2004) J Clin Oncol , vol.22 , pp. 499-506
    • Chan, L.W.1    Moses, M.A.2    Goley, E.3    Sproull, M.4    Muanza, T.5    Coleman, C.N.6    Figg, W.D.7    Albert, P.S.8    Menard, C.9    Camphausen, K.10
  • 22
    • 0037441381 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase 9 as biomarker of prostate cancer progression in Dunning (Copenhagen) rats
    • Jung K., Krell H.W., Ortel B., Hasan T., Romer A., Schnorr D., Loening S.A., Lein M. Plasma matrix metalloproteinase 9 as biomarker of prostate cancer progression in Dunning (Copenhagen) rats. Prostate 2003, 54:206-211.
    • (2003) Prostate , vol.54 , pp. 206-211
    • Jung, K.1    Krell, H.W.2    Ortel, B.3    Hasan, T.4    Romer, A.5    Schnorr, D.6    Loening, S.A.7    Lein, M.8
  • 24
    • 40749099079 scopus 로고    scopus 로고
    • Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer
    • Wu Z.S., Wu Q., Yang J.H., Wang H.Q., Ding X.D., Yang F., Xu X.C. Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer. Int J Cancer 2008, 122:2050-2056.
    • (2008) Int J Cancer , vol.122 , pp. 2050-2056
    • Wu, Z.S.1    Wu, Q.2    Yang, J.H.3    Wang, H.Q.4    Ding, X.D.5    Yang, F.6    Xu, X.C.7
  • 25
    • 45949091054 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) immunoreactive protein in urinary bladder cancer: a marker of favorable prognosis
    • Vasala K., Paakko P., Turpeenniemi-Hujanen T. Matrix metalloproteinase-9 (MMP-9) immunoreactive protein in urinary bladder cancer: a marker of favorable prognosis. Anticancer Res 2008, 28:1757-1761.
    • (2008) Anticancer Res , vol.28 , pp. 1757-1761
    • Vasala, K.1    Paakko, P.2    Turpeenniemi-Hujanen, T.3
  • 26
    • 23044499535 scopus 로고    scopus 로고
    • The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients
    • Fernandez C.A., Yan L., Louis G., Yang J., Kutok J.L., Moses M.A. The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients. Clin Cancer Res 2005, 11:5390-5395.
    • (2005) Clin Cancer Res , vol.11 , pp. 5390-5395
    • Fernandez, C.A.1    Yan, L.2    Louis, G.3    Yang, J.4    Kutok, J.L.5    Moses, M.A.6
  • 28
    • 0035813187 scopus 로고    scopus 로고
    • The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL
    • Yan L., Borregaard N., Kjeldsen L., Moses M.A. The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL. J Biol Chem 2001, 276:37258-37265.
    • (2001) J Biol Chem , vol.276 , pp. 37258-37265
    • Yan, L.1    Borregaard, N.2    Kjeldsen, L.3    Moses, M.A.4
  • 29
    • 34249829865 scopus 로고    scopus 로고
    • A recurrent craniopharyngioma illustrates the potential usefulness of urinary matrix metalloproteinases as noninvasive biomarkers: case report
    • discussion E1149
    • Smith E.R., Manfredi M., Scott R.M., Black P.M., Moses M.A. A recurrent craniopharyngioma illustrates the potential usefulness of urinary matrix metalloproteinases as noninvasive biomarkers: case report. Neurosurgery 2007, 60:E1148-E1149. discussion E1149.
    • (2007) Neurosurgery , vol.60
    • Smith, E.R.1    Manfredi, M.2    Scott, R.M.3    Black, P.M.4    Moses, M.A.5
  • 30
    • 2342487379 scopus 로고    scopus 로고
    • Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera
    • La Rocca G., Pucci-Minafra I., Marrazzo A., Taormina P., Minafra S. Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera. Br J Cancer 2004, 90:1414-1421.
    • (2004) Br J Cancer , vol.90 , pp. 1414-1421
    • La Rocca, G.1    Pucci-Minafra, I.2    Marrazzo, A.3    Taormina, P.4    Minafra, S.5
  • 31
    • 10944263573 scopus 로고    scopus 로고
    • ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage
    • Roy R., Wewer U.M., Zurakowski D., Pories S.E., Moses M.A. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. J Biol Chem 2004, 279:51323-51330.
    • (2004) J Biol Chem , vol.279 , pp. 51323-51330
    • Roy, R.1    Wewer, U.M.2    Zurakowski, D.3    Pories, S.E.4    Moses, M.A.5
  • 33
    • 0030721640 scopus 로고    scopus 로고
    • Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay
    • Beekman B., van El B., Drijfhout J.W., Ronday H.K., TeKoppele J.M. Highly increased levels of active stromelysin in rheumatoid synovial fluid determined by a selective fluorogenic assay. FEBS Lett 1997, 418:305-309.
    • (1997) FEBS Lett , vol.418 , pp. 305-309
    • Beekman, B.1    van El, B.2    Drijfhout, J.W.3    Ronday, H.K.4    TeKoppele, J.M.5
  • 34
    • 1542744002 scopus 로고    scopus 로고
    • Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases
    • Rasmussen F.H., Yeung N., Kiefer L., Murphy G., Lopez-Otin C., Vitek M.P., Moss M.L. Use of a multiple-enzyme/multiple-reagent assay system to quantify activity levels in samples containing mixtures of matrix metalloproteinases. Biochemistry 2004, 43:2987-2995.
    • (2004) Biochemistry , vol.43 , pp. 2987-2995
    • Rasmussen, F.H.1    Yeung, N.2    Kiefer, L.3    Murphy, G.4    Lopez-Otin, C.5    Vitek, M.P.6    Moss, M.L.7
  • 35
    • 34250169073 scopus 로고    scopus 로고
    • Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening
    • Moss M.L., Rasmussen F.H. Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening. Anal Biochem 2007, 366:144-148.
    • (2007) Anal Biochem , vol.366 , pp. 144-148
    • Moss, M.L.1    Rasmussen, F.H.2
  • 36
    • 44849120587 scopus 로고    scopus 로고
    • Drug insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis
    • Moss M.L., Sklair-Tavron L., Nudelman R. Drug insight: tumor necrosis factor-converting enzyme as a pharmaceutical target for rheumatoid arthritis. Nat Clin Pract Rheumatol 2008, 4:300-309.
    • (2008) Nat Clin Pract Rheumatol , vol.4 , pp. 300-309
    • Moss, M.L.1    Sklair-Tavron, L.2    Nudelman, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.