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Volumn 14, Issue 20, 2008, Pages 6610-6617

Tumor-specific urinary matrix metalloproteinase fingerprinting: Identification of high molecular weight urinary matrix metalloproteinase species

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; PROTEIN ADAMTS 7; UNCLASSIFIED DRUG; ADAM PROTEIN; ADAMTS7 PROTEIN, HUMAN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TUMOR MARKER;

EID: 58049203639     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-08-1136     Document Type: Article
Times cited : (140)

References (45)
  • 1
    • 33344466450 scopus 로고    scopus 로고
    • Making the cut: Protease-mediated regulation of angiogenesis
    • Roy R, Zhang B, Moses MA. Making the cut: protease-mediated regulation of angiogenesis. Exp Cell Res 2006;312:608-22.
    • (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 AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 1997;89:1260-70.
    • (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 GI. Matrix metalloproteinases in tumour invasion and metastasis. J Pathol 1999;189:300-8.
    • (1999) J Pathol , vol.189 , pp. 300-308
    • Curran, S.1    Murray, G.I.2
  • 6
    • 0034635995 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 is required for the switch to the angiogenic phenotype in a tumor mode
    • Fang J, Shing Y, Wiederschain D, et al. Matrix metalloproteinase-2 is required for the switch to the angiogenic phenotype in a tumor mode. Proc Nat Acad Sci USA 2000;97:3884-9.
    • (2000) Proc Nat Acad Sci USA , vol.97 , pp. 3884-3889
    • Fang, J.1    Shing, Y.2    Wiederschain, D.3
  • 7
    • 0000391746 scopus 로고    scopus 로고
    • Matrix met-alloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers G, Brekken R, McMahon G, et al. Matrix met-alloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2000;2:737-44.
    • (2000) Nat Cell Biol , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    McMahon, G.3
  • 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. Nature reviews 2002;2:161-74.
    • (2002) Nature reviews , 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;70:1-14.
    • (2003) Biochem Soc Symp , vol.70 , pp. 1-14
    • Bode, W.1
  • 10
    • 0026802371 scopus 로고
    • Correlation of serum metalloproteinase levels with lung cancer metastasis and response to therapy
    • Garbisa S, Scagliotti G, Masiero L, et al. Correlation of serum metalloproteinase levels with lung cancer metastasis and response to therapy. Cancer Res 1992;52:4548-9.
    • (1992) Cancer Res , vol.52 , pp. 4548-4549
    • Garbisa, S.1    Scagliotti, G.2    Masiero, L.3
  • 11
    • 0027331362 scopus 로고
    • Serum and plasma M(r) 92,000 progelatinase levels correlate with spontaneous metastasis of rat 13762NF mammary adenocarcinoma
    • Nakajima M, Welch DR, Wynn DM, TsuruoT, Nicolson GL. Serum and plasma M(r) 92,000 progelatinase levels correlate with spontaneous metastasis of rat 13762NF mammary adenocarcinoma. Cancer Res 1993;53:5802-7.
    • (1993) Cancer Res , vol.53 , pp. 5802-5807
    • Nakajima, M.1    Welch, D.R.2    Wynn, D.M.3    Tsuruo, T.4    Nicolson, G.L.5
  • 12
    • 0029845841 scopus 로고    scopus 로고
    • Elevationof serum levels of matrix metalloproteinase-2 and-3 as new predictors of recurrence in patients with urothelial carcinoma
    • Gohji K, Fujimoto N, Komiyama T, et al. Elevationof serum levels of matrix metalloproteinase-2 and-3 as new predictors of recurrence in patients with urothelial carcinoma. Cancer1996;78:2379-87.
    • Cancer1996 , vol.78 , pp. 2379-2387
    • Gohji, K.1    Fujimoto, N.2    Komiyama, T.3
  • 13
    • 0037380202 scopus 로고    scopus 로고
    • Serum levels of endostatin and matrix metalloproteinase-9 associated with high stage and grade primary transitional cell carcinoma of the bladder
    • Guan KP, Ye HY, Yan Z,Wang Y, Hou SK. Serum levels of endostatin and matrix metalloproteinase-9 associated with high stage and grade primary transitional cell carcinoma of the bladder. Urology 2003;61:719-23.
    • (2003) Urology , vol.61 , pp. 719-723
    • Guan, K.P.1    Ye, H.Y.2    Yan, Z.3    Wang, Y.4    Hou, S.K.5
  • 14
    • 34249748753 scopus 로고    scopus 로고
    • Serum tissue inhibitor of metalloproteinase-2 (TIMP-2) and matrix metalloproteinase-2 in complex with the inhibitor (MMP-2:TIMP-2) as prognostic markers in bladder cancer
    • Vasala K, Turpeenniemi-Hujanen T. Serum tissue inhibitor of metalloproteinase-2 (TIMP-2) and matrix metalloproteinase-2 in complex with the inhibitor (MMP-2:TIMP-2) as prognostic markers in bladder cancer. Clin Biochem 2007;40:640-4.
    • (2007) Clin Biochem , vol.40 , pp. 640-644
    • Vasala, K.1    Turpeenniemi-Hujanen, T.2
  • 15
    • 40749099079 scopus 로고    scopus 로고
    • Prognostic significance of MMP-9 andTIMP-1 serum and tissue expression in breast cancer
    • Wu ZS, Wu Q, Yang JH, et al. Prognostic significance of MMP-9 andTIMP-1 serum and tissue expression in breast cancer. Int J Cancer 2008;122:2050-6.
    • (2008) Int J Cancer , vol.122 , pp. 2050-2056
    • Wu, Z.S.1    Wu, Q.2    Yang, J.H.3
  • 16
    • 0027384917 scopus 로고
    • Levels of matrix metalloproteases in bladder cancer correlate with tumor grade and invasion
    • Davies B, Waxman J, Wasan H, et al. Levels of matrix metalloproteases in bladder cancer correlate with tumor grade and invasion. Cancer Res 1993;53:5365-9.
    • (1993) Cancer Res , vol.53 , pp. 5365-5369
    • Davies, B.1    Waxman, J.2    Wasan, H.3
  • 17
    • 0037441381 scopus 로고    scopus 로고
    • Plasma matrix metal- loproteinase 9 as biomarker of prostate cancer progression in Dunning (Copenhagen) rats
    • Jung K, Krell HW, Ortel B, et al. Plasma matrix metal- loproteinase 9 as biomarker of prostate cancer progression in Dunning (Copenhagen) rats. Prostate 2003;54:206-11.
    • (2003) Prostate , vol.54 , pp. 206-211
    • Jung, K.1    Krell, H.W.2    Ortel, B.3
  • 19
    • 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 MA. 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;276:37258-65.
    • (2001) J Biol Chem , vol.276 , pp. 37258-37265
    • Yan, L.1    Borregaard, N.2    Kjeldsen, L.3    Moses, M.A.4
  • 20
    • 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 CA,Yan L, Louis G,Yang J, Kutok JL, Moses MA. 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;11:5390-5.
    • (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
  • 21
    • 42249085231 scopus 로고    scopus 로고
    • Urinary biomarkers predict brain tumor presence and response to therapy
    • Smith E, Zurakowski D, Saad A, Scott RM, Moses MA. Urinary biomarkers predict brain tumor presence and response to therapy. Clin Cancer Res 2008;14:2378-86.
    • (2008) Clin Cancer Res , vol.14 , pp. 2378-2386
    • Smith, E.1    Zurakowski, D.2    Saad, A.3    Scott, R.M.4    Moses, M.A.5
  • 22
    • 34249829865 scopus 로고    scopus 로고
    • A recurrent craniopharyngioma illustrates the potential usefulness of urinary matrix metalloproteinases as noninvasive biomarkers: Case report
    • discussion E9
    • Smith ER, Manfredi M, Scott RM, Black PM, Moses MA. A recurrent craniopharyngioma illustrates the potential usefulness of urinary matrix metalloproteinases as noninvasive biomarkers: case report. Neurosurgery 2007;60:E1148-9;discussion E9.
    • (2007) Neurosurgery , vol.60
    • Smith, E.R.1    Manfredi, M.2    Scott, R.M.3    Black, P.M.4    Moses, M.A.5
  • 23
    • 0034122601 scopus 로고    scopus 로고
    • Enhanced urinary gelatinase activities (matrix metalloproteinases 2 and 9) are associated with early-stage bladder carcinoma: A comparison with clinically used tumor markers
    • Sier CF, Casetta G,Verheijen JH, et al. Enhanced urinary gelatinase activities (matrix metalloproteinases 2 and 9) are associated with early-stage bladder carcinoma: a comparison with clinically used tumor markers. Clin Cancer Res 2000;6:2333-40.
    • (2000) Clin Cancer Res , vol.6 , pp. 2333-2340
    • Sier, C.F.1    Casetta, G.2    Verheijen, J.H.3
  • 24
    • 0033936377 scopus 로고    scopus 로고
    • Gelatinase isoforms in urine from bladder cancer pzatients
    • Monier F, Surla A, Guillot M, Morel F. Gelatinase isoforms in urine from bladder cancer pzatients. Clin Chim Acta 2000;299:11-23.
    • (2000) Clin Chim Acta , vol.299 , pp. 11-23
    • Monier, F.1    Surla, A.2    Guillot, M.3    Morel, F.4
  • 25
    • 0035318082 scopus 로고    scopus 로고
    • Excretion of matrix metalloproteinases 2 and 9 in urine is associated with a high stage and grade of bladder carcinoma
    • Gerhards S, Jung K, Koenig F, et al. Excretion of matrix metalloproteinases 2 and 9 in urine is associated with a high stage and grade of bladder carcinoma. Urology2001;57:675-9.
    • Urology2001;57 , pp. 675-679
    • Gerhards, S.1    Jung, K.2    Koenig, F.3
  • 26
    • 0035186345 scopus 로고    scopus 로고
    • Prognostic significance of matrix metal-loproteinase-1 and tissue inhibitor of metalloprotei-nase-1 in voided urine samples from patients with transitional cell carcinoma of the bladder
    • Durkan GC, Nutt JE, Rajjayabun PH, Neal DE, Lunec J, Mellon JK. Prognostic significance of matrix metal-loproteinase-1 and tissue inhibitor of metalloprotei-nase-1 in voided urine samples from patients with transitional cell carcinoma of the bladder. Clin Cancer Res 2001;7:3450-6.
    • (2001) Clin Cancer Res , vol.7 , pp. 3450-3456
    • Durkan, G.C.1    Nutt, J.E.2    Rajjayabun, P.H.3    Neal, D.E.4    Lunec, J.5    Mellon, J.K.6
  • 27
    • 0036795252 scopus 로고    scopus 로고
    • Urinary release of 72 and 92 kDa gelatinases, TIMPs, N-GAL and conventional prognostic factors in urothelial carcinomas
    • Monier F, Mollier S, Guillot M, Rambeaud JJ, Morel F, Zaoui P. Urinary release of 72 and 92 kDa gelatinases, TIMPs, N-GAL and conventional prognostic factors in urothelial carcinomas. Eur Urol 2002;42:356-63.
    • (2002) Eur Urol , vol.42 , pp. 356-363
    • Monier, F.1    Mollier, S.2    Guillot, M.3    Rambeaud, J.J.4    Morel, F.5    Zaoui, P.6
  • 28
    • 0142243281 scopus 로고    scopus 로고
    • Diagnostic value of urinary molecular markers in bladder cancer
    • Eissa S, Swellam M, el-Mosallamy H, et al. Diagnostic value of urinary molecular markers in bladder cancer. Anticancer Res 2003;23:4347-55.
    • (2003) Anticancer Res , vol.23 , pp. 4347-4355
    • Eissa, S.1    Swellam, M.2    el-Mosallamy, H.3
  • 29
    • 0037234945 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in bladder cancer: The induction of MMP9 by epidermal growth factor and its detection in urine
    • Nutt JE, Durkan GC, Mellon JK, Lunec J. Matrix metalloproteinases (MMPs) in bladder cancer: the induction of MMP9 by epidermal growth factor and its detection in urine. BJU Int 2003;91:99-104.
    • (2003) BJU Int , vol.91 , pp. 99-104
    • Nutt, J.E.1    Durkan, G.C.2    Mellon, J.K.3    Lunec, J.4
  • 30
    • 27144531588 scopus 로고    scopus 로고
    • Proteomeanalysis of gelatin-bound urinary proteins from patients with bladder cancers
    • Saito M, Kimoto M, Araki T, et al. Proteomeanalysis of gelatin-bound urinary proteins from patients with bladder cancers. Eur Urol 2005;48:865-71.
    • (2005) Eur Urol , vol.48 , pp. 865-871
    • Saito, M.1    Kimoto, M.2    Araki, T.3
  • 31
    • 10944263573 scopus 로고    scopus 로고
    • ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage
    • Roy R,Wewer UM, Zurakowski D, Pories SE, Moses MA. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. J Biol Chem 2004;279:51323-30.
    • (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
  • 32
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUES Talgorithm
    • MacCoss MJ, Wu CC, Yates JR III. Probability-based validation of protein identifications using a modified SEQUES Talgorithm. Anal Chem 2002;74:5593-9.
    • (2002) Anal Chem , vol.74 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates III, J.R.3
  • 33
    • 0028760247 scopus 로고
    • Users' guides to the medical literature. III. How to use an article about a diagnostic test. B.What are the results and will they help me in caring for my patients? The Evidence-Based Medicine Working Group
    • Jaeschke R, Guyatt GH, Sackett DL. Users' guides to the medical literature. III. How to use an article about a diagnostic test. B.What are the results and will they help me in caring for my patients? The Evidence-Based Medicine Working Group. JAMA 1994;271: 703-7.
    • (1994) JAMA , vol.271 , pp. 703-707
    • Jaeschke, R.1    Guyatt, G.H.2    Sackett, D.L.3
  • 35
    • 0026630048 scopus 로고
    • Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin
    • Goldberg GI, Strongin A, Collier IE, Genrich LT, Marmer BL. Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J Biol Chem 1992;267:4583-91.
    • (1992) J Biol Chem , vol.267 , pp. 4583-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 36
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen L, Johnsen AH, Sengelov H, Borregaard N. Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J Biol Chem 1993;268:10425-32.
    • (1993) J Biol Chem , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengelov, H.3    Borregaard, N.4
  • 37
    • 0030755456 scopus 로고    scopus 로고
    • Phorbol ester-induced cell surface association of matrix metalloprotei-nase-9 in human MCF10A breast epithelial cells
    • Toth M, Gervasi DC, Fridman R. Phorbol ester-induced cell surface association of matrix metalloprotei-nase-9 in human MCF10A breast epithelial cells. Cancer Res 1997;57:3159-67.
    • (1997) Cancer Res , vol.57 , pp. 3159-3167
    • Toth, M.1    Gervasi, D.C.2    Fridman, R.3
  • 38
    • 0024414124 scopus 로고
    • Human gelatinase/type IV procollagenase is a regular plasma component
    • Vartio T, Baumann M. Human gelatinase/type IV procollagenase is a regular plasma component. FEBS Lett 1989;255:285-9.
    • (1989) FEBS Lett , vol.255 , pp. 285-289
    • Vartio, T.1    Baumann, M.2
  • 39
    • 0034723402 scopus 로고    scopus 로고
    • Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1
    • Olson MW, Bernardo MM, Pietila M, et al. Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1. J Biol Chem 2000;275:2661-8.
    • (2000) J Biol Chem , vol.275 , pp. 2661-2668
    • Olson, M.W.1    Bernardo, M.M.2    Pietila, M.3
  • 40
    • 33747159104 scopus 로고    scopus 로고
    • MMP-9 and MMP-2 gelatinases and TIMP-1 and TIMP-2 inhibitors in breast cancer: Correlations with prognostic factors
    • Jinga DC, Blidaru A, Condrea I, et al. MMP-9 and MMP-2 gelatinases and TIMP-1 and TIMP-2 inhibitors in breast cancer: correlations with prognostic factors. J Cell Mol Med 2006;10:499-510.
    • (2006) J Cell Mol Med , vol.10 , pp. 499-510
    • Jinga, D.C.1    Blidaru, A.2    Condrea, I.3
  • 41
    • 33847197955 scopus 로고    scopus 로고
    • Usefulness of MMP-9/TIMP-1 in predicting tumor recurrence in patients undergoing curative surgical resection for gastric car-cinoma.Dig Dis
    • Seo YS, Park JJ, Kim JH, et al. Usefulness of MMP-9/TIMP-1 in predicting tumor recurrence in patients undergoing curative surgical resection for gastric car-cinoma.Dig Dis Sci 2007;52:753-9.
    • (2007) Sci , vol.52 , pp. 753-759
    • Seo, Y.S.1    Park, J.J.2    Kim, J.H.3
  • 42
    • 16844381574 scopus 로고    scopus 로고
    • Matrix metalloproteinases as diagnostic (MMP-13) and prognostic (MMP-2, MMP-9) markers of prostate cancer
    • Morgia G, Falsaperla M, Malaponte G, et al. Matrix metalloproteinases as diagnostic (MMP-13) and prognostic (MMP-2, MMP-9) markers of prostate cancer. Neurol Res 2005;33:44-50.
    • (2005) Neurol Res , vol.33 , pp. 44-50
    • Morgia, G.1    Falsaperla, M.2    Malaponte, G.3
  • 44
    • 4143112912 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type1 motifs: The ADAMTS family
    • Apte SS. A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type1 motifs: the ADAMTS family. Int J Biochem Cell Biol 2004;36: 981-5.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 981-985
    • Apte, S.S.1
  • 45
    • 33845702259 scopus 로고    scopus 로고
    • ADAMTS-7: A metal-loproteinase that directly binds to and degrades cartilage oligomeric matrix protein
    • Liu CJ, Kong W, Ilalov K, et al. ADAMTS-7: a metal-loproteinase that directly binds to and degrades cartilage oligomeric matrix protein. FASEB J 2006;20:988-90.
    • (2006) FASEB J , vol.20 , pp. 988-990
    • Liu, C.J.1    Kong, W.2    Ilalov, K.3


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