메뉴 건너뛰기




Volumn 36, Issue , 2014, Pages 64-76

Matrilysin/matrix metalloproteinase-7(MMP7) cleavage of perlecan/HSPG2 creates a molecular switch to alter prostate cancer cell behavior

Author keywords

Matrilysin; Matrix metalloproteinase 7 MMP7; Perlecan HSPG2; Prostate cancer

Indexed keywords

HEPSIN; IMMUNOGLOBULIN; MATRILYSIN; PERLECAN; PROSTATE SPECIFIC ANTIGEN; MMP7 PROTEIN, HUMAN; PROTEOHEPARAN SULFATE; SCLEROPROTEIN;

EID: 84909966044     PISSN: 0945053X     EISSN: 15691802     Source Type: Journal    
DOI: 10.1016/j.matbio.2014.04.005     Document Type: Article
Times cited : (62)

References (68)
  • 2
    • 3843135193 scopus 로고    scopus 로고
    • Perlecan and its immunoglobulin like domain IV are abundant in vitreous and serum of the chick embryo
    • Balasubramani M., Bier M.E., Hummel S., Schneider W.J., Halfter W. Perlecan and its immunoglobulin like domain IV are abundant in vitreous and serum of the chick embryo. Matrix Biol. 2004, 23:143-152.
    • (2004) Matrix Biol. , vol.23 , pp. 143-152
    • Balasubramani, M.1    Bier, M.E.2    Hummel, S.3    Schneider, W.J.4    Halfter, W.5
  • 3
    • 84861537861 scopus 로고    scopus 로고
    • The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens
    • Behrens D.T., Villone D., Koch M., Brunner G., Sorokin L., Robenek H., Bruckner-Tuderman L., Bruckner P., Hansen U. The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens. J. Biol. Chem. 2012, 287:18700-18709.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18700-18709
    • Behrens, D.T.1    Villone, D.2    Koch, M.3    Brunner, G.4    Sorokin, L.5    Robenek, H.6    Bruckner-Tuderman, L.7    Bruckner, P.8    Hansen, U.9
  • 7
    • 33645825874 scopus 로고    scopus 로고
    • Quantitative immunohistochemical and in situ hybridization analysis of metalloproteinases in prostate cancer
    • Cardillo M.R., Di Silverio F., Gentile V. Quantitative immunohistochemical and in situ hybridization analysis of metalloproteinases in prostate cancer. Anticancer Res. 2006, 26:973-982.
    • (2006) Anticancer Res. , vol.26 , pp. 973-982
    • Cardillo, M.R.1    Di Silverio, F.2    Gentile, V.3
  • 8
    • 21244441962 scopus 로고    scopus 로고
    • Functional characterization of neostatins, the MMP-derived, enzymatic cleavage products of type XVIII collagen
    • Chang J.H., Javier J.A., Chang G.Y., Oliveira H.B., Azar D.T. Functional characterization of neostatins, the MMP-derived, enzymatic cleavage products of type XVIII collagen. FEBS Lett. 2005, 579:3601-3606.
    • (2005) FEBS Lett. , vol.579 , pp. 3601-3606
    • Chang, J.H.1    Javier, J.A.2    Chang, G.Y.3    Oliveira, H.B.4    Azar, D.T.5
  • 9
    • 33846018363 scopus 로고    scopus 로고
    • Effect of fibroblast activation protein and alpha2-antiplasmin cleaving enzyme on collagen types I, III, and IV
    • Christiansen V.J., Jackson K.W., Lee K.N., McKee P.A. Effect of fibroblast activation protein and alpha2-antiplasmin cleaving enzyme on collagen types I, III, and IV. Arch. Biochem. Biophys. 2007, 457:177-186.
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 177-186
    • Christiansen, V.J.1    Jackson, K.W.2    Lee, K.N.3    McKee, P.A.4
  • 12
    • 38949207947 scopus 로고    scopus 로고
    • A novel peptide sequence in perlecan domain IV supports cell adhesion, spreading and FAK activation
    • Farach-Carson M.C., Brown A.J., Lynam M., Safran J.B., Carson D.D. A novel peptide sequence in perlecan domain IV supports cell adhesion, spreading and FAK activation. Matrix Biol. 2008, 27:150-160.
    • (2008) Matrix Biol. , vol.27 , pp. 150-160
    • Farach-Carson, M.C.1    Brown, A.J.2    Lynam, M.3    Safran, J.B.4    Carson, D.D.5
  • 13
    • 84900304808 scopus 로고    scopus 로고
    • Border patrol: Insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders
    • (Epub ahead of print)
    • Farach-Carson M.C., Warren C.R., Harrington D.A., Carson D.D. Border patrol: Insights into the unique role of perlecan/heparan sulfate proteoglycan 2 at cell and tissue borders. Matrix Biol. 2014, 34:64-79. (Epub ahead of print).
    • (2014) Matrix Biol. , vol.34 , pp. 64-79
    • Farach-Carson, M.C.1    Warren, C.R.2    Harrington, D.A.3    Carson, D.D.4
  • 14
    • 0026701977 scopus 로고
    • The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B
    • Fosang A.J., Neame P.J., Last K., Hardingham T.E., Murphy G., Hamilton J.A. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J. Biol. Chem. 1992, 267:19470-19474.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19470-19474
    • Fosang, A.J.1    Neame, P.J.2    Last, K.3    Hardingham, T.E.4    Murphy, G.5    Hamilton, J.A.6
  • 15
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase.
    • Fu X., Kassim S.Y., Parks W.C., Heinecke J.W. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J. Biol. Chem. 2001, 276:41279-41287.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 16
    • 0034682850 scopus 로고    scopus 로고
    • Perlecan heparan sulfate proteoglycan: a novel receptor that mediates a distinct pathway for ligand catabolism
    • Fuki I.V., Iozzo R.V., Williams K.J. Perlecan heparan sulfate proteoglycan: a novel receptor that mediates a distinct pathway for ligand catabolism. J. Biol. Chem. 2000, 275:25742-25750.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25742-25750
    • Fuki, I.V.1    Iozzo, R.V.2    Williams, K.J.3
  • 18
    • 0032126693 scopus 로고    scopus 로고
    • Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope
    • Gohring W., Sasaki T., Heldin C.H., Timpl R. Mapping of the binding of platelet-derived growth factor to distinct domains of the basement membrane proteins BM-40 and perlecan and distinction from the BM-40 collagen-binding epitope. Eur. J. Biochem. 1998, 255:60-66.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 60-66
    • Gohring, W.1    Sasaki, T.2    Heldin, C.H.3    Timpl, R.4
  • 20
    • 69249230753 scopus 로고    scopus 로고
    • Hyaluronic acid-based hydrogels as 3D matrices for in vitro evaluation of chemotherapeutic drugs using poorly adherent prostate cancer cells
    • Gurski L.A., Jha A.K., Zhang C., Jia X., Farach-Carson M.C. Hyaluronic acid-based hydrogels as 3D matrices for in vitro evaluation of chemotherapeutic drugs using poorly adherent prostate cancer cells. Biomaterials 2009, 30:6076-6085.
    • (2009) Biomaterials , vol.30 , pp. 6076-6085
    • Gurski, L.A.1    Jha, A.K.2    Zhang, C.3    Jia, X.4    Farach-Carson, M.C.5
  • 21
    • 0037041640 scopus 로고    scopus 로고
    • Role of proteolytic enzymes in human prostate bone metastasis formation: in vivo and in vitro studies
    • Hart C.A., Scott L.J., Bagley S., Bryden A.A., Clarke N.W., Lang S.H. Role of proteolytic enzymes in human prostate bone metastasis formation: in vivo and in vitro studies. Br. J. Cancer 2002, 86:1136-1142.
    • (2002) Br. J. Cancer , vol.86 , pp. 1136-1142
    • Hart, C.A.1    Scott, L.J.2    Bagley, S.3    Bryden, A.A.4    Clarke, N.W.5    Lang, S.H.6
  • 22
    • 0008427936 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-7 and tissue inhibitor of metalloproteinase-1 in human prostate
    • Hashimoto K., Kihira Y., Matuo Y., Usui T. Expression of matrix metalloproteinase-7 and tissue inhibitor of metalloproteinase-1 in human prostate. J. Urol. 1998, 160:1872-1876.
    • (1998) J. Urol. , vol.160 , pp. 1872-1876
    • Hashimoto, K.1    Kihira, Y.2    Matuo, Y.3    Usui, T.4
  • 24
    • 0024830822 scopus 로고
    • Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes
    • Heremans A., van der Schueren B., de Cock B., Paulsson M., Cassiman J.J., van den Berghe H., David G. Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes. J. Cell Biol. 1989, 109:3199-3211.
    • (1989) J. Cell Biol. , vol.109 , pp. 3199-3211
    • Heremans, A.1    van der Schueren, B.2    de Cock, B.3    Paulsson, M.4    Cassiman, J.J.5    van den Berghe, H.6    David, G.7
  • 25
    • 0033082328 scopus 로고    scopus 로고
    • Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin
    • Hopf M., Gohring W., Kohfeldt E., Yamada Y., Timpl R. Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin. Eur. J. Biochem. 1999, 259:917-925.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 917-925
    • Hopf, M.1    Gohring, W.2    Kohfeldt, E.3    Yamada, Y.4    Timpl, R.5
  • 26
    • 0029081738 scopus 로고
    • Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9
    • Imai K., Shikata H., Okada Y. Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9. FEBS Lett. 1995, 369:249-251.
    • (1995) FEBS Lett. , vol.369 , pp. 249-251
    • Imai, K.1    Shikata, H.2    Okada, Y.3
  • 27
    • 0021258357 scopus 로고
    • Biosynthesis of heparan sulfate proteoglycan by human colon carcinoma cells and its localization at the cell surface
    • Iozzo R.V. Biosynthesis of heparan sulfate proteoglycan by human colon carcinoma cells and its localization at the cell surface. J. Cell Biol. 1984, 99:403-417.
    • (1984) J. Cell Biol. , vol.99 , pp. 403-417
    • Iozzo, R.V.1
  • 28
    • 66749098832 scopus 로고    scopus 로고
    • Basement membrane proteoglycans: modulators Par Excellence of cancer growth and angiogenesis
    • Iozzo R.V., Zoeller J.J., Nystrom A. Basement membrane proteoglycans: modulators Par Excellence of cancer growth and angiogenesis. Mol. Cells 2009, 27:503-513.
    • (2009) Mol. Cells , vol.27 , pp. 503-513
    • Iozzo, R.V.1    Zoeller, J.J.2    Nystrom, A.3
  • 30
    • 77949871625 scopus 로고    scopus 로고
    • Proteome mining of human follicular fluid reveals a crucial role of complement cascade and key biological pathways in women undergoing in vitro fertilization
    • Jarkovska K., Martinkova J., Liskova L., Halada P., Moos J., Rezabek K., Gadher S.J., Kovarova H. Proteome mining of human follicular fluid reveals a crucial role of complement cascade and key biological pathways in women undergoing in vitro fertilization. J. Proteome Res. 2010, 9:1289-1301.
    • (2010) J. Proteome Res. , vol.9 , pp. 1289-1301
    • Jarkovska, K.1    Martinkova, J.2    Liskova, L.3    Halada, P.4    Moos, J.5    Rezabek, K.6    Gadher, S.J.7    Kovarova, H.8
  • 33
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 34
    • 84861112580 scopus 로고    scopus 로고
    • Fibroblast activation protein-alpha: a key modulator of the microenvironment in multiple pathologies
    • Kelly T., Huang Y., Simms A.E., Mazur A. Fibroblast activation protein-alpha: a key modulator of the microenvironment in multiple pathologies. Int. Rev. Cell Mol. Biol. 2012, 297:83-116.
    • (2012) Int. Rev. Cell Mol. Biol. , vol.297 , pp. 83-116
    • Kelly, T.1    Huang, Y.2    Simms, A.E.3    Mazur, A.4
  • 36
    • 0028625509 scopus 로고
    • Perlecan in human bone marrow: a growth-factor-presenting, but anti-adhesive, extracellular matrix component for hematopoietic cells
    • Klein G., Conzelmann S., Beck S., Timpl R., Muller C.A. Perlecan in human bone marrow: a growth-factor-presenting, but anti-adhesive, extracellular matrix component for hematopoietic cells. Matrix Biol. 1995, 14:457-465.
    • (1995) Matrix Biol. , vol.14 , pp. 457-465
    • Klein, G.1    Conzelmann, S.2    Beck, S.3    Timpl, R.4    Muller, C.A.5
  • 37
    • 55549104048 scopus 로고    scopus 로고
    • Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling
    • Lamanna W.C., Frese M.A., Balleininger M., Dierks T. Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling. J. Biol. Chem. 2008, 283:27724-27735.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27724-27735
    • Lamanna, W.C.1    Frese, M.A.2    Balleininger, M.3    Dierks, T.4
  • 40
    • 0037423391 scopus 로고    scopus 로고
    • Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan
    • Mongiat M., Sweeney S.M., San Antonio J.D., Fu J., Iozzo R.V. Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan. J. Biol. Chem. 2003, 278:4238-4249.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4238-4249
    • Mongiat, M.1    Sweeney, S.M.2    San Antonio, J.D.3    Fu, J.4    Iozzo, R.V.5
  • 41
    • 0030606329 scopus 로고    scopus 로고
    • Purification and characterization of perlecan fragment in urine of end-stage renal failure patients
    • Oda O., Shinzato T., Ohbayashi K., Takai I., Kunimatsu M., Maeda K., Yamanaka N. Purification and characterization of perlecan fragment in urine of end-stage renal failure patients. Clin. Chim. Acta 1996, 255:119-132.
    • (1996) Clin. Chim. Acta , vol.255 , pp. 119-132
    • Oda, O.1    Shinzato, T.2    Ohbayashi, K.3    Takai, I.4    Kunimatsu, M.5    Maeda, K.6    Yamanaka, N.7
  • 43
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 44
    • 0346499121 scopus 로고    scopus 로고
    • Epidemiology of inflammation and prostate cancer
    • Platz E.A., De Marzo A.M. Epidemiology of inflammation and prostate cancer. J. Urol. 2004, 171:S36-S40.
    • (2004) J. Urol. , vol.171 , pp. S36-S40
    • Platz, E.A.1    De Marzo, A.M.2
  • 45
    • 63049123066 scopus 로고    scopus 로고
    • Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits
    • Polyak K., Weinberg R.A. Transitions between epithelial and mesenchymal states: acquisition of malignant and stem cell traits. Nat. Rev. Cancer 2009, 9:265-273.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 265-273
    • Polyak, K.1    Weinberg, R.A.2
  • 46
    • 0027530706 scopus 로고
    • Expression of the metalloproteinase matrilysin in DU-145 cells increases their invasive potential in severe combined immunodeficient mice
    • Powell W.C., Knox J.D., Navre M., Grogan T.M., Kittelson J., Nagle R.B., Bowden G.T. Expression of the metalloproteinase matrilysin in DU-145 cells increases their invasive potential in severe combined immunodeficient mice. Cancer Res. 1993, 53:417-422.
    • (1993) Cancer Res. , vol.53 , pp. 417-422
    • Powell, W.C.1    Knox, J.D.2    Navre, M.3    Grogan, T.M.4    Kittelson, J.5    Nagle, R.B.6    Bowden, G.T.7
  • 47
    • 70350458704 scopus 로고    scopus 로고
    • Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans
    • Ra H.J., Harju-Baker S., Zhang F., Linhardt R.J., Wilson C.L., Parks W.C. Control of promatrilysin (MMP7) activation and substrate-specific activity by sulfated glycosaminoglycans. J. Biol. Chem. 2009, 284:27924-27932.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27924-27932
    • Ra, H.J.1    Harju-Baker, S.2    Zhang, F.3    Linhardt, R.J.4    Wilson, C.L.5    Parks, W.C.6
  • 48
    • 1542319836 scopus 로고    scopus 로고
    • Heparanase degrades syndecan-1 and perlecan heparan sulfate: functional implications for tumor cell invasion
    • Reiland J., Sanderson R.D., Waguespack M., Barker S.A., Long R., Carson D.D., Marchetti D. Heparanase degrades syndecan-1 and perlecan heparan sulfate: functional implications for tumor cell invasion. J. Biol. Chem. 2004, 279:8047-8055.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8047-8055
    • Reiland, J.1    Sanderson, R.D.2    Waguespack, M.3    Barker, S.A.4    Long, R.5    Carson, D.D.6    Marchetti, D.7
  • 49
    • 83055170853 scopus 로고    scopus 로고
    • The chicken cornea as a model of wound healing and neuronal re-innervation
    • Ritchey E.R., Code K., Zelinka C.P., Scott M.A., Fischer A.J. The chicken cornea as a model of wound healing and neuronal re-innervation. Mol. Vis. 2011, 17:2440-2454.
    • (2011) Mol. Vis. , vol.17 , pp. 2440-2454
    • Ritchey, E.R.1    Code, K.2    Zelinka, C.P.3    Scott, M.A.4    Fischer, A.J.5
  • 50
    • 54049137191 scopus 로고    scopus 로고
    • Breaching the basement membrane: who, when and how?
    • Rowe R.G., Weiss S.J. Breaching the basement membrane: who, when and how?. Trends Cell Biol. 2008, 18:560-574.
    • (2008) Trends Cell Biol. , vol.18 , pp. 560-574
    • Rowe, R.G.1    Weiss, S.J.2
  • 51
    • 41149140769 scopus 로고    scopus 로고
    • MMass data miner: an open source alternative for mass spectrometric data analysis
    • Strohalm M., Hassman M., Kosata B., Kodicek M. mMass data miner: an open source alternative for mass spectrometric data analysis. Rapid Commun. Mass Spectrom. 2008, 22:905-908.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 905-908
    • Strohalm, M.1    Hassman, M.2    Kosata, B.3    Kodicek, M.4
  • 52
    • 77952980825 scopus 로고    scopus 로고
    • MMass 3: a cross-platform software environment for precise analysis of mass spectrometric data
    • Strohalm M., Kavan D., Novak P., Volny M., Havlicek V. mMass 3: a cross-platform software environment for precise analysis of mass spectrometric data. Anal. Chem. 2010, 82:4648-4651.
    • (2010) Anal. Chem. , vol.82 , pp. 4648-4651
    • Strohalm, M.1    Kavan, D.2    Novak, P.3    Volny, M.4    Havlicek, V.5
  • 53
    • 0034234571 scopus 로고    scopus 로고
    • LNCaP progression model of human prostate cancer: androgen-independence and osseous metastasis
    • (Jul 101;144(102))
    • Thalmann G.N., Sikes R.A., Wu T.T., Degeorges A., Chang S.M., Ozen M., Pathak S., Chung L.W. LNCaP progression model of human prostate cancer: androgen-independence and osseous metastasis. Prostate 2000, 44:91-103. (Jul 101;144(102)).
    • (2000) Prostate , vol.44 , pp. 91-103
    • Thalmann, G.N.1    Sikes, R.A.2    Wu, T.T.3    Degeorges, A.4    Chang, S.M.5    Ozen, M.6    Pathak, S.7    Chung, L.W.8
  • 55
    • 57649155897 scopus 로고    scopus 로고
    • Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression
    • Tripathi M., Nandana S., Yamashita H., Ganesan R., Kirchhofer D., Quaranta V. Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression. J. Biol. Chem. 2008, 283:30576-30584.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30576-30584
    • Tripathi, M.1    Nandana, S.2    Yamashita, H.3    Ganesan, R.4    Kirchhofer, D.5    Quaranta, V.6
  • 56
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • Turk B.E., Huang L.L., Piro E.T., Cantley L.C. Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nat. Biotechnol. 2001, 19:661-667.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 57
    • 0036718369 scopus 로고    scopus 로고
    • Reactive stroma in human prostate cancer: induction of myofibroblast phenotype and extracellular matrix remodeling
    • Tuxhorn J.A., Ayala G.E., Smith M.J., Smith V.C., Dang T.D., Rowley D.R. Reactive stroma in human prostate cancer: induction of myofibroblast phenotype and extracellular matrix remodeling. Clin. Cancer Res. 2002, 8:2912-2923.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2912-2923
    • Tuxhorn, J.A.1    Ayala, G.E.2    Smith, M.J.3    Smith, V.C.4    Dang, T.D.5    Rowley, D.R.6
  • 60
    • 84900027494 scopus 로고    scopus 로고
    • Perlecan/HSPG2 increases in the desmoplastic prostate tumor microenvironment involve transcriptional activation by nuclear factor kappa B
    • Warren C.R., Grindel B.J., Farach-Carson M.C., Carson D. Perlecan/HSPG2 increases in the desmoplastic prostate tumor microenvironment involve transcriptional activation by nuclear factor kappa B. Clin. Exp. Metastasis 2014, 115(7):1322-1333.
    • (2014) Clin. Exp. Metastasis , vol.115 , Issue.7 , pp. 1322-1333
    • Warren, C.R.1    Grindel, B.J.2    Farach-Carson, M.C.3    Carson, D.4
  • 61
    • 0028865036 scopus 로고
    • Prostate-specific antigen, a serine protease, facilitates human prostate cancer cell invasion
    • Webber M.M., Waghray A., Bello D. Prostate-specific antigen, a serine protease, facilitates human prostate cancer cell invasion. Clin. Cancer Res. 1995, 1:1089-1094.
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1089-1094
    • Webber, M.M.1    Waghray, A.2    Bello, D.3
  • 62
    • 0029666453 scopus 로고    scopus 로고
    • Understanding the P1' specificity of the matrix metalloproteinases: effect of S1' pocket mutations in matrilysin and stromelysin-1
    • Welch A.R., Holman C.M., Huber M., Brenner M.C., Browner M.F., Van Wart H.E. Understanding the P1' specificity of the matrix metalloproteinases: effect of S1' pocket mutations in matrilysin and stromelysin-1. Biochemistry 1996, 35:10103-10109.
    • (1996) Biochemistry , vol.35 , pp. 10103-10109
    • Welch, A.R.1    Holman, C.M.2    Huber, M.3    Brenner, M.C.4    Browner, M.F.5    Van Wart, H.E.6
  • 63
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock J.M., Murdoch A.D., Iozzo R.V., Underwood P.A. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J. Biol. Chem. 1996, 271:10079-10086.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 64
    • 54849436630 scopus 로고    scopus 로고
    • Diverse cell signaling events modulated by perlecan
    • Whitelock J.M., Melrose J., Iozzo R.V. Diverse cell signaling events modulated by perlecan. Biochemistry 2008, 47:11174-11183.
    • (2008) Biochemistry , vol.47 , pp. 11174-11183
    • Whitelock, J.M.1    Melrose, J.2    Iozzo, R.V.3
  • 65
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metalloproteinase of the rat uterus
    • Woessner J.F., Taplin C.J. Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J. Biol. Chem. 1988, 263:16918-16925.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16918-16925
    • Woessner, J.F.1    Taplin, C.J.2
  • 66
    • 0028321891 scopus 로고
    • Derivation of androgen-independent human LNCaP prostatic cancer cell sublines: role of bone stromal cells
    • Wu H.C., Hsieh J.T., Gleave M.E., Brown N.M., Pathak S., Chung L.W. Derivation of androgen-independent human LNCaP prostatic cancer cell sublines: role of bone stromal cells. Int. J. Cancer 1994, 57:406-412.
    • (1994) Int. J. Cancer , vol.57 , pp. 406-412
    • Wu, H.C.1    Hsieh, J.T.2    Gleave, M.E.3    Brown, N.M.4    Pathak, S.5    Chung, L.W.6
  • 67
    • 0034635483 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)
    • Yu W.H., Woessner J.F. Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). J. Biol. Chem. 2000, 275:4183-4191.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4183-4191
    • Yu, W.H.1    Woessner, J.F.2
  • 68
    • 0032010153 scopus 로고    scopus 로고
    • A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
    • Zhang Z., Marshall A.G. A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 1998, 9:225-233.
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 225-233
    • Zhang, Z.1    Marshall, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.