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Volumn 19, Issue 1, 2008, Pages 57-64

Matrix metalloproteinase-assisted triggered release of liposomal contents

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYFLUORESCEIN; GELATINASE B; LIPOPEPTIDE; LIPOSOME; MATRIX METALLOPROTEINASE; PEPTIDE DERIVATIVE; TRYPSIN;

EID: 38949203367     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc070081p     Document Type: Article
Times cited : (62)

References (35)
  • 1
    • 31744445961 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in health and disease: An overview
    • Malemud, C. J. (2006) Matrix metalloproteinases (MMPs) in health and disease: an overview. Front. Biosci. 11, 1696-1701.
    • (2006) Front. Biosci , vol.11 , pp. 1696-1701
    • Malemud, C.J.1
  • 2
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • Deryugina, E. I., and Quigley, J. P. (2006) Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 25, 9-34.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 3
    • 33846906016 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs): Chemical-biological functions and (Q)SARs
    • Verma, R. P., and Hansch, C. (2007) Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs. Bioorg. Med. Chem. 15, 2223-2268.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 2223-2268
    • Verma, R.P.1    Hansch, C.2
  • 4
    • 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., and Minafra, S. (2004) Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera. Br. J. Cancer 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
  • 5
    • 9944258056 scopus 로고    scopus 로고
    • The role of gelatinases in colorectal cancer progression and metastasis
    • Mook, O. R. F., Frederiks, W. M., and Van Noorden, C. J. F. (2004) The role of gelatinases in colorectal cancer progression and metastasis. Biochim. Biophys. Acta 1705, 69-89.
    • (2004) Biochim. Biophys. Acta , vol.1705 , pp. 69-89
    • Mook, O.R.F.1    Frederiks, W.M.2    Van Noorden, C.J.F.3
  • 7
    • 20244362234 scopus 로고    scopus 로고
    • Dong, Z., Bonfil, R. D., Chinni, S., Deng, X., Trindade Filho, J. C., Bernardo, M., Vaishampayan, U., Che, M., Sloane, B. F., Sheng, S., Fridman, R., and, and Cher, M. L. (2005) Matrix metalloproteinase activity and osteoclasts in experimental prostate cancer bone metastasis tissue. Am. J. Pathol. 166, 1173-1186.
    • Dong, Z., Bonfil, R. D., Chinni, S., Deng, X., Trindade Filho, J. C., Bernardo, M., Vaishampayan, U., Che, M., Sloane, B. F., Sheng, S., Fridman, R., and, and Cher, M. L. (2005) Matrix metalloproteinase activity and osteoclasts in experimental prostate cancer bone metastasis tissue. Am. J. Pathol. 166, 1173-1186.
  • 9
    • 33645060214 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase-2 secretion and invasion by human ovarian cancer cell line SKOV-3 with lysine, proline, arginine, ascorbic acid and green tea extract
    • Roomi, M. W., Ivanov, V., Kalinovsky, T., Niedzwiecki, A., and Rath, M. (2006) Inhibition of matrix metalloproteinase-2 secretion and invasion by human ovarian cancer cell line SKOV-3 with lysine, proline, arginine, ascorbic acid and green tea extract. J. Obstet. Gynaecol. Res. 32, 148-157.
    • (2006) J. Obstet. Gynaecol. Res. 32 , pp. 148-157
    • Roomi, M.W.1    Ivanov, V.2    Kalinovsky, T.3    Niedzwiecki, A.4    Rath, M.5
  • 10
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher, J. F., and Mobashery, S. (2006) Recent advances in MMP inhibitor design. Cancer Metastasis Rev. 25, 115-136.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 11
    • 33746319850 scopus 로고    scopus 로고
    • Emerging implications of nanotechnology on cancer diagnosis and therapeutics
    • Cuenca, A. G., Jiang, H., Hochwald, S. N., Delano, M., Cance, W. G., and Grobmyer, S. R. (2006) Emerging implications of nanotechnology on cancer diagnosis and therapeutics. Cancer 107, 459-466.
    • (2006) Cancer , vol.107 , pp. 459-466
    • Cuenca, A.G.1    Jiang, H.2    Hochwald, S.N.3    Delano, M.4    Cance, W.G.5    Grobmyer, S.R.6
  • 12
    • 14144250911 scopus 로고    scopus 로고
    • Recent advances with liposomes as pharmaceutical carriers
    • Torchilin, V. P. (2005) Recent advances with liposomes as pharmaceutical carriers. Nat. Rev. Drug Discovery 4, 145-160.
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 145-160
    • Torchilin, V.P.1
  • 13
    • 14644399827 scopus 로고    scopus 로고
    • Advanced strategies in liposomal cancer therapy: Problems and prospects of active and tumor specific drug release
    • Anderson, T. L., Jensen, S. S., and Jorgensen, K. (2005) Advanced strategies in liposomal cancer therapy: problems and prospects of active and tumor specific drug release. Prog. Lipid Res. 44, 68-97.
    • (2005) Prog. Lipid Res , vol.44 , pp. 68-97
    • Anderson, T.L.1    Jensen, S.S.2    Jorgensen, K.3
  • 14
    • 33748126226 scopus 로고    scopus 로고
    • Recent approaches to intracellular delivery of drugs and DNA and organelle targeting
    • Torchilin, V. P. (2006) Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Ann. Rev. Biomed. Eng. 8, 343-375.
    • (2006) Ann. Rev. Biomed. Eng , vol.8 , pp. 343-375
    • Torchilin, V.P.1
  • 15
    • 33748498232 scopus 로고    scopus 로고
    • Pros and cons of the liposome platform in cancer drug targeting
    • Gabizon, A. A., Shmeeda, H., and Zalipsky, S. (2006) Pros and cons of the liposome platform in cancer drug targeting. J. Liposome Res. 16, 175-183.
    • (2006) J. Liposome Res , vol.16 , pp. 175-183
    • Gabizon, A.A.1    Shmeeda, H.2    Zalipsky, S.3
  • 16
    • 34250187101 scopus 로고    scopus 로고
    • pH-sensitive liposomes-principle and application in cancer therapy
    • Karanth, H., and Murthy, R. S. R. (2007) pH-sensitive liposomes-principle and application in cancer therapy. J. Pharm. Pharmacol. 59, 469-483.
    • (2007) J. Pharm. Pharmacol , vol.59 , pp. 469-483
    • Karanth, H.1    Murthy, R.S.R.2
  • 17
  • 18
    • 0032213127 scopus 로고    scopus 로고
    • Cholesterol phosphate derivatives: Synthesis and incorporation into a phosphate and calcium sensitive triggered release liposome
    • Davis, S. C., and Szoka, F. C. (1998) Cholesterol phosphate derivatives: synthesis and incorporation into a phosphate and calcium sensitive triggered release liposome. Bioconjugate Chem. 9, 783-792.
    • (1998) Bioconjugate Chem , vol.9 , pp. 783-792
    • Davis, S.C.1    Szoka, F.C.2
  • 20
    • 32044471846 scopus 로고    scopus 로고
    • Photoisomerisable cholesterol derivatives as photo-trigger of liposomes: Effect of lipid polarity, temperature, incorporation ratio, and cholesterol
    • Liu, X. M., Yang, B., Wang, Y. L., and Wang, J. Y. (2005) Photoisomerisable cholesterol derivatives as photo-trigger of liposomes: effect of lipid polarity, temperature, incorporation ratio, and cholesterol. Biochim. Biophys. Acta 1720, 28-34.
    • (2005) Biochim. Biophys. Acta , vol.1720 , pp. 28-34
    • Liu, X.M.1    Yang, B.2    Wang, Y.L.3    Wang, J.Y.4
  • 21
    • 24644473641 scopus 로고    scopus 로고
    • Triggered activation and release of liposomal prodrugs and drugs in cancer tissue by secretory phospholipase A2
    • Andresen, T. L., Jensen, S. S., Kaasgaard, T., and Jørgensen, K. (2005) Triggered activation and release of liposomal prodrugs and drugs in cancer tissue by secretory phospholipase A2. Curr. Drug Delivery 2, 353-362.
    • (2005) Curr. Drug Delivery , vol.2 , pp. 353-362
    • Andresen, T.L.1    Jensen, S.S.2    Kaasgaard, T.3    Jørgensen, K.4
  • 23
    • 0037705345 scopus 로고    scopus 로고
    • Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9
    • Lauer-Fields, J. L., Sritharan, T., Stack, M. S., Nagase, H., and Fields, G. B. (2003) Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9. J. Biol. Chem. 278, 18140-18145.
    • (2003) J. Biol. Chem , vol.278 , pp. 18140-18145
    • Lauer-Fields, J.L.1    Sritharan, T.2    Stack, M.S.3    Nagase, H.4    Fields, G.B.5
  • 25
    • 0042531935 scopus 로고    scopus 로고
    • The role of cystine knots in collagen folding and stability, part II. Conformational properties of (Pro-Hyp-Gly)n model trimers with N- and C-terminal collagen type III cystine knots
    • Barth, D., Kyrieleis, O., Frank, S., Renner, C., and Moroder, L. (2003) The role of cystine knots in collagen folding and stability, part II. Conformational properties of (Pro-Hyp-Gly)n model trimers with N- and C-terminal collagen type III cystine knots. Chem. - Eur. J. 9, 3703-3714.
    • (2003) Chem. - Eur. J , vol.9 , pp. 3703-3714
    • Barth, D.1    Kyrieleis, O.2    Frank, S.3    Renner, C.4    Moroder, L.5
  • 26
    • 0037077541 scopus 로고    scopus 로고
    • Metal assisted stabilization and probing of collagenous triple helices
    • Koide, T., Yuguchi, M., Kawakita, M., and Kono H. (2002) Metal assisted stabilization and probing of collagenous triple helices, J. Am. Chem. Soc. 124, 9388-9389.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9388-9389
    • Koide, T.1    Yuguchi, M.2    Kawakita, M.3    Kono, H.4
  • 27
    • 4444290999 scopus 로고    scopus 로고
    • Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability
    • Minod, D., Lauer-Fields, J. L., Nagase, H., and Fields, G. B. (2004) Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability. Biochemistry 43, 11474-11481.
    • (2004) Biochemistry , vol.43 , pp. 11474-11481
    • Minod, D.1    Lauer-Fields, J.L.2    Nagase, H.3    Fields, G.B.4
  • 29
    • 0036660865 scopus 로고    scopus 로고
    • Triple helical peptide analysis of collagenolytic protease activity
    • Lauer-Fields, J. L., and Fields, G. B. (2002) Triple helical peptide analysis of collagenolytic protease activity. Biol. Chem. 383, 1095-1105.
    • (2002) Biol. Chem , vol.383 , pp. 1095-1105
    • Lauer-Fields, J.L.1    Fields, G.B.2
  • 30
    • 0036303549 scopus 로고    scopus 로고
    • Structural properties of collagenenous heterotrimer that mimics the collagenase cleavage site of collagen type I
    • Fiori, S., Sacca, B., and Moroder, L. (2002) Structural properties of collagenenous heterotrimer that mimics the collagenase cleavage site of collagen type I. J. Biol. Chem. 319, 1235-1242.
    • (2002) J. Biol. Chem , vol.319 , pp. 1235-1242
    • Fiori, S.1    Sacca, B.2    Moroder, L.3
  • 31
    • 33947655361 scopus 로고    scopus 로고
    • Differentiation of secreted and membrane-type metrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences
    • Minond, D., Lauer-Fields, J. L., Cudic, M., Overall, C. M., Pei, D., Brew, K., Moss, M. L., and Fields, G. B. (2007) Differentiation of secreted and membrane-type metrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences. Biochemistry 46, 3724-3733.
    • (2007) Biochemistry , vol.46 , pp. 3724-3733
    • Minond, D.1    Lauer-Fields, J.L.2    Cudic, M.3    Overall, C.M.4    Pei, D.5    Brew, K.6    Moss, M.L.7    Fields, G.B.8
  • 33
    • 0036712127 scopus 로고    scopus 로고
    • Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles
    • Pokorny, A., Birkbeck, T. H., and Almeida, P. F. F. (2002) Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles. Biochemistry 41, 11044-11056.
    • (2002) Biochemistry , vol.41 , pp. 11044-11056
    • Pokorny, A.1    Birkbeck, T.H.2    Almeida, P.F.F.3
  • 34
    • 12944281484 scopus 로고    scopus 로고
    • On the stability of polyproline-I and II structures of proline oligopeptides
    • Kakinoki, S., Hirano, Y., and Oka, M. (2005) On the stability of polyproline-I and II structures of proline oligopeptides. Polym. Bull. 53, 109-115.
    • (2005) Polym. Bull , vol.53 , pp. 109-115
    • Kakinoki, S.1    Hirano, Y.2    Oka, M.3
  • 35
    • 13444253811 scopus 로고    scopus 로고
    • Direct visualization of lipid phase segregation in single lipid bilayers with coherent anti-stokes Raman scattering microscopy
    • Potma, E. O., and Xie, X. S. (2005) Direct visualization of lipid phase segregation in single lipid bilayers with coherent anti-stokes Raman scattering microscopy. ChemPhysChem 6, 77-79.
    • (2005) ChemPhysChem , vol.6 , pp. 77-79
    • Potma, E.O.1    Xie, X.S.2


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