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Volumn 61, Issue 3, 2007, Pages 195-207

Mechanisms of heparin induced anti-cancer activity in experimental cancer models

Author keywords

Animal model; Anticoagulant activity; Cancer; Haematogenous metastases; Heparins; Low molecular weight heparin

Indexed keywords

HEPARANASE; HEPARIN; HEPARIN DERIVATIVE; LOW MOLECULAR WEIGHT HEPARIN; PROTEOHEPARAN SULFATE; SELECTIN; TINZAPARIN;

EID: 33847291915     PISSN: 10408428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.critrevonc.2006.07.007     Document Type: Review
Times cited : (181)

References (112)
  • 1
    • 0026569416 scopus 로고
    • Comparison of subcutaneous low-molecular-weight heparin with intravenous standard heparin in proximal deep-vein thrombosis
    • Prandoni P., Lensing A.W., Buller H.R., et al. Comparison of subcutaneous low-molecular-weight heparin with intravenous standard heparin in proximal deep-vein thrombosis. Lancet 339 (1992) 441-445
    • (1992) Lancet , vol.339 , pp. 441-445
    • Prandoni, P.1    Lensing, A.W.2    Buller, H.R.3
  • 2
    • 0032699382 scopus 로고    scopus 로고
    • Do heparins do more than just treat thrombosis? The influence of heparins on cancer spread
    • Hettiarachchi R.J., Smorenburg S.M., Ginsberg J., et al. Do heparins do more than just treat thrombosis? The influence of heparins on cancer spread. Thromb. Haemost. 82 (1999) 947-952
    • (1999) Thromb. Haemost. , vol.82 , pp. 947-952
    • Hettiarachchi, R.J.1    Smorenburg, S.M.2    Ginsberg, J.3
  • 3
    • 0033827861 scopus 로고    scopus 로고
    • Antithrombotic therapy in gynecologic surgery and gynecologic oncology
    • ix.
    • Von Tempelhoff G.F., and Heilmann L. Antithrombotic therapy in gynecologic surgery and gynecologic oncology. Hematol. Oncol. Clin. North Am. 14 (2000) 1151-1169 ix.
    • (2000) Hematol. Oncol. Clin. North Am. , vol.14 , pp. 1151-1169
    • Von Tempelhoff, G.F.1    Heilmann, L.2
  • 4
    • 0037775584 scopus 로고    scopus 로고
    • Low-molecular-weight heparin versus a coumarin for the prevention of recurrent venous thromboembolism in patients with cancer
    • Lee A.Y., Levine M.N., Baker R.I., et al. Low-molecular-weight heparin versus a coumarin for the prevention of recurrent venous thromboembolism in patients with cancer. N. Engl. J. Med. 349 (2003) 146-153
    • (2003) N. Engl. J. Med. , vol.349 , pp. 146-153
    • Lee, A.Y.1    Levine, M.N.2    Baker, R.I.3
  • 5
    • 17144385138 scopus 로고    scopus 로고
    • Randomized comparison of low molecular weight heparin and coumarin derivatives on the survival of patients with cancer and venous thromboembolism
    • Lee A.Y., Rickles F.R., Julian J.A., et al. Randomized comparison of low molecular weight heparin and coumarin derivatives on the survival of patients with cancer and venous thromboembolism. J. Clin. Oncol. 23 (2005) 2123-2129
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2123-2129
    • Lee, A.Y.1    Rickles, F.R.2    Julian, J.A.3
  • 6
    • 20244376337 scopus 로고    scopus 로고
    • The effect of low molecular weight heparin on survival in patients with advanced malignancy
    • Klerk C.P., Smorenburg S.M., Otten H.M., et al. The effect of low molecular weight heparin on survival in patients with advanced malignancy. J. Clin. Oncol. 23 10 (2005) 2130-2135
    • (2005) J. Clin. Oncol. , vol.23 , Issue.10 , pp. 2130-2135
    • Klerk, C.P.1    Smorenburg, S.M.2    Otten, H.M.3
  • 7
    • 3042704507 scopus 로고    scopus 로고
    • Low molecular weight heparin, therapy with dalteparin, and survival in advanced cancer: the fragmin advanced malignancy outcome study (FAMOUS)
    • Kakkar A.K., Levine M.N., Kadziola Z., et al. Low molecular weight heparin, therapy with dalteparin, and survival in advanced cancer: the fragmin advanced malignancy outcome study (FAMOUS). J. Clin. Oncol. 22 (2004) 1944-1948
    • (2004) J. Clin. Oncol. , vol.22 , pp. 1944-1948
    • Kakkar, A.K.1    Levine, M.N.2    Kadziola, Z.3
  • 8
    • 0028239146 scopus 로고
    • Subcutaneous heparin treatment increases survival in small cell lung cancer
    • "Petites Cellules" Group
    • Lebeau B., Chastang C., Brechot J.M., et al., "Petites Cellules" Group. Subcutaneous heparin treatment increases survival in small cell lung cancer. Cancer 74 (1994) 38-45
    • (1994) Cancer , vol.74 , pp. 38-45
    • Lebeau, B.1    Chastang, C.2    Brechot, J.M.3
  • 9
    • 12844289104 scopus 로고    scopus 로고
    • A randomized clinical trial of combination chemotherapy with and without low-molecular-weight heparin in small cell lung cancer
    • Altinbas M., Coskun H.S., Er O., et al. A randomized clinical trial of combination chemotherapy with and without low-molecular-weight heparin in small cell lung cancer. J. Thromb. Haemost. 2 (2004) 1266-1271
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 1266-1271
    • Altinbas, M.1    Coskun, H.S.2    Er, O.3
  • 10
    • 1642322919 scopus 로고    scopus 로고
    • Biochemical and pharmacologic heterogeneity in low molecular weight heparins. Impact on the therapeutic profile
    • Fareed J., Hoppensteadt D., Schultz C., et al. Biochemical and pharmacologic heterogeneity in low molecular weight heparins. Impact on the therapeutic profile. Curr. Pharm. Des. 10 (2004) 983-999
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 983-999
    • Fareed, J.1    Hoppensteadt, D.2    Schultz, C.3
  • 11
    • 0026025457 scopus 로고
    • Role of antithrombin III as a regulator of in vivo coagulation
    • Bauer K.A., and Rosenberg R.D. Role of antithrombin III as a regulator of in vivo coagulation. Semin. Hematol. 28 (1991) 10-18
    • (1991) Semin. Hematol. , vol.28 , pp. 10-18
    • Bauer, K.A.1    Rosenberg, R.D.2
  • 12
    • 0025204512 scopus 로고
    • Pharmacology of low molecular weight heparins
    • Harenberg J. Pharmacology of low molecular weight heparins. Semin. Thromb. Hemost. 16 Suppl. (1990) 12-18
    • (1990) Semin. Thromb. Hemost. , vol.16 , Issue.SUPPL , pp. 12-18
    • Harenberg, J.1
  • 14
    • 0022977122 scopus 로고
    • Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa
    • Danielsson A., Raub E., Lindahl U., and Bjork I. Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. J. Biol. Chem. 261 (1986) 15467-15473
    • (1986) J. Biol. Chem. , vol.261 , pp. 15467-15473
    • Danielsson, A.1    Raub, E.2    Lindahl, U.3    Bjork, I.4
  • 15
    • 0023948862 scopus 로고
    • Pharmacokinetic studies of standard unfractionated heparin, and low molecular weight heparins in the rabbit
    • Boneu B., Caranobe C., Cadroy Y., et al. Pharmacokinetic studies of standard unfractionated heparin, and low molecular weight heparins in the rabbit. Semin. Thromb. Hemost. 14 (1988) 18-27
    • (1988) Semin. Thromb. Hemost. , vol.14 , pp. 18-27
    • Boneu, B.1    Caranobe, C.2    Cadroy, Y.3
  • 16
    • 0035125405 scopus 로고    scopus 로고
    • Heparin and low-molecular-weight heparin: mechanisms of action, pharmacokinetics, dosing, monitoring, efficacy, and safety
    • Hirsh J., Warkentin T.E., Shaughnessy S.G., et al. Heparin and low-molecular-weight heparin: mechanisms of action, pharmacokinetics, dosing, monitoring, efficacy, and safety. Chest 119 (2001) 64S-94S
    • (2001) Chest , vol.119
    • Hirsh, J.1    Warkentin, T.E.2    Shaughnessy, S.G.3
  • 17
    • 0016108318 scopus 로고
    • Alkaline and smith degradation of oxidized dermatan sulphate-chondroitin sulphate copolymers
    • Fransson L.A., and Carlstedt I. Alkaline and smith degradation of oxidized dermatan sulphate-chondroitin sulphate copolymers. Carbohydr. Res. 36 (1974) 349-358
    • (1974) Carbohydr. Res. , vol.36 , pp. 349-358
    • Fransson, L.A.1    Carlstedt, I.2
  • 18
    • 0026661607 scopus 로고
    • Structural analysis of periodate-oxidized heparin
    • Conrad H.E., and Guo Y. Structural analysis of periodate-oxidized heparin. Adv. Exp. Med. Biol. 313 (1992) 31-36
    • (1992) Adv. Exp. Med. Biol. , vol.313 , pp. 31-36
    • Conrad, H.E.1    Guo, Y.2
  • 19
    • 0022921889 scopus 로고
    • Chemically modified heparins as inhibitors of heparan sulfate specific endo-beta-glucuronidase (heparanase) of metastatic melanoma cells
    • Irimura T., Nakajima M., and Nicolson G.L. Chemically modified heparins as inhibitors of heparan sulfate specific endo-beta-glucuronidase (heparanase) of metastatic melanoma cells. Biochemistry 25 (1986) 5322-5328
    • (1986) Biochemistry , vol.25 , pp. 5322-5328
    • Irimura, T.1    Nakajima, M.2    Nicolson, G.L.3
  • 20
    • 0028675219 scopus 로고
    • Inhibition of tumor metastasis by heparanase inhibiting species of heparin
    • Vlodavsky I., Mohsen M., Lider O., et al. Inhibition of tumor metastasis by heparanase inhibiting species of heparin. Invasion Metastasis 14 (1994) 290-302
    • (1994) Invasion Metastasis , vol.14 , pp. 290-302
    • Vlodavsky, I.1    Mohsen, M.2    Lider, O.3
  • 21
    • 1842557429 scopus 로고    scopus 로고
    • Inhibition of experimental lung metastases of Lewis lung carcinoma cells by chemically modified heparin with reduced anticoagulant activity
    • Yoshitomi Y., Nakanishi H., Kusano Y., et al. Inhibition of experimental lung metastases of Lewis lung carcinoma cells by chemically modified heparin with reduced anticoagulant activity. Cancer Lett. 207 (2004) 165-174
    • (2004) Cancer Lett. , vol.207 , pp. 165-174
    • Yoshitomi, Y.1    Nakanishi, H.2    Kusano, Y.3
  • 22
    • 0030428370 scopus 로고    scopus 로고
    • Treatment with modified heparins inhibits experimental metastasis formation and leads, in some animals, to long-term survival
    • Sciumbata T., Caretto P., Pirovano P., et al. Treatment with modified heparins inhibits experimental metastasis formation and leads, in some animals, to long-term survival. Invasion Metastasis 16 (1996) 132-143
    • (1996) Invasion Metastasis , vol.16 , pp. 132-143
    • Sciumbata, T.1    Caretto, P.2    Pirovano, P.3
  • 23
    • 0036687269 scopus 로고    scopus 로고
    • Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide
    • Poggi A., Rossi C., Casella N., et al. Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide. Semin. Thromb. Hemost. 28 (2002) 383-392
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 383-392
    • Poggi, A.1    Rossi, C.2    Casella, N.3
  • 24
    • 0017101062 scopus 로고
    • Effect of aprotinin, EACA and heparin on growth and vasopeptide system of Murphy-Sturm lymphosarcoma
    • Back N., and Steger R. Effect of aprotinin, EACA and heparin on growth and vasopeptide system of Murphy-Sturm lymphosarcoma. Eur. J. Pharmacol. 38 (1976) 313-319
    • (1976) Eur. J. Pharmacol. , vol.38 , pp. 313-319
    • Back, N.1    Steger, R.2
  • 25
    • 0027227523 scopus 로고
    • Effects of serine protease inhibitor FOY-305 and heparin on the growth of squamous cell carcinoma
    • Ohkoshi M., Akagawa T., and Nakajima M. Effects of serine protease inhibitor FOY-305 and heparin on the growth of squamous cell carcinoma. Anticancer Res. 13 (1993) 963-966
    • (1993) Anticancer Res. , vol.13 , pp. 963-966
    • Ohkoshi, M.1    Akagawa, T.2    Nakajima, M.3
  • 26
    • 0019975921 scopus 로고
    • Anticoagulant treatment of rats with Walker 256 carcinosarcoma
    • Owen Jr. C.A. Anticoagulant treatment of rats with Walker 256 carcinosarcoma. J. Cancer Res. Clin. Oncol. 104 (1982) 191-193
    • (1982) J. Cancer Res. Clin. Oncol. , vol.104 , pp. 191-193
    • Owen Jr., C.A.1
  • 27
    • 0018849669 scopus 로고
    • Metastasis-enhancing effect of heparin and its relationship to a lipoprotein factor
    • Chan S.Y., and Pollard M. Metastasis-enhancing effect of heparin and its relationship to a lipoprotein factor. J. Natl. Cancer Inst. 64 (1980) 1121-1125
    • (1980) J. Natl. Cancer Inst. , vol.64 , pp. 1121-1125
    • Chan, S.Y.1    Pollard, M.2
  • 28
    • 0030001467 scopus 로고    scopus 로고
    • Chemical modifications of heparin that diminish its anticoagulant but preserve its heparanase-inhibitory, angiostatic, anti-tumor and anti-metastatic properties
    • Lapierre F., Holme K., Lam L., et al. Chemical modifications of heparin that diminish its anticoagulant but preserve its heparanase-inhibitory, angiostatic, anti-tumor and anti-metastatic properties. Glycobiology 6 (1996) 355-366
    • (1996) Glycobiology , vol.6 , pp. 355-366
    • Lapierre, F.1    Holme, K.2    Lam, L.3
  • 29
    • 18444403123 scopus 로고    scopus 로고
    • Periodate-treated, non-anticoagulant heparin-carrying polystyrene (NAC-HCPS) affects angiogenesis and inhibits subcutaneous induced tumour growth and metastasis to the lung
    • Ono K., Ishihara M., Ishikawa K., et al. Periodate-treated, non-anticoagulant heparin-carrying polystyrene (NAC-HCPS) affects angiogenesis and inhibits subcutaneous induced tumour growth and metastasis to the lung. Br. J. Cancer 86 (2002) 1803-1812
    • (2002) Br. J. Cancer , vol.86 , pp. 1803-1812
    • Ono, K.1    Ishihara, M.2    Ishikawa, K.3
  • 30
    • 0005899035 scopus 로고
    • The effect of heparin on primary tumors and metastases
    • Retik A.B., Arons M.S., Ketcham A.S., and Mantel N. The effect of heparin on primary tumors and metastases. JSR II (1962) 49-53
    • (1962) JSR , vol.II , pp. 49-53
    • Retik, A.B.1    Arons, M.S.2    Ketcham, A.S.3    Mantel, N.4
  • 31
    • 0014385938 scopus 로고
    • Effect of heparin, epsilon-aminocaproic acid and coumarin on tumour growth and spontaneous metastasis formation
    • Hagmar B. Effect of heparin, epsilon-aminocaproic acid and coumarin on tumour growth and spontaneous metastasis formation. Pathol. Eur. 3 (1968) 622-630
    • (1968) Pathol. Eur. , vol.3 , pp. 622-630
    • Hagmar, B.1
  • 32
    • 0014721357 scopus 로고
    • Tumour growth and spontaneous metastasis spread in two syngeneic systems
    • Hagmar B. Tumour growth and spontaneous metastasis spread in two syngeneic systems. Acta Pathol. Microbiol. Scand. [A] 78 (1970) 131-142
    • (1970) Acta Pathol. Microbiol. Scand. [A] , vol.78 , pp. 131-142
    • Hagmar, B.1
  • 33
    • 0021139107 scopus 로고
    • The evaluation of heparin in control of metastasis of Nb rat androgen-insensitive prostate carcinoma
    • Drago J.R., Weed P., and Fralisch A. The evaluation of heparin in control of metastasis of Nb rat androgen-insensitive prostate carcinoma. Anticancer Res. 4 (1984) 171-172
    • (1984) Anticancer Res. , vol.4 , pp. 171-172
    • Drago, J.R.1    Weed, P.2    Fralisch, A.3
  • 34
    • 0021827261 scopus 로고
    • Metastasis in the androgen-insensitive Nb rat prostatic carcinoma system
    • Drago J.R., and Lombard J.S. Metastasis in the androgen-insensitive Nb rat prostatic carcinoma system. J. Surg. Oncol. 28 (1985) 252-256
    • (1985) J. Surg. Oncol. , vol.28 , pp. 252-256
    • Drago, J.R.1    Lombard, J.S.2
  • 35
    • 0022368463 scopus 로고
    • Treatment with cortisone plus heparin or hexuronyl hexoaminoglycan sulfates of murine tumors and their lung deposits
    • Milas L., Hunter N., and Basic I. Treatment with cortisone plus heparin or hexuronyl hexoaminoglycan sulfates of murine tumors and their lung deposits. Clin. Exp. Metastasis 3 (1985) 247-255
    • (1985) Clin. Exp. Metastasis , vol.3 , pp. 247-255
    • Milas, L.1    Hunter, N.2    Basic, I.3
  • 36
    • 0025259784 scopus 로고
    • Reduction of metastasis in a murine mammary tumour model by heparin and polyinosinic-polycytidylic acid
    • Lee A.E., Rogers L.A., Longcroft J.M., and Jeffery R.E. Reduction of metastasis in a murine mammary tumour model by heparin and polyinosinic-polycytidylic acid. Clin. Exp. Metastasis 8 (1990) 165-171
    • (1990) Clin. Exp. Metastasis , vol.8 , pp. 165-171
    • Lee, A.E.1    Rogers, L.A.2    Longcroft, J.M.3    Jeffery, R.E.4
  • 37
    • 0029965540 scopus 로고    scopus 로고
    • Low-dose heparin treatment does not inhibit SW480 human colon cancer growth and metastasis in vivo
    • Antachopoulos C.T., Gagos S., Iliopoulos D.C., et al. Low-dose heparin treatment does not inhibit SW480 human colon cancer growth and metastasis in vivo. In Vivo 10 (1996) 527-531
    • (1996) In Vivo , vol.10 , pp. 527-531
    • Antachopoulos, C.T.1    Gagos, S.2    Iliopoulos, D.C.3
  • 38
    • 0033391856 scopus 로고    scopus 로고
    • In vivo treatment of rats with unfractionated heparin (UFH) or low molecular weight heparin (LMWH) does not affect experimentally induced colon carcinoma metastasis
    • Smorenburg S.M., Vink R., te Lintelo M., et al. In vivo treatment of rats with unfractionated heparin (UFH) or low molecular weight heparin (LMWH) does not affect experimentally induced colon carcinoma metastasis. Clin. Exp. Metastasis 17 (1999) 451-456
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 451-456
    • Smorenburg, S.M.1    Vink, R.2    te Lintelo, M.3
  • 39
    • 11444257143 scopus 로고    scopus 로고
    • Anticoagulant drugs increase natural killer cell activity in lung cancer
    • Bobek V., Boubelik M., Fiserova A., et al. Anticoagulant drugs increase natural killer cell activity in lung cancer. Lung Cancer 47 (2005) 215-223
    • (2005) Lung Cancer , vol.47 , pp. 215-223
    • Bobek, V.1    Boubelik, M.2    Fiserova, A.3
  • 40
    • 0027234042 scopus 로고
    • Inhibition of peritoneal tumor-cell implantation: model for laparoscopic cancer surgery
    • Goldstein D.S., Lu M.L., Hattori T., et al. Inhibition of peritoneal tumor-cell implantation: model for laparoscopic cancer surgery. J. Endourol. 7 (1993) 237-241
    • (1993) J. Endourol. , vol.7 , pp. 237-241
    • Goldstein, D.S.1    Lu, M.L.2    Hattori, T.3
  • 41
    • 0030770536 scopus 로고    scopus 로고
    • Inhibition of peritoneal tumor cell growth and implantation in laparoscopic surgery in a rat model
    • Jacobi C.A., Ordemann J., Bohm B., et al. Inhibition of peritoneal tumor cell growth and implantation in laparoscopic surgery in a rat model. Am. J. Surg. 174 (1997) 359-363
    • (1997) Am. J. Surg. , vol.174 , pp. 359-363
    • Jacobi, C.A.1    Ordemann, J.2    Bohm, B.3
  • 42
    • 0032751144 scopus 로고    scopus 로고
    • New therapeutic strategies to avoid intra- and extraperitoneal metastases during laparoscopy: results of a tumor model in the rat
    • Jacobi C.A., Peter F.J., Wenger F.A., Ordemann J., and Muller J.M. New therapeutic strategies to avoid intra- and extraperitoneal metastases during laparoscopy: results of a tumor model in the rat. Dig. Surg. 16 (1999) 393-399
    • (1999) Dig. Surg. , vol.16 , pp. 393-399
    • Jacobi, C.A.1    Peter, F.J.2    Wenger, F.A.3    Ordemann, J.4    Muller, J.M.5
  • 43
    • 0033009361 scopus 로고    scopus 로고
    • Experimental study of the effect of intraperitoneal heparin on tumour implantation following laparoscopy
    • Neuhaus S.J., Ellis T., Jamieson G.G., and Watson D.I. Experimental study of the effect of intraperitoneal heparin on tumour implantation following laparoscopy. Br. J. Surg. 86 (1999) 400-404
    • (1999) Br. J. Surg. , vol.86 , pp. 400-404
    • Neuhaus, S.J.1    Ellis, T.2    Jamieson, G.G.3    Watson, D.I.4
  • 44
    • 0032706441 scopus 로고    scopus 로고
    • Topical treatments of laparoscopic port sites can decrease the incidence of incision metastasis
    • Eshraghi N., Swanstrom L.L., Bax T., et al. Topical treatments of laparoscopic port sites can decrease the incidence of incision metastasis. Surg. Endosc. 13 (1999) 1121-1124
    • (1999) Surg. Endosc. , vol.13 , pp. 1121-1124
    • Eshraghi, N.1    Swanstrom, L.L.2    Bax, T.3
  • 45
    • 0242380339 scopus 로고    scopus 로고
    • Low-molecular-weight heparin (reviparin) diminishes tumor cell adhesion and invasion in vitro, and decreases intraperitoneal growth of colonadeno-carcinoma cells in rats after laparoscopy
    • Pross M., Lippert H., Misselwitz F., et al. Low-molecular-weight heparin (reviparin) diminishes tumor cell adhesion and invasion in vitro, and decreases intraperitoneal growth of colonadeno-carcinoma cells in rats after laparoscopy. Thromb. Res. 110 (2003) 215-220
    • (2003) Thromb. Res. , vol.110 , pp. 215-220
    • Pross, M.1    Lippert, H.2    Misselwitz, F.3
  • 46
    • 1242285585 scopus 로고    scopus 로고
    • Effect of low molecular weight heparin on intra-abdominal metastasis in a laparoscopic experimental study
    • Pross M., Lippert H., Nestler G., et al. Effect of low molecular weight heparin on intra-abdominal metastasis in a laparoscopic experimental study. Int. J. Colorectal Dis. 19 (2004) 143-146
    • (2004) Int. J. Colorectal Dis. , vol.19 , pp. 143-146
    • Pross, M.1    Lippert, H.2    Nestler, G.3
  • 47
    • 1842463681 scopus 로고    scopus 로고
    • Antimetastatic effect of tinzaparin, a low-molecular-weight heparin
    • Amirkhosravi A., Mousa S.A., Amaya M., and Francis J.L. Antimetastatic effect of tinzaparin, a low-molecular-weight heparin. J. Thromb. Haemost. 1 (2003) 1972-1976
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1972-1976
    • Amirkhosravi, A.1    Mousa, S.A.2    Amaya, M.3    Francis, J.L.4
  • 48
    • 0025631658 scopus 로고
    • Treatment of experimental liver metastases in the rat by continuous intraportal infusion of 5-fluorouracil and heparin: a pilot study
    • Nagawa H., Paris P., Chauffert B., and Martin F. Treatment of experimental liver metastases in the rat by continuous intraportal infusion of 5-fluorouracil and heparin: a pilot study. Anticancer Drugs 1 (1990) 149-156
    • (1990) Anticancer Drugs , vol.1 , pp. 149-156
    • Nagawa, H.1    Paris, P.2    Chauffert, B.3    Martin, F.4
  • 49
    • 0041765051 scopus 로고    scopus 로고
    • Visualization of early events in tumor formation of eGFP-transfected rat colon cancer cells in liver
    • Mook O.R., Van Marle J., Vreeling-Sindelarova H., et al. Visualization of early events in tumor formation of eGFP-transfected rat colon cancer cells in liver. Hepatology 38 (2003) 295-304
    • (2003) Hepatology , vol.38 , pp. 295-304
    • Mook, O.R.1    Van Marle, J.2    Vreeling-Sindelarova, H.3
  • 50
    • 0023176857 scopus 로고
    • Combined immunostimulation (Propionibacterium avidum KP 40) and anticoagulation (heparin) prevents metastatic lung and liver colonization in mice
    • Beuth J., Ko H.L., Uhlenbruck G., and Pulverer G. Combined immunostimulation (Propionibacterium avidum KP 40) and anticoagulation (heparin) prevents metastatic lung and liver colonization in mice. J. Cancer Res. Clin. Oncol. 113 (1987) 359-362
    • (1987) J. Cancer Res. Clin. Oncol. , vol.113 , pp. 359-362
    • Beuth, J.1    Ko, H.L.2    Uhlenbruck, G.3    Pulverer, G.4
  • 51
    • 0023795478 scopus 로고
    • Comparison of metastatic cell lines derived from a murine mammary tumour, and reduction of metastasis by heparin
    • Lee A.E., Rogers L.A., Jeffery R.E., and Longcroft J.M. Comparison of metastatic cell lines derived from a murine mammary tumour, and reduction of metastasis by heparin. Clin. Exp. Metastasis 6 (1988) 463-471
    • (1988) Clin. Exp. Metastasis , vol.6 , pp. 463-471
    • Lee, A.E.1    Rogers, L.A.2    Jeffery, R.E.3    Longcroft, J.M.4
  • 52
    • 0032879625 scopus 로고    scopus 로고
    • Inhibition of heparanase activity and tumor metastasis by laminarin sulfate and synthetic phosphorothioate oligodeoxynucleotides
    • Miao H.Q., Elkin M., Aingorn E., et al. Inhibition of heparanase activity and tumor metastasis by laminarin sulfate and synthetic phosphorothioate oligodeoxynucleotides. Int. J. Cancer 83 (1999) 424-431
    • (1999) Int. J. Cancer , vol.83 , pp. 424-431
    • Miao, H.Q.1    Elkin, M.2    Aingorn, E.3
  • 53
    • 0035853111 scopus 로고    scopus 로고
    • Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis
    • Borsig L., Wong R., Feramisco J., et al. Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 3352-3357
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3352-3357
    • Borsig, L.1    Wong, R.2    Feramisco, J.3
  • 54
    • 0036687269 scopus 로고    scopus 로고
    • Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide
    • Poggi A., Rossi C., Casella N., et al. Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide. Semin. Thromb. Hemost. 28 (2002) 383-392
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 383-392
    • Poggi, A.1    Rossi, C.2    Casella, N.3
  • 55
    • 26444566779 scopus 로고    scopus 로고
    • Differential metastasis inhibition by clinically relevant levels of heparins-correlation with selectin inhibition, not antithrombotic activity
    • Stevenson J.L., Choi S.H., and Varki A. Differential metastasis inhibition by clinically relevant levels of heparins-correlation with selectin inhibition, not antithrombotic activity. Clin. Cancer Res. 11 (2005) 7003-7011
    • (2005) Clin. Cancer Res. , vol.11 , pp. 7003-7011
    • Stevenson, J.L.1    Choi, S.H.2    Varki, A.3
  • 56
    • 23944442968 scopus 로고    scopus 로고
    • Selective antimetastatic effect of heparins in preclinical human melanoma models is based on inhibition of migration and microvascular arrest
    • Bereczky B., Gilly R., Raso E., et al. Selective antimetastatic effect of heparins in preclinical human melanoma models is based on inhibition of migration and microvascular arrest. Clin. Exp. Metastasis 22 (2005) 69-76
    • (2005) Clin. Exp. Metastasis , vol.22 , pp. 69-76
    • Bereczky, B.1    Gilly, R.2    Raso, E.3
  • 57
    • 9244265563 scopus 로고    scopus 로고
    • Coagulation facilitates tumor cell spreading in the pulmonary vasculature during early metastatic colony formation
    • Im J.H., Fu W., Wang H., et al. Coagulation facilitates tumor cell spreading in the pulmonary vasculature during early metastatic colony formation. Cancer Res. 64 (2004) 8613-8619
    • (2004) Cancer Res. , vol.64 , pp. 8613-8619
    • Im, J.H.1    Fu, W.2    Wang, H.3
  • 58
    • 8644287603 scopus 로고    scopus 로고
    • Downregulation of tissue factor by RNA interference in human melanoma LOX-L cells reduces pulmonary metastasis in nude mice
    • Wang X., Wang M., Amarzguioui M., et al. Downregulation of tissue factor by RNA interference in human melanoma LOX-L cells reduces pulmonary metastasis in nude mice. Int. J. Cancer 112 (2004) 994-1002
    • (2004) Int. J. Cancer , vol.112 , pp. 994-1002
    • Wang, X.1    Wang, M.2    Amarzguioui, M.3
  • 59
    • 10844222440 scopus 로고    scopus 로고
    • Platelet-cancer interactions: mechanisms and pharmacology of tumour cell-induced platelet aggregation
    • Jurasz P., Alonso-Escolano D., and Radomski M.W. Platelet-cancer interactions: mechanisms and pharmacology of tumour cell-induced platelet aggregation. Br. J. Pharmacol. 143 (2004) 819-826
    • (2004) Br. J. Pharmacol. , vol.143 , pp. 819-826
    • Jurasz, P.1    Alonso-Escolano, D.2    Radomski, M.W.3
  • 61
    • 3142592165 scopus 로고    scopus 로고
    • Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis
    • Camerer E., Qazi A.A., Duong D.N., et al. Platelets, protease-activated receptors, and fibrinogen in hematogenous metastasis. Blood 104 (2004) 397-401
    • (2004) Blood , vol.104 , pp. 397-401
    • Camerer, E.1    Qazi, A.A.2    Duong, D.N.3
  • 62
    • 0023946733 scopus 로고
    • Role of adhesive proteins in platelet tumor interaction in vitro and metastasis formation in vivo
    • Karpatkin S., Pearlstein E., Ambrogio C., and Coller B.S. Role of adhesive proteins in platelet tumor interaction in vitro and metastasis formation in vivo. J. Clin. Invest. 81 (1988) 1012-1019
    • (1988) J. Clin. Invest. , vol.81 , pp. 1012-1019
    • Karpatkin, S.1    Pearlstein, E.2    Ambrogio, C.3    Coller, B.S.4
  • 63
    • 0033646764 scopus 로고    scopus 로고
    • Potential future clinical applications for the GPIIb/IIIa antagonist, abciximab in thrombosis, vascular and oncological indications
    • Cohen S.A., Trikha M., and Mascelli M.A. Potential future clinical applications for the GPIIb/IIIa antagonist, abciximab in thrombosis, vascular and oncological indications. Pathol. Oncol. Res. 6 (2000) 163-174
    • (2000) Pathol. Oncol. Res. , vol.6 , pp. 163-174
    • Cohen, S.A.1    Trikha, M.2    Mascelli, M.A.3
  • 64
    • 0141651848 scopus 로고    scopus 로고
    • Inhibition of tumor cell-induced platelet aggregation and lung metastasis by the oral GpIIb/IIIa antagonist XV454
    • Amirkhosravi A., Mousa S.A., Amaya M., et al. Inhibition of tumor cell-induced platelet aggregation and lung metastasis by the oral GpIIb/IIIa antagonist XV454. Thromb. Haemost. 90 (2003) 549-554
    • (2003) Thromb. Haemost. , vol.90 , pp. 549-554
    • Amirkhosravi, A.1    Mousa, S.A.2    Amaya, M.3
  • 65
    • 20244379858 scopus 로고
    • Vascular permeability factor, fibrin, and the pathogenesis of tumor stroma formation
    • Dvorak H.F., Nagy J.A., Berse B., et al. Vascular permeability factor, fibrin, and the pathogenesis of tumor stroma formation. Ann. N. Y. Acad. Sci. 667 (1992) 101-111
    • (1992) Ann. N. Y. Acad. Sci. , vol.667 , pp. 101-111
    • Dvorak, H.F.1    Nagy, J.A.2    Berse, B.3
  • 67
    • 0034669975 scopus 로고    scopus 로고
    • Fibrinogen is an important determinant of the metastatic potential of circulating tumor cells
    • Palumbo J.S., Kombrinck K.W., Drew A.F., et al. Fibrinogen is an important determinant of the metastatic potential of circulating tumor cells. Blood 96 (2000) 3302-3309
    • (2000) Blood , vol.96 , pp. 3302-3309
    • Palumbo, J.S.1    Kombrinck, K.W.2    Drew, A.F.3
  • 68
    • 0028932993 scopus 로고
    • Tissue factor pathway inhibitor and the revised theory of coagulation
    • Broze Jr. G.J. Tissue factor pathway inhibitor and the revised theory of coagulation. Annu. Rev. Med. 46 (1995) 103-112
    • (1995) Annu. Rev. Med. , vol.46 , pp. 103-112
    • Broze Jr., G.J.1
  • 69
    • 0025719380 scopus 로고
    • Extrinsic pathway inhibitor-the key to feedback control of blood coagulation initiated by tissue thromboplastin
    • Sandset P.M., and Abildgaard U. Extrinsic pathway inhibitor-the key to feedback control of blood coagulation initiated by tissue thromboplastin. Haemostasis 21 (1991) 219-239
    • (1991) Haemostasis , vol.21 , pp. 219-239
    • Sandset, P.M.1    Abildgaard, U.2
  • 70
    • 4544370585 scopus 로고    scopus 로고
    • Inhibition of endothelial cell tube formation by the low molecular weight heparin, tinzaparin, is mediated by tissue factor pathway inhibitor
    • Mousa S.A., and Mohamed S. Inhibition of endothelial cell tube formation by the low molecular weight heparin, tinzaparin, is mediated by tissue factor pathway inhibitor. Thromb. Haemost. 92 (2004) 627-633
    • (2004) Thromb. Haemost. , vol.92 , pp. 627-633
    • Mousa, S.A.1    Mohamed, S.2
  • 71
    • 0036687269 scopus 로고    scopus 로고
    • Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide
    • Poggi A., Rossi C., Casella N., et al. Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide. Semin. Thromb. Hemost. 28 (2002) 383-392
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 383-392
    • Poggi, A.1    Rossi, C.2    Casella, N.3
  • 72
    • 0037567437 scopus 로고    scopus 로고
    • Tissue factor/factor VIIa inhibitors block angiogenesis and tumor growth through a nonhemostatic mechanism
    • Hembrough T.A., Swartz G.M., Papathanassiu A., et al. Tissue factor/factor VIIa inhibitors block angiogenesis and tumor growth through a nonhemostatic mechanism. Cancer Res. 63 (2003) 2997-3000
    • (2003) Cancer Res. , vol.63 , pp. 2997-3000
    • Hembrough, T.A.1    Swartz, G.M.2    Papathanassiu, A.3
  • 73
    • 0021118858 scopus 로고
    • Role of plasma, platelets, and endothelial cells in tumor metastasis
    • Gasic G.J. Role of plasma, platelets, and endothelial cells in tumor metastasis. Cancer Metastasis Rev. 3 (1984) 99-114
    • (1984) Cancer Metastasis Rev. , vol.3 , pp. 99-114
    • Gasic, G.J.1
  • 74
    • 0026494476 scopus 로고
    • Platelets and cancer metastasis: a causal relationship?
    • Honn K.V., Tang D.G., and Crissman J.D. Platelets and cancer metastasis: a causal relationship?. Cancer Metastasis Rev. 11 (1992) 325-351
    • (1992) Cancer Metastasis Rev. , vol.11 , pp. 325-351
    • Honn, K.V.1    Tang, D.G.2    Crissman, J.D.3
  • 75
    • 0033559946 scopus 로고    scopus 로고
    • Lysis of tumor cells by natural killer cells in mice is impeded by platelets
    • Nieswandt B., Hafner M., Echtenacher B., and Mannel D.N. Lysis of tumor cells by natural killer cells in mice is impeded by platelets. Cancer Res. 59 (1999) 1295-1300
    • (1999) Cancer Res. , vol.59 , pp. 1295-1300
    • Nieswandt, B.1    Hafner, M.2    Echtenacher, B.3    Mannel, D.N.4
  • 76
    • 0030999872 scopus 로고    scopus 로고
    • Role of endothelial selectins in wound repair
    • Subramaniam M., Saffaripour S., van de W.L., et al. Role of endothelial selectins in wound repair. Am. J. Pathol. 150 (1997) 1701-1709
    • (1997) Am. J. Pathol. , vol.150 , pp. 1701-1709
    • Subramaniam, M.1    Saffaripour, S.2    van de, W.L.3
  • 77
    • 0028538864 scopus 로고
    • Leukocyte-endothelial interactions and organ injury: the role of adhesion molecules
    • Talbott G.A., Sharar S.R., Harlan J.M., and Winn R.K. Leukocyte-endothelial interactions and organ injury: the role of adhesion molecules. New Horiz. 2 (1994) 545-554
    • (1994) New Horiz. , vol.2 , pp. 545-554
    • Talbott, G.A.1    Sharar, S.R.2    Harlan, J.M.3    Winn, R.K.4
  • 78
    • 0027106199 scopus 로고
    • The selectin family of carbohydrate-binding proteins: structure and importance of carbohydrate ligands for cell adhesion
    • Cummings R.D., and Smith D.F. The selectin family of carbohydrate-binding proteins: structure and importance of carbohydrate ligands for cell adhesion. Bioessays 14 (1992) 849-856
    • (1992) Bioessays , vol.14 , pp. 849-856
    • Cummings, R.D.1    Smith, D.F.2
  • 79
    • 0027248439 scopus 로고
    • Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells
    • Norgard-Sumnicht K.E., Varki N.M., and Varki A. Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells. Science 261 (1993) 480-483
    • (1993) Science , vol.261 , pp. 480-483
    • Norgard-Sumnicht, K.E.1    Varki, N.M.2    Varki, A.3
  • 80
    • 0032519957 scopus 로고    scopus 로고
    • Differential interactions of heparin and heparan sulfate glycosaminoglycans with the selectins. Implications for the use of unfractionated and low molecular weight heparins as therapeutic agents
    • Koenig A., Norgard-Sumnicht K., Linhardt R., and Varki A. Differential interactions of heparin and heparan sulfate glycosaminoglycans with the selectins. Implications for the use of unfractionated and low molecular weight heparins as therapeutic agents. J. Clin. Invest. 101 (1998) 877-889
    • (1998) J. Clin. Invest. , vol.101 , pp. 877-889
    • Koenig, A.1    Norgard-Sumnicht, K.2    Linhardt, R.3    Varki, A.4
  • 81
    • 0027484507 scopus 로고
    • Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation
    • Nelson R.M., Cecconi O., Roberts W.G., et al. Heparin oligosaccharides bind L- and P-selectin and inhibit acute inflammation. Blood 82 (1993) 3253-3258
    • (1993) Blood , vol.82 , pp. 3253-3258
    • Nelson, R.M.1    Cecconi, O.2    Roberts, W.G.3
  • 82
    • 0036189961 scopus 로고    scopus 로고
    • Heparin inhibition of selectin-mediated interactions during the hematogenous phase of carcinoma metastasis: rationale for clinical studies in humans
    • Varki N.M., and Varki A. Heparin inhibition of selectin-mediated interactions during the hematogenous phase of carcinoma metastasis: rationale for clinical studies in humans. Semin. Thromb. Hemost. 28 (2002) 53-66
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 53-66
    • Varki, N.M.1    Varki, A.2
  • 84
    • 0025013701 scopus 로고
    • Extracellular matrix-resident growth factors and enzymes: possible involvement in tumor metastasis and angiogenesis
    • Vlodavsky I., Korner G., Ishai-Michaeli R., et al. Extracellular matrix-resident growth factors and enzymes: possible involvement in tumor metastasis and angiogenesis. Cancer Metastasis Rev. 9 (1990) 203-226
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 203-226
    • Vlodavsky, I.1    Korner, G.2    Ishai-Michaeli, R.3
  • 85
    • 0035999158 scopus 로고    scopus 로고
    • Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development
    • Vlodavsky I., Goldshmidt O., Zcharia E., et al. Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development. Semin. Cancer Biol. 12 (2002) 121-129
    • (2002) Semin. Cancer Biol. , vol.12 , pp. 121-129
    • Vlodavsky, I.1    Goldshmidt, O.2    Zcharia, E.3
  • 86
    • 0036672885 scopus 로고    scopus 로고
    • Heparanase-1 expression is associated with the metastatic potential of breast cancer
    • Maxhimer J.B., Quiros R.M., Stewart R., et al. Heparanase-1 expression is associated with the metastatic potential of breast cancer. Surgery 132 (2002) 326-333
    • (2002) Surgery , vol.132 , pp. 326-333
    • Maxhimer, J.B.1    Quiros, R.M.2    Stewart, R.3
  • 87
    • 0033810052 scopus 로고    scopus 로고
    • Expression of heparanase in normal, dysplastic, and neoplastic human colonic mucosa and stroma. Evidence for its role in colonic tumorigenesis
    • Friedmann Y., Vlodavsky I., Aingorn H., et al. Expression of heparanase in normal, dysplastic, and neoplastic human colonic mucosa and stroma. Evidence for its role in colonic tumorigenesis. Am. J. Pathol. 157 (2000) 1167-1175
    • (2000) Am. J. Pathol. , vol.157 , pp. 1167-1175
    • Friedmann, Y.1    Vlodavsky, I.2    Aingorn, H.3
  • 88
    • 17644447902 scopus 로고    scopus 로고
    • Expression of heparanase, Mdm2, and erbB2 in ovarian cancer
    • Ginath S., Menczer J., Friedmann Y., et al. Expression of heparanase, Mdm2, and erbB2 in ovarian cancer. Int. J. Oncol. 18 (2001) 1133-1144
    • (2001) Int. J. Oncol. , vol.18 , pp. 1133-1144
    • Ginath, S.1    Menczer, J.2    Friedmann, Y.3
  • 89
    • 0035922067 scopus 로고    scopus 로고
    • Expression of three extracellular matrix degradative enzymes in bladder cancer
    • Gohji K., Hirano H., Okamoto M., et al. Expression of three extracellular matrix degradative enzymes in bladder cancer. Int. J. Cancer 95 (2001) 295-301
    • (2001) Int. J. Cancer , vol.95 , pp. 295-301
    • Gohji, K.1    Hirano, H.2    Okamoto, M.3
  • 90
    • 0035875082 scopus 로고    scopus 로고
    • Heparanase expression in primary and metastatic pancreatic cancer
    • Koliopanos A., Friess H., Kleeff J., et al. Heparanase expression in primary and metastatic pancreatic cancer. Cancer Res. 61 (2001) 4655-4659
    • (2001) Cancer Res. , vol.61 , pp. 4655-4659
    • Koliopanos, A.1    Friess, H.2    Kleeff, J.3
  • 91
    • 18244385274 scopus 로고    scopus 로고
    • Heparanase expression in human leukemias is restricted to acute myeloid leukemias
    • Bitan M., Polliack A., Zecchina G., et al. Heparanase expression in human leukemias is restricted to acute myeloid leukemias. Exp. Hematol. 30 (2002) 34-41
    • (2002) Exp. Hematol. , vol.30 , pp. 34-41
    • Bitan, M.1    Polliack, A.2    Zecchina, G.3
  • 92
    • 3042788473 scopus 로고    scopus 로고
    • Clinical significance of heparanase activity in primary resected non-small cell lung cancer
    • Takahashi H., Ebihara S., Okazaki T., et al. Clinical significance of heparanase activity in primary resected non-small cell lung cancer. Lung Cancer 45 (2004) 207-214
    • (2004) Lung Cancer , vol.45 , pp. 207-214
    • Takahashi, H.1    Ebihara, S.2    Okazaki, T.3
  • 93
    • 19944430539 scopus 로고    scopus 로고
    • Heparanase promotes the spontaneous metastasis of myeloma cells to bone
    • Yang Y., Macleod V., Bendre M., et al. Heparanase promotes the spontaneous metastasis of myeloma cells to bone. Blood 105 (2005) 1303-1309
    • (2005) Blood , vol.105 , pp. 1303-1309
    • Yang, Y.1    Macleod, V.2    Bendre, M.3
  • 94
    • 0025501812 scopus 로고
    • Heparanase activity expressed by platelets, neutrophils, and lymphoma cells releases active fibroblast growth factor from extracellular matrix
    • Ishai-Michaeli R., Eldor A., and Vlodavsky I. Heparanase activity expressed by platelets, neutrophils, and lymphoma cells releases active fibroblast growth factor from extracellular matrix. Cell Regul. 1 (1990) 833-842
    • (1990) Cell Regul. , vol.1 , pp. 833-842
    • Ishai-Michaeli, R.1    Eldor, A.2    Vlodavsky, I.3
  • 95
    • 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., and 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. 271 (1996) 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
  • 96
    • 7944230119 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans and heparanase-partners in osteolytic tumor growth and metastasis
    • Sanderson R.D., Yang Y., Suva L.J., and Kelly T. Heparan sulfate proteoglycans and heparanase-partners in osteolytic tumor growth and metastasis. Matrix Biol. 23 (2004) 341-352
    • (2004) Matrix Biol. , vol.23 , pp. 341-352
    • Sanderson, R.D.1    Yang, Y.2    Suva, L.J.3    Kelly, T.4
  • 97
    • 0035405778 scopus 로고    scopus 로고
    • Heparanase as mediator of angiogenesis: mode of action
    • Elkin M., Ilan N., Ishai-Michaeli R., et al. Heparanase as mediator of angiogenesis: mode of action. FASEB J. 15 (2001) 1661-1663
    • (2001) FASEB J. , vol.15 , pp. 1661-1663
    • Elkin, M.1    Ilan, N.2    Ishai-Michaeli, R.3
  • 98
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky I., and Friedmann Y. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J. Clin. Invest. 108 (2001) 341-347
    • (2001) J. Clin. Invest. , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 99
    • 0031749471 scopus 로고    scopus 로고
    • Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2
    • Kato M., Wang H., Kainulainen V., et al. Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. Nat. Med. 4 (1998) 691-697
    • (1998) Nat. Med. , vol.4 , pp. 691-697
    • Kato, M.1    Wang, H.2    Kainulainen, V.3
  • 100
    • 0023640553 scopus 로고
    • Evidence that sulphated polysaccharides inhibit tumour metastasis by blocking tumour-cell-derived heparanases
    • Parish C.R., Coombe D.R., Jakobsen K.B., Bennett F.A., and Underwood P.A. Evidence that sulphated polysaccharides inhibit tumour metastasis by blocking tumour-cell-derived heparanases. Int. J. Cancer 40 (1987) 511-518
    • (1987) Int. J. Cancer , vol.40 , pp. 511-518
    • Parish, C.R.1    Coombe, D.R.2    Jakobsen, K.B.3    Bennett, F.A.4    Underwood, P.A.5
  • 101
    • 0033057962 scopus 로고    scopus 로고
    • Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis
    • Vlodavsky I., Friedmann Y., Elkin M., et al. Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. Nat. Med. 5 (1999) 793-802
    • (1999) Nat. Med. , vol.5 , pp. 793-802
    • Vlodavsky, I.1    Friedmann, Y.2    Elkin, M.3
  • 102
    • 0036687269 scopus 로고    scopus 로고
    • Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide
    • Poggi A., Rossi C., Casella N., et al. Inhibition of B16-BL6 melanoma lung colonies by semisynthetic sulfaminoheparosan sulfates from E. coli K5 polysaccharide. Semin. Thromb. Hemost. 28 (2002) 383-392
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 383-392
    • Poggi, A.1    Rossi, C.2    Casella, N.3
  • 103
    • 0032923918 scopus 로고    scopus 로고
    • In vivo involvement of heparan sulfate proteoglycan in the bioavailability, internalization, and catabolism of exogenous basic fibroblast growth factor
    • Colin S., Jeanny J.C., Mascarelli F., et al. In vivo involvement of heparan sulfate proteoglycan in the bioavailability, internalization, and catabolism of exogenous basic fibroblast growth factor. Mol. Pharmacol. 55 (1999) 74-82
    • (1999) Mol. Pharmacol. , vol.55 , pp. 74-82
    • Colin, S.1    Jeanny, J.C.2    Mascarelli, F.3
  • 104
    • 0034326271 scopus 로고    scopus 로고
    • Unfractionated and low molecular weight heparin affect fibrin structure and angiogenesis in vitro
    • Collen A., Smorenburg S.M., Peters E., et al. Unfractionated and low molecular weight heparin affect fibrin structure and angiogenesis in vitro. Cancer Res. 60 (2000) 6196-6200
    • (2000) Cancer Res. , vol.60 , pp. 6196-6200
    • Collen, A.1    Smorenburg, S.M.2    Peters, E.3
  • 105
    • 0026842641 scopus 로고
    • Capillary growth: a two-cell system
    • D'Amore P.A. Capillary growth: a two-cell system. Semin. Cancer Biol. 3 (1992) 49-56
    • (1992) Semin. Cancer Biol. , vol.3 , pp. 49-56
    • D'Amore, P.A.1
  • 106
    • 0024593040 scopus 로고
    • Control of angiogenesis with synthetic heparin substitutes
    • Folkman J., Weisz P.B., Joullie M.M., Li W.W., and Ewing W.R. Control of angiogenesis with synthetic heparin substitutes. Science 243 (1989) 1490-1493
    • (1989) Science , vol.243 , pp. 1490-1493
    • Folkman, J.1    Weisz, P.B.2    Joullie, M.M.3    Li, W.W.4    Ewing, W.R.5
  • 107
    • 0028142828 scopus 로고
    • Variations in the size and sulfation of heparin modulate the effect of heparin on the binding of VEGF165 to its receptors
    • Soker S., Goldstaub D., Svahn C.M., et al. Variations in the size and sulfation of heparin modulate the effect of heparin on the binding of VEGF165 to its receptors. Biochem. Biophys. Res. Commun. 203 (1994) 1339-1347
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1339-1347
    • Soker, S.1    Goldstaub, D.2    Svahn, C.M.3
  • 108
    • 0028355534 scopus 로고
    • Effect of low molecular weight heparan sulphate on angiogenesis in the rat cornea after chemical cauterization
    • Lepri A., Benelli U., Bernardini N., et al. Effect of low molecular weight heparan sulphate on angiogenesis in the rat cornea after chemical cauterization. J. Ocul. Pharmacol. 10 (1994) 273-280
    • (1994) J. Ocul. Pharmacol. , vol.10 , pp. 273-280
    • Lepri, A.1    Benelli, U.2    Bernardini, N.3
  • 109
    • 0031032234 scopus 로고    scopus 로고
    • Heparin oligosaccharides: inhibitors of the biological activity of bFGF on Caco-2 cells
    • Jayson G.C., and Gallagher J.T. Heparin oligosaccharides: inhibitors of the biological activity of bFGF on Caco-2 cells. Br. J. Cancer 75 (1997) 9-16
    • (1997) Br. J. Cancer , vol.75 , pp. 9-16
    • Jayson, G.C.1    Gallagher, J.T.2
  • 110
    • 24644478267 scopus 로고    scopus 로고
    • Non-anti-coagulant heparin inhibits metastasis but not primary tumor growth
    • Kragh M., Binderup L., Vig Hjarnaa P.J., et al. Non-anti-coagulant heparin inhibits metastasis but not primary tumor growth. Oncol. Rep. 14 (2005) 99-104
    • (2005) Oncol. Rep. , vol.14 , pp. 99-104
    • Kragh, M.1    Binderup, L.2    Vig Hjarnaa, P.J.3
  • 111
    • 4143094988 scopus 로고    scopus 로고
    • Circulating tumor cells, disease progression, and survival in metastatic breast cancer
    • Cristofanilli M., Budd G.T., Ellis M.J., et al. Circulating tumor cells, disease progression, and survival in metastatic breast cancer. N. Engl. J. Med. 351 (2004) 781-791
    • (2004) N. Engl. J. Med. , vol.351 , pp. 781-791
    • Cristofanilli, M.1    Budd, G.T.2    Ellis, M.J.3
  • 112
    • 20144385756 scopus 로고    scopus 로고
    • Circulating tumor cells: a novel prognostic factor for newly diagnosed metastatic breast cancer
    • Cristofanilli M., Hayes D.F., Budd G.T., et al. Circulating tumor cells: a novel prognostic factor for newly diagnosed metastatic breast cancer. J. Clin. Oncol. 23 (2005) 1420-1430
    • (2005) J. Clin. Oncol. , vol.23 , pp. 1420-1430
    • Cristofanilli, M.1    Hayes, D.F.2    Budd, G.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.