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Volumn 7, Issue 4, 2008, Pages 295-310

Exogenous proteases confer a significant chemopreventive effect in experimental tumor models

Author keywords

Breast; Chemoprevention; Lewis lung cancer; Melanoma; Pancreas; Protease

Indexed keywords

BREAST CANCER; CANCER RESEARCH; CARCINOGENESIS; CHEMOPROPHYLAXIS; ENZYME THERAPY; HUMAN; LEWIS CARCINOMA; MELANOMA; PANCREAS CANCER; PRIORITY JOURNAL; REVIEW; TUMOR MODEL;

EID: 58149177390     PISSN: 15347354     EISSN: 1552695X     Source Type: Journal    
DOI: 10.1177/1534735408327036     Document Type: Review
Times cited : (8)

References (75)
  • 1
    • 0002247909 scopus 로고    scopus 로고
    • Chemoprevention of cancer for the next millennium-quo vadis
    • Zänker KS Chemoprevention of cancer for the next millennium-quo vadis ? Cancer Lett. 1999 ; 143 (suppl 1). S7 - S11.
    • (1999) Cancer Lett , vol.143 , Issue.1
    • Zänker, K.S.1
  • 2
    • 29244447358 scopus 로고    scopus 로고
    • Bromelain exerts anti-inflammatory effects in an ovalbumin-induced murine model of allergic airway disease
    • Secor ER, Jr, Carson WF, Cloutier MM, et al. Bromelain exerts anti-inflammatory effects in an ovalbumin-induced murine model of allergic airway disease. Cell Immunol. 2005 ; 237: 68-75.
    • (2005) Cell Immunol , vol.237 , pp. 68-75
    • Secor Jr., E.R.1    Carson, W.F.2    Cloutier, M.M.3
  • 3
    • 0035153395 scopus 로고    scopus 로고
    • Association of alpha(1)-antichymotrypsin deficiency with milder lung disease in patients with cystic fibrosis
    • Mahadeva R., Sharples L., Ross-Russell RI, Webb AK, Bilton D., Lomas DA Association of alpha(1)-antichymotrypsin deficiency with milder lung disease in patients with cystic fibrosis. Thorax. 2001 ; 56: 53-58.
    • (2001) Thorax , vol.56 , pp. 53-58
    • Mahadeva, R.1    Sharples, L.2    Ross-Russell, R.I.3    Webb, A.K.4    Bilton, D.5    Lomas, D.A.6
  • 5
    • 58149186540 scopus 로고
    • Historia das Plantas Medicinaes e Utesi do Brazil. Rio de Janeiro
    • Peckolt T., Peckolt G. Historia das Plantas Medicinaes e Utesi do Brazil. Rio de Janeiro ; 1988. Cited by Asenjo CF. J Am Pharm Assoc. 1940 ; 29: 8.
    • (1940) Asenjo CF. J Am Pharm Assoc , vol.29 , pp. 8
    • Peckolt, T.1    Peckolt, G.2
  • 9
    • 13144289948 scopus 로고
    • Allergy to cow's milk in infants with nutritional disorders
    • Anderson AF, Schloss OM Allergy to cow's milk in infants with nutritional disorders. Am J Dis Child. 1923 ; 26: 415.
    • (1923) Am J Dis Child , vol.26 , pp. 415
    • Anderson, A.F.1    Schloss, O.M.2
  • 10
    • 58149183757 scopus 로고
    • Acne vulgaris. Treatment with oral bromelain (protease) and parenteral Staphyloccocus antigen
    • Baker A. Acne vulgaris. Treatment with oral bromelain (protease) and parenteral Staphyloccocus antigen. Pa Med J. 1962.
    • (1962) Pa Med J.
    • Baker, A.1
  • 12
    • 0015896128 scopus 로고
    • The interaction of alpha2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanisms
    • Barrett AJ, Starkey PM The interaction of alpha2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanisms. Biochem J. 1973 ; 133: 709-724.
    • (1973) Biochem J. , vol.133 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 13
  • 14
    • 0002669142 scopus 로고
    • Zur Behandlung von Zystitiden und Zystopyelitiden mit hydrolytischen Enzymen
    • Barsom S., Sasse-Rollenhagen K., Bettermann A. Zur Behandlung von Zystitiden und Zystopyelitiden mit hydrolytischen Enzymen. Acta Med Empir. 1983 ; 32: 125.
    • (1983) Acta Med Empir , vol.32 , pp. 125
    • Barsom, S.1    Sasse-Rollenhagen, K.2    Bettermann, A.3
  • 16
    • 0000828459 scopus 로고
    • Inflammation and inflammatory mechanisms
    • Jancsó N. Inflammation and inflammatory mechanisms. J Pharm Pharmacol. 1961 ; 13: 577-594.
    • (1961) J Pharm Pharmacol , vol.13 , pp. 577-594
    • Jancsó, N.1
  • 17
    • 58149197670 scopus 로고
    • Effect of trypsin on levels of antibiotics in the spinal fluid
    • Moss JN, Beiler JM, Martin GJ Effect of trypsin on levels of antibiotics in the spinal fluid. Bact Proc. 1955 ; 80.
    • (1955) Bact Proc. , pp. 80
    • Moss, J.N.1    Beiler, J.M.2    Martin, G.J.3
  • 18
    • 0000533014 scopus 로고
    • A plant protease for potentiation of and possible replacement of antibiotics
    • Neubauer R. A plant protease for potentiation of and possible replacement of antibiotics. Exp Med Surg. 1961 ; 19: 143-160.
    • (1961) Exp Med Surg , vol.19 , pp. 143-160
    • Neubauer, R.1
  • 19
    • 58149193319 scopus 로고
    • The use of trypsin in the therapy of tuberculous lymphadenitis and tuberculous fistulae
    • Rapoport C. The use of trypsin in the therapy of tuberculous lymphadenitis and tuberculous fistulae. Chest. 1958 ; 34: 154-161.
    • (1958) Chest , vol.34 , pp. 154-161
    • Rapoport, C.1
  • 20
    • 58149183756 scopus 로고
    • A case report of miliary tuberculosis and tuberculous meningitis treated with trypsin and antibiotics: One-year follow-up
    • Rapoport C. A case report of miliary tuberculosis and tuberculous meningitis treated with trypsin and antibiotics: one-year follow-up. Del Med J. 1958 ; 30: 167-169.
    • (1958) Del Med J , vol.30 , pp. 167-169
    • Rapoport, C.1
  • 22
    • 0021958280 scopus 로고
    • Basic studies on enzyme therapy of immune complex diseases
    • Steffen C., Menzel J. Basic studies on enzyme therapy of immune complex diseases. Wien Klin Wochenschr. 1985 ; 12: 376-385.
    • (1985) Wien Klin Wochenschr , vol.12 , pp. 376-385
    • Steffen, C.1    Menzel, J.2
  • 25
    • 0030878648 scopus 로고    scopus 로고
    • Intestinal absorption of undegraded proteins in men: Presence of bromelain in plasma after oral intake
    • Castell JV, Friedrich G., Kuhn CS, Poppe GE Intestinal absorption of undegraded proteins in men: presence of bromelain in plasma after oral intake. Am J Physiol. 1997 ; 273: 139-146.
    • (1997) Am J Physiol , vol.273 , pp. 139-146
    • Castell, J.V.1    Friedrich, G.2    Kuhn, C.S.3    Poppe, G.E.4
  • 26
    • 0025236251 scopus 로고
    • Interactions between cytokines and alpha2-macroglobulin
    • James K. Interactions between cytokines and alpha2-macroglobulin. Immunol Today. 1990 ; 11: 163-166.
    • (1990) Immunol Today , vol.11 , pp. 163-166
    • James, K.1
  • 27
    • 0023875968 scopus 로고
    • Immunomodulation by alpha 2-macroglobulin and alpha 2-macroglobulin- proteinase complexes: The effect on the human T lymphocyte response
    • Heumann D., Vischer TL Immunomodulation by alpha 2-macroglobulin and alpha 2-macroglobulin-proteinase complexes: the effect on the human T lymphocyte response. Eur J Immunol. 1988 ; 18: 755-760.
    • (1988) Eur J Immunol , vol.18 , pp. 755-760
    • Heumann, D.1    Vischer, T.L.2
  • 28
  • 29
    • 0000789424 scopus 로고    scopus 로고
    • Dose-related bioavailability of bromelain and trypsin after repeated oral administration
    • Donath F., Roots I., Mai I., et al. Dose-related bioavailability of bromelain and trypsin after repeated oral administration. Eur J Clin Pharmacol. 1997 ; 52 (suppl): 146.
    • (1997) Eur J Clin Pharmacol. , vol.52 , pp. 146
    • Donath, F.1    Roots, I.2    Mai, I.3
  • 30
    • 4444353546 scopus 로고
    • Sport, Alter und Immunsystem
    • Uhlenbruck G. Sport, Alter und Immunsystem. Med Welt. 1993 ; 44: 303-308.
    • (1993) Med Welt , vol.44 , pp. 303-308
    • Uhlenbruck, G.1
  • 33
    • 0027077553 scopus 로고
    • Bromelain treatment of human T cells removes CD44, CD45RA, E2/MIC2, CD6, CD7, CD8, and Leu8/ LAM1 surface molecules and markedly enhances D2-mediated T cell activation
    • Hale LP, Haynes BF Bromelain treatment of human T cells removes CD44, CD45RA, E2/MIC2, CD6, CD7, CD8, and Leu8/ LAM1 surface molecules and markedly enhances D2-mediated T cell activation. J Immunol. 1992 ; 149: 3809-3816.
    • (1992) J Immunol , vol.149 , pp. 3809-3816
    • Hale, L.P.1    Haynes, B.F.2
  • 34
    • 0027959260 scopus 로고
    • Bromelain proteinases modulate CD44 expression on human Molt 4/8 leukaemia and SK-Mel 28 melanoma cells in vitro
    • Harrach T., Gebauer F., Eckert K., Kunze R., Maurer H. Bromelain proteinases modulate CD44 expression on human Molt 4/8 leukaemia and SK-Mel 28 melanoma cells in vitro. Int J Oncol. 1994 ; 5: 485-488.
    • (1994) Int J Oncol , vol.5 , pp. 485-488
    • Harrach, T.1    Gebauer, F.2    Eckert, K.3    Kunze, R.4    Maurer, H.5
  • 35
    • 0025785601 scopus 로고
    • Cytokine binding and clearance properties of proteinase-activated alpha 2-macroglobulins
    • LaMarre J., Wollenberg GK, Gonias SL, Hayes MA Cytokine binding and clearance properties of proteinase-activated alpha 2-macroglobulins. Lab Invest. 1991 ; 65: 3-14.
    • (1991) Lab Invest , vol.65 , pp. 3-14
    • Lamarre, J.1    Wollenberg, G.K.2    Gonias, S.L.3    Hayes, M.A.4
  • 36
    • 0029897625 scopus 로고    scopus 로고
    • Immunomodulation by proteolytic enzymes
    • Lehmann PV Immunomodulation by proteolytic enzymes. Nephrol Dial Transplant. 1996 ; 11: 952-955.
    • (1996) Nephrol Dial Transplant , vol.11 , pp. 952-955
    • Lehmann, P.V.1
  • 37
    • 0031402602 scopus 로고    scopus 로고
    • Potential of targeting cell surface CD44 proteins with proteinases in preventing tumor growth and metastasis
    • Sy MS, Lu D., Kogerman P., Culp LA Potential of targeting cell surface CD44 proteins with proteinases in preventing tumor growth and metastasis. Int J Immunother. 1997 ; 3/4: 105-109.
    • (1997) Int J Immunother , vol.34 , pp. 105-109
    • Sy, M.S.1    Lu, D.2    Kogerman, P.3    Culp, L.A.4
  • 41
    • 0035136630 scopus 로고    scopus 로고
    • Alpha 2-macroglobulin-mediated degradation of amyloid beta 1-42: A mechanism to enhance amyloid beta catabolism
    • Lauer D., Reichenbach A., Birkenmeier G. Alpha 2-macroglobulin-mediated degradation of amyloid beta 1-42: a mechanism to enhance amyloid beta catabolism. Exp Neurol. 2001 ; 167: 385-392.
    • (2001) Exp Neurol , vol.167 , pp. 385-392
    • Lauer, D.1    Reichenbach, A.2    Birkenmeier, G.3
  • 42
    • 0004524722 scopus 로고
    • Zirkulierende Immunkomplexe: Immunsuppressive Wirkung auf Monozyten und NK- Zellen und deren partielle Aufhebung durch hydrolytische Enzyme
    • Leskovar P., Zanon R., Nachbar F., Meschik K. Zirkulierende Immunkomplexe: Immunsuppressive Wirkung auf Monozyten und NK- Zellen und deren partielle Aufhebung durch hydrolytische Enzyme. Dtsch Zschr Onkol. 1993 ; 25: 12-18.
    • (1993) Dtsch Zschr Onkol , vol.25 , pp. 12-18
    • Leskovar, P.1    Zanon, R.2    Nachbar, F.3    Meschik, K.4
  • 43
    • 58149196243 scopus 로고    scopus 로고
    • Proteolytic enzymes modulate the C1q-binding capacity of fixed immunocomplexes in vitro
    • Kunze R., Ransberger K., Stauder G., Gebauer F. Proteolytic enzymes modulate the C1q-binding capacity of fixed immunocomplexes in vitro. Eur J Immunol Dis. 1996 ; 1 (suppl): 17-29.
    • (1996) Eur J Immunol Dis. , vol.1 , pp. 17-29
    • Kunze, R.1    Ransberger, K.2    Stauder, G.3    Gebauer, F.4
  • 44
    • 0023647297 scopus 로고
    • In vivo degradation of immune complexes in the kidney by orally administered enzymes
    • Steffen C., Menzel J. In vivo degradation of immune complexes in the kidney by orally administered enzymes. Wien Klin Wochenschr. 1987 ; 99: 525-531.
    • (1987) Wien Klin Wochenschr , vol.99 , pp. 525-531
    • Steffen, C.1    Menzel, J.2
  • 45
    • 0033071821 scopus 로고    scopus 로고
    • Thrombin and trypsin receptors: The same mechanism of signalling on cellular surfaces
    • Olejar T., Nouza K. Thrombin and trypsin receptors: the same mechanism of signalling on cellular surfaces. Bratisl Lek Listy. 1999 ; 100: 75-79.
    • (1999) Bratisl Lek Listy , vol.100 , pp. 75-79
    • Olejar, T.1    Nouza, K.2
  • 46
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery O., Corvera C., Steinhoff M., Bunnett NW Proteinase-activated receptors: novel mechanisms of signaling by serine proteases. Am J Physiol. 1998 ; 274: 1429-1452.
    • (1998) Am J Physiol , vol.274 , pp. 1429-1452
    • Dery, O.1    Corvera, C.2    Steinhoff, M.3    Bunnett, N.W.4
  • 47
    • 0031807665 scopus 로고    scopus 로고
    • Activation of protease-activated receptor-2 (PAR2) elicits nitric oxide-dependent dilatation of the basilar artery in vitro
    • Sobey CG, Cocks TM Activation of protease-activated receptor-2 (PAR2) elicits nitric oxide-dependent dilatation of the basilar artery in vitro. Stroke. 1998 ; 29: 1439-1444.
    • (1998) Stroke , vol.29 , pp. 1439-1444
    • Sobey, C.G.1    Cocks, T.M.2
  • 49
    • 0031927754 scopus 로고    scopus 로고
    • Thrombin receptor overexpression in malignant and physiological invasion processes
    • Evev-Eam S., Uziely B., Cohen P., et al. Thrombin receptor overexpression in malignant and physiological invasion processes. Nat Med. 1998 ; 4: 909-914.
    • (1998) Nat Med , vol.4 , pp. 909-914
    • Evev-Eam, S.1    Uziely, B.2    Cohen, P.3
  • 50
    • 0030741026 scopus 로고    scopus 로고
    • Luminal trypsin may regulate enteroctes through proteinase activated receptor 2
    • Kong W., McConalogue K., Khitin LM, et al. Luminal trypsin may regulate enteroctes through proteinase activated receptor 2. Proc Natl Acad Sci USA. 1997 ; 94: 8884-8889.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8884-8889
    • Kong, W.1    McConalogue, K.2    Khitin, L.M.3
  • 51
    • 0029670360 scopus 로고    scopus 로고
    • Thrombin and trypsin induced Ca(2+) mobilization in human T cell lines through interaction with different proteinase activated receptors
    • Mari B., Guerin S., Far DF, et al. Thrombin and trypsin induced Ca(2+) mobilization in human T cell lines through interaction with different proteinase activated receptors. FASEB J. 1996 ; 10: 309-316.
    • (1996) FASEB J , vol.10 , pp. 309-316
    • Mari, B.1    Guerin, S.2    Far, D.F.3
  • 52
    • 0029928236 scopus 로고    scopus 로고
    • Neutrophil apoptosis induced by proteolytic enzymes
    • Trevani AS, Andonegui G., Giordano M., et al. Neutrophil apoptosis induced by proteolytic enzymes. Lab Invest. 1996 ; 74: 711-721.
    • (1996) Lab Invest , vol.74 , pp. 711-721
    • Trevani, A.S.1    Andonegui, G.2    Giordano, M.3
  • 53
    • 0037040862 scopus 로고    scopus 로고
    • Protease-activated receptor-2 activation causes EDHF-like coronary vasodilation: Selective preservation in ischemia/reperfusion injury: Involvement of lipoxygenase products, VR1 receptors, and C-fibers
    • McLean PG, Aston D., Sarkar D., Ahluwalia A. Protease-activated receptor-2 activation causes EDHF-like coronary vasodilation: selective preservation in ischemia/reperfusion injury: involvement of lipoxygenase products, VR1 receptors, and C-fibers. Circ Res. 2002 ; 90: 465-472.
    • (2002) Circ Res , vol.90 , pp. 465-472
    • McLean, P.G.1    Aston, D.2    Sarkar, D.3    Ahluwalia, A.4
  • 54
    • 0034817423 scopus 로고    scopus 로고
    • Advanced glycation end products and the progressive course of renal disease
    • Heidland A., Sebekova K., Schinzel R. Advanced glycation end products and the progressive course of renal disease. Am J Kidney Dis. 2001 ; 38 (suppl 1). S100 - S106.
    • (2001) Am J Kidney Dis , vol.38 , Issue.1
    • Heidland, A.1    Sebekova, K.2    Schinzel, R.3
  • 55
    • 0035128914 scopus 로고    scopus 로고
    • Advanced glycation end products impair protein turnover in LLC-PK1: Amelioration by trypsin
    • Xiang G., Schinzel R., Simm A., Sebekova K., Heidland A. Advanced glycation end products impair protein turnover in LLC-PK1: amelioration by trypsin. Kidney Int. 2001 ; 78 (suppl): S53 - S57.
    • (2001) Kidney Int. , vol.78
    • Xiang, G.1    Schinzel, R.2    Simm, A.3    Sebekova, K.4    Heidland, A.5
  • 56
    • 0034879125 scopus 로고    scopus 로고
    • Advanced glycation end products (AGEs)-induced expression of TGF-β1 is suppressed by a protease in the tubule cell line LLC-PK1
    • Xiang G., Schinzel R., Simm A., et al. Advanced glycation end products (AGEs)-induced expression of TGF-β1 is suppressed by a protease in the tubule cell line LLC-PK1. Nephrol Dial Transplant. 2001 ; 16: 1562-1567.
    • (2001) Nephrol Dial Transplant , vol.16 , pp. 1562-1567
    • Xiang, G.1    Schinzel, R.2    Simm, A.3
  • 57
    • 0037455982 scopus 로고    scopus 로고
    • Genotoxicity of advanced glycation end products in mammalian cells
    • Stopper H., Schinzel R., Sebeková K., Heidland A. Genotoxicity of advanced glycation end products in mammalian cells. Cancer Lett. 2003 ; 190: 151-156.
    • (2003) Cancer Lett , vol.190 , pp. 151-156
    • Stopper, H.1    Schinzel, R.2    Sebeková, K.3    Heidland, A.4
  • 58
    • 0012784114 scopus 로고
    • Influence of bromelain on penetration of antibiotics in uterus, salpinx and ovary
    • Luerti M., Vignali ML Influence of bromelain on penetration of antibiotics in uterus, salpinx and ovary. Drugs Expt Clin Res. 1978 ; 4: 45-48.
    • (1978) Drugs Expt Clin Res , vol.4 , pp. 45-48
    • Luerti, M.1    Vignali, M.L.2
  • 59
    • 0001828930 scopus 로고
    • Effect of bromelain on serum and tissue levels of amoxycillin
    • Tinozzi S., Venegoni A. Effect of bromelain on serum and tissue levels of amoxycillin. Drugs Exp Clin Res. 1978 ; 4: 39-44.
    • (1978) Drugs Exp Clin Res , vol.4 , pp. 39-44
    • Tinozzi, S.1    Venegoni, A.2
  • 60
    • 58149194672 scopus 로고
    • Activity on cancers cells and distribution in tissue of anticancer drugs
    • Shibata HR, et al. Activity on cancers cells and distribution in tissue of anticancer drugs. Prog Antimicrob Anticancer Chemother. 1970 ; 2: 334-339.
    • (1970) Prog Antimicrob Anticancer Chemother , vol.2 , pp. 334-339
    • Shibata, H.R.1
  • 61
    • 0028171487 scopus 로고
    • Proteolytic enzymes and amylase induce cytokine production in human peripheral blood mononuclear cells in vitro
    • Desser L., Rehberger A., Paukovits W. Proteolytic enzymes and amylase induce cytokine production in human peripheral blood mononuclear cells in vitro. Cancer Biother. 1994 ; 3: 253-263.
    • (1994) Cancer Biother , vol.3 , pp. 253-263
    • Desser, L.1    Rehberger, A.2    Paukovits, W.3
  • 62
    • 0027496317 scopus 로고
    • Cytokine synthesis in human peripheral blood mononuclear cells after oral administration of polyenzyme preparations
    • Desser L., Rehberger A., Kokron E., Paukovits W. Cytokine synthesis in human peripheral blood mononuclear cells after oral administration of polyenzyme preparations. Oncology. 1993 ; 50: 403-407.
    • (1993) Oncology , vol.50 , pp. 403-407
    • Desser, L.1    Rehberger, A.2    Kokron, E.3    Paukovits, W.4
  • 63
    • 0025065408 scopus 로고
    • Induction of tumor necrosis factor in human peripheral-blood mononuclear cells by proteolytic enzymes
    • Desser L., Rehberger A. Induction of tumor necrosis factor in human peripheral-blood mononuclear cells by proteolytic enzymes. Oncology. 1990 ; 6: 475-477.
    • (1990) Oncology , vol.6 , pp. 475-477
    • Desser, L.1    Rehberger, A.2
  • 64
    • 0029022727 scopus 로고
    • Stimulation of reactive oxygen species production and cytotoxicity in human neutrophils in vitro and after oral administration of a polyenzyme preparation
    • Závadová E., Desser L., Mohr T. Stimulation of reactive oxygen species production and cytotoxicity in human neutrophils in vitro and after oral administration of a polyenzyme preparation. Cancer Biother. 1995 ; 10: 147-152.
    • (1995) Cancer Biother , vol.10 , pp. 147-152
    • Závadová, E.1    Desser, L.2    Mohr, T.3
  • 65
    • 58149187939 scopus 로고    scopus 로고
    • The influence of proteinases on in vivo blastic transformation in rat species SD/IPCV with spontaneous lymphoblastic leukaemia
    • Wald M., Olejár T., Poučková P., Zadinová M. The influence of proteinases on in vivo blastic transformation in rat species SD/IPCV with spontaneous lymphoblastic leukaemia. Br J Haematol. 1998 ; 102: 294.
    • (1998) Br J Haematol , vol.102 , pp. 294
    • Wald, M.1    Olejár, T.2    Poučková, P.3    Zadinová, M.4
  • 66
    • 0031565954 scopus 로고    scopus 로고
    • Polyenzyme preparation Wobe-Mugos e inhibits growth of solid tumors and development of experimental metastases in mice
    • Wald M., Závadová E., Poučková P., Zadinová M., Boubelík M. Polyenzyme preparation Wobe-Mugos E inhibits growth of solid tumors and development of experimental metastases in mice. Life Sci. 1997 ; 3: PL43 - PL48.
    • (1997) Life Sci. , vol.3
    • Wald, M.1    Závadová, E.2    Poučková, P.3    Zadinová, M.4    Boubelík, M.5
  • 67
    • 0034919719 scopus 로고    scopus 로고
    • Mixture of trypsin, chymotrypsin and papain reduces formation of metastases and extends survival time of C57Bl6 mice with syngeneic melanoma B16
    • Wald M., Olejár T., Šebková V., Zadinová M., Boubelík M., Pou?ková P. Mixture of trypsin, chymotrypsin and papain reduces formation of metastases and extends survival time of C57Bl6 mice with syngeneic melanoma B16. Cancer Chemother Pharmacol. 2001 ; 47 (suppl): S16 - S22.
    • (2001) Cancer Chemother Pharmacol. , vol.47
    • Wald, M.1    Olejár, T.2    Šebková, V.3    Zadinová, M.4    Boubelík, M.5    Pouková, P.6
  • 68
    • 0032544368 scopus 로고    scopus 로고
    • Proteinases reduce metastatic dissemination and increase survival time in C57Bl6 mice with Lewis lung carcinoma
    • Wald M., Olejár T., Poučková P., Zadinová M. Proteinases reduce metastatic dissemination and increase survival time in C57Bl6 mice with Lewis lung carcinoma. Life Sci. 1998 ; 63: PL237 - PL243.
    • (1998) Life Sci. , vol.63
    • Wald, M.1    Olejár, T.2    Poučková, P.3    Zadinová, M.4
  • 69
    • 58149195143 scopus 로고    scopus 로고
    • The influence of trypsin, chymotrypsin and papain on the growth of human pancreatic adenocarcinoma transplanted to nu/nu mice
    • Wald M., Poučková P., Hloušková D., Altnerová M., Olejár T. The influence of trypsin, chymotrypsin and papain on the growth of human pancreatic adenocarcinoma transplanted to nu/nu mice. Eur J Cancer. 1999 ; 4 (suppl): 148.
    • (1999) Eur J Cancer. , vol.4 , pp. 148
    • Wald, M.1    Poučková, P.2    Hloušková, D.3    Altnerová, M.4    Olejár, T.5
  • 70
    • 0035724017 scopus 로고    scopus 로고
    • Proteinase administration reduces growth of human breast and pancreatic cancer in nude mice and diminishes expression of some tumorigenesis biomarkers
    • Wald M., Šebková V., Österreicher J., Zadinová M., Poučková P. Proteinase administration reduces growth of human breast and pancreatic cancer in nude mice and diminishes expression of some tumorigenesis biomarkers. Int J Immunother. 2001 ; 2-4: 65-73.
    • (2001) Int J Immunother , vol.2-4 , pp. 65-73
    • Wald, M.1    Šebková, V.2    Österreicher, J.3    Zadinová, M.4    Poučková, P.5
  • 71
    • 0034919720 scopus 로고    scopus 로고
    • Retrolective cohort study of an additive therapy with an oral enzyme preparation in patients with multiple myeloma
    • Sakalová A., Bock PR, Dedík L., et al. Retrolective cohort study of an additive therapy with an oral enzyme preparation in patients with multiple myeloma. Cancer Chemother Pharmacol. 2001 ; 47 (suppl): S38 - S44.
    • (2001) Cancer Chemother Pharmacol. , vol.47
    • Sakalová, A.1    Bock, P.R.2    Dedík, L.3
  • 72
    • 58149177227 scopus 로고    scopus 로고
    • Enzyme therapy improved remission time, soluble TNF-receptors and beta2-microglobulin concentration in chemotherapy treated multiple myeloma patients
    • Sakalova A., Desser L., Zavadova E., Holomanova D., Mohr T. Enzyme therapy improved remission time, soluble TNF-receptors and beta2-microglobulin concentration in chemotherapy treated multiple myeloma patients. Br J Haematol. 1998 ; 1: 353.
    • (1998) Br J Haematol , vol.1 , pp. 353
    • Sakalova, A.1    Desser, L.2    Zavadova, E.3    Holomanova, D.4    Mohr, T.5
  • 73
    • 0031396359 scopus 로고    scopus 로고
    • Concentrations of soluble tumor necrosis factor receptors, β2-microglobulin, IL-6 and TNF in serum of multiple myeloma patients after chemotherapy and after combined enzyme + chemotherapy
    • Desser L., Sakalová A., Závadová E., Holomanová D., Mohr T. Concentrations of soluble tumor necrosis factor receptors, β2-microglobulin, IL-6 and TNF in serum of multiple myeloma patients after chemotherapy and after combined enzyme + chemotherapy. Int J Immunother. 1997 ; 3/4: 121-130.
    • (1997) Int J Immunother , vol.34 , pp. 121-130
    • Desser, L.1    Sakalová, A.2    Závadová, E.3    Holomanová, D.4    Mohr, T.5


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