메뉴 건너뛰기




Volumn 26, Issue 3, 2013, Pages 444-455

Azaspiracid-1 inhibits the maturation of cathepsin D in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

AZASPIRACID 1; CATHEPSIN D; LYSOSOME ENZYME; MARINE TOXIN; UNCLASSIFIED DRUG;

EID: 84875176985     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx300511z     Document Type: Article
Times cited : (14)

References (59)
  • 1
    • 68949089361 scopus 로고    scopus 로고
    • Marine biotoxins in shellfish - Azaspiracid group. Scientific Opinion of the Panel on Contaminants in the Food chain
    • European Food Safety Authority
    • European Food Safety Authority (2008) Marine biotoxins in shellfish-Azaspiracid group. Scientific Opinion of the Panel on Contaminants in the Food chain EFSA J. 723, 1-52
    • (2008) EFSA J. , vol.723 , pp. 1-52
  • 2
    • 0002893951 scopus 로고    scopus 로고
    • Winter toxicity of unknown aetiology in mussels
    • McMahon, T. and Silke, J. (1996) Winter toxicity of unknown aetiology in mussels Harmful Algae News 14, 2
    • (1996) Harmful Algae News , vol.14 , pp. 2
    • McMahon, T.1    Silke, J.2
  • 3
    • 0032582026 scopus 로고    scopus 로고
    • Azaspiracid, a new marine toxin having a unique spiro ring assemblies, isolated from Irish mussels Mytilus edulis
    • Satake, M., Ofuji, K., Naoki, H., James, K. J., Furey, A., McMahon, T., Silke, J., and Yasumoto, T. (1998) Azaspiracid, a new marine toxin having a unique spiro ring assemblies, isolated from Irish mussels Mytilus edulis J. Am. Chem. Soc. 120, 9967-9968
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9967-9968
    • Satake, M.1    Ofuji, K.2    Naoki, H.3    James, K.J.4    Furey, A.5    McMahon, T.6    Silke, J.7    Yasumoto, T.8
  • 5
    • 0141767093 scopus 로고    scopus 로고
    • The first identification of azaspiracids in shellfish from France and Spain
    • Magdalena, A. B., Lehane, M., Krys, S., Fernández, M. L., Furey, A., and James, K. J. (2003) The first identification of azaspiracids in shellfish from France and Spain Toxicon 42, 105-108
    • (2003) Toxicon , vol.42 , pp. 105-108
    • Magdalena, A.B.1    Lehane, M.2    Krys, S.3    Fernández, M.L.4    Furey, A.5    James, K.J.6
  • 7
    • 72749106350 scopus 로고    scopus 로고
    • First identification of azaspiracid and spirolides in Mesodesma donacium and Mulinia edulis from Northern Chile
    • álvarez, G., Uribe, E., ávalos, P., Mariño, C., and Blanco, J. (2010) First identification of azaspiracid and spirolides in Mesodesma donacium and Mulinia edulis from Northern Chile Toxicon 55, 638-641
    • (2010) Toxicon , vol.55 , pp. 638-641
    • Álvarez, G.1    Uribe, E.2    Ávalos, P.3    Mariño, C.4    Blanco, J.5
  • 8
    • 77953434547 scopus 로고    scopus 로고
    • First evidence of azaspiracids (AZAs): A family of lipophilic polyether marine toxins in scallops (Argopecten purpuratus) and mussels (Mytilus chilensis) collected in two regions of Chile
    • López-Rivera, A., O'Callaghan, K., Moriarty, M., O'Driscoll, D., Hamilton, B., Lehane, M., James, K. J., and Furey, A. (2010) First evidence of azaspiracids (AZAs): A family of lipophilic polyether marine toxins in scallops (Argopecten purpuratus) and mussels (Mytilus chilensis) collected in two regions of Chile Toxicon 55, 692-701
    • (2010) Toxicon , vol.55 , pp. 692-701
    • López-Rivera, A.1    O'Callaghan, K.2    Moriarty, M.3    O'Driscoll, D.4    Hamilton, B.5    Lehane, M.6    James, K.J.7    Furey, A.8
  • 9
    • 0033974774 scopus 로고    scopus 로고
    • Multiple organ damage caused by a new toxin azaspiracid, isolated from mussels produced in Ireland
    • Ito, E., Satake, M., Ofuji, K., Kurita, N., McMahon, T., James, K., and Yasumoto, T. (2000) Multiple organ damage caused by a new toxin azaspiracid, isolated from mussels produced in Ireland Toxicon 38, 917-930
    • (2000) Toxicon , vol.38 , pp. 917-930
    • Ito, E.1    Satake, M.2    Ofuji, K.3    Kurita, N.4    McMahon, T.5    James, K.6    Yasumoto, T.7
  • 10
    • 0036027438 scopus 로고    scopus 로고
    • Chronic effects in mice caused by oral administration of sublethal doses of azaspiracid, a new marine toxin isolated from mussels
    • Ito, E., Satake, M., Ofuji, K., Higashi, M., Harigaya, K., McMahon, T., and Yasumoto, T. (2002) Chronic effects in mice caused by oral administration of sublethal doses of azaspiracid, a new marine toxin isolated from mussels Toxicon 40, 193-203
    • (2002) Toxicon , vol.40 , pp. 193-203
    • Ito, E.1    Satake, M.2    Ofuji, K.3    Higashi, M.4    Harigaya, K.5    McMahon, T.6    Yasumoto, T.7
  • 12
    • 77958508740 scopus 로고    scopus 로고
    • Sub-lethal dosing of azaspiracid-1 in female NMRI mice
    • Aasen, J. A. B., Espenes, A., Hess, P., and Aune, T. (2010) Sub-lethal dosing of azaspiracid-1 in female NMRI mice Toxicon 56, 1419-1425
    • (2010) Toxicon , vol.56 , pp. 1419-1425
    • Aasen, J.A.B.1    Espenes, A.2    Hess, P.3    Aune, T.4
  • 13
    • 19344361922 scopus 로고    scopus 로고
    • Teratogenic effects of azaspiracid-1 identified by microinjection of Japanese medaka (Oryzias latipes) embryos
    • Colman, J. R., Twiner, M. J., Hess, P., McMahon, T., Satake, M., Yasumoto, T., Doucette, G. J., and Ramsdell, J. S. (2005) Teratogenic effects of azaspiracid-1 identified by microinjection of Japanese medaka (Oryzias latipes) embryos Toxicon 45, 881-890
    • (2005) Toxicon , vol.45 , pp. 881-890
    • Colman, J.R.1    Twiner, M.J.2    Hess, P.3    McMahon, T.4    Satake, M.5    Yasumoto, T.6    Doucette, G.J.7    Ramsdell, J.S.8
  • 14
    • 33744940640 scopus 로고    scopus 로고
    • Regulation 853/2004
    • European Communities () - 206
    • European Communities (2004) Regulation 853/2004 Off. J. Eur. Commun. L139, 55-206
    • (2004) Off. J. Eur. Commun. , vol.139 , pp. 55
  • 15
    • 38449093683 scopus 로고    scopus 로고
    • Regulation 2074/2005
    • European Communities () - 59
    • European Communities (2005) Regulation 2074/2005 Off. J. Eur. Commun. L338, 27-59
    • (2005) Off. J. Eur. Commun. , vol.338 , pp. 27
  • 16
    • 77950909207 scopus 로고    scopus 로고
    • Phycotoxins: Chemistry, Mechanisms of Action and Shellfish Poisoning
    • in (Luch, A. Ed.) pp, BirkhaÌŠuser-Verlag AG, Basel, Switzerland. - 122
    • Rossini, G. P. and Hess, P. (2010) Phycotoxins: Chemistry, Mechanisms of Action and Shellfish Poisoning, in Molecular, Clinical and Environmental Toxicology (Luch, A., Ed.) pp 65-122, BirkhaÌŠuser-Verlag AG, Basel, Switzerland.
    • (2010) Molecular, Clinical and Environmental Toxicology , pp. 65
    • Rossini, G.P.1    Hess, P.2
  • 19
    • 33846512435 scopus 로고    scopus 로고
    • Azaspiracid-1 alters the E-cadherin pool in epithelial cells
    • Ronzitti, G., Hess, P., Rehmann, N., and Rossini, G. P. (2007) Azaspiracid-1 alters the E-cadherin pool in epithelial cells Toxicol. Sci. 95, 427-435
    • (2007) Toxicol. Sci. , vol.95 , pp. 427-435
    • Ronzitti, G.1    Hess, P.2    Rehmann, N.3    Rossini, G.P.4
  • 20
    • 33846404512 scopus 로고    scopus 로고
    • Effects of azaspiracid-1, a potent cytotoxic agent, on primary neuronal cultures. A structure-activity relationship study
    • Vale, C., Nicolaou, K. C., Frederick, M. O., Gómez-Limia, B., Alfonso, A., Vieytes, M. R., and Botana, L. M. (2007) Effects of azaspiracid-1, a potent cytotoxic agent, on primary neuronal cultures. A structure-activity relationship study J. Med. Chem. 50, 356-363
    • (2007) J. Med. Chem. , vol.50 , pp. 356-363
    • Vale, C.1    Nicolaou, K.C.2    Frederick, M.O.3    Gómez-Limia, B.4    Alfonso, A.5    Vieytes, M.R.6    Botana, L.M.7
  • 21
    • 77951528520 scopus 로고    scopus 로고
    • Involvement of caspase activation in azaspiracid-induced neurotoxicity in neonatal neurons
    • Cao, Z., LePage, K. T., Frederick, M. O., Nicolaou, K. C., and Murray, T. F. (2010) Involvement of caspase activation in azaspiracid-induced neurotoxicity in neonatal neurons Toxicol. Sci. 114, 323-334
    • (2010) Toxicol. Sci. , vol.114 , pp. 323-334
    • Cao, Z.1    Lepage, K.T.2    Frederick, M.O.3    Nicolaou, K.C.4    Murray, T.F.5
  • 25
    • 39149132818 scopus 로고    scopus 로고
    • Transcriptional profiling and inhibition of cholesterol biosynthesis in human T lymphocyte cells by the marine toxin azaspiracid
    • Twiner, M. J., Ryan, J. C., Morey, J. S., Van Dolah, F. M., Hess, P., McMahon, T., and Doucette, G. J. (2008) Transcriptional profiling and inhibition of cholesterol biosynthesis in human T lymphocyte cells by the marine toxin azaspiracid Genomics 91, 289-300
    • (2008) Genomics , vol.91 , pp. 289-300
    • Twiner, M.J.1    Ryan, J.C.2    Morey, J.S.3    Van Dolah, F.M.4    Hess, P.5    McMahon, T.6    Doucette, G.J.7
  • 28
    • 75249087776 scopus 로고    scopus 로고
    • Cell volume decrease as a link between azaspiracid-induced cytotoxicity and c-Jun-N-terminal kinase activation in cultured neurons
    • Vale, C., Nicolaou, K. C., Frederick, M. O., Vieytes, M. R., and Botana, L. M. (2010) Cell volume decrease as a link between azaspiracid-induced cytotoxicity and c-Jun-N-terminal kinase activation in cultured neurons Toxicol. Sci. 113, 158-168
    • (2010) Toxicol. Sci. , vol.113 , pp. 158-168
    • Vale, C.1    Nicolaou, K.C.2    Frederick, M.O.3    Vieytes, M.R.4    Botana, L.M.5
  • 29
    • 77955874348 scopus 로고    scopus 로고
    • Azaspiracid-1 inhibits endocytosis of plasma membrane proteins in epithelial cells
    • Bellocci, M., Sala, G. L., Callegari, F., and Rossini, G. P. (2010) Azaspiracid-1 inhibits endocytosis of plasma membrane proteins in epithelial cells Toxicol. Sci. 117, 109-121
    • (2010) Toxicol. Sci. , vol.117 , pp. 109-121
    • Bellocci, M.1    Sala, G.L.2    Callegari, F.3    Rossini, G.P.4
  • 34
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D - Many functions of one aspartic protease
    • Benes, P., Vetvicka, V., and Fusek, M. (2008) Cathepsin D-Many functions of one aspartic protease Crit. Rev. Oncol. Hematol. 68, 12-28
    • (2008) Crit. Rev. Oncol. Hematol. , vol.68 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 35
    • 0018847874 scopus 로고
    • A secreted glycoprotein induced by estrogen in human breast cancer cell lines
    • Westley, B. and Rochefort, H. (1980) A secreted glycoprotein induced by estrogen in human breast cancer cell lines Cell 20, 352-362
    • (1980) Cell , vol.20 , pp. 352-362
    • Westley, B.1    Rochefort, H.2
  • 37
    • 0031709904 scopus 로고    scopus 로고
    • Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors
    • Laurent-Matha, V., Farnoud, M. R., Lucas, A., Rougeot, C., Garcia, M., and Rochefort, H. (1998) Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors J. Cell Sci. 111, 2539-2549
    • (1998) J. Cell Sci. , vol.111 , pp. 2539-2549
    • Laurent-Matha, V.1    Farnoud, M.R.2    Lucas, A.3    Rougeot, C.4    Garcia, M.5    Rochefort, H.6
  • 38
    • 4544262273 scopus 로고    scopus 로고
    • Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells
    • Kokkonen, N., Rivinoja, A., Kauppila, A., Suokas, M., Kellokumpu, I., and Kellokumpu, S. (2004) Defective acidification of intracellular organelles results in aberrant secretion of cathepsin D in cancer cells J. Biol. Chem. 279, 39982-39988
    • (2004) J. Biol. Chem. , vol.279 , pp. 39982-39988
    • Kokkonen, N.1    Rivinoja, A.2    Kauppila, A.3    Suokas, M.4    Kellokumpu, I.5    Kellokumpu, S.6
  • 39
    • 33646367913 scopus 로고    scopus 로고
    • Processing of human cathepsin D is independent of its catalytic function and auto-activation: Involvement of cathepsins L and B
    • Laurent-Matha, V., Derocq, D., Prébois, C., Katunuma, N., and Liaudet-Coopman, E. (2006) Processing of human cathepsin D is independent of its catalytic function and auto-activation: involvement of cathepsins L and B J. Biochem. 139, 363-371
    • (2006) J. Biochem. , vol.139 , pp. 363-371
    • Laurent-Matha, V.1    Derocq, D.2    Prébois, C.3    Katunuma, N.4    Liaudet-Coopman, E.5
  • 40
    • 0033566342 scopus 로고    scopus 로고
    • Different sensitivities of p42 mitogen activated protein kinase to phorbol ester and okadaic acid tumor promoters among cell types
    • Rossini, G. P., Pinna, C., and Malaguti, C. (1999) Different sensitivities of p42 mitogen activated protein kinase to phorbol ester and okadaic acid tumor promoters among cell types Biochem. Pharmacol. 58, 279-284
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 279-284
    • Rossini, G.P.1    Pinna, C.2    Malaguti, C.3
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 73849141896 scopus 로고    scopus 로고
    • The cytotoxicity pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins
    • Sala, G. L., Bellocci, M., and Rossini, G. P. (2009) The cytotoxicity pathway triggered by palytoxin involves a change in the cellular pool of stress response proteins Chem. Res. Toxicol. 22, 2009-2016
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 2009-2016
    • Sala, G.L.1    Bellocci, M.2    Rossini, G.P.3
  • 45
    • 38749087936 scopus 로고    scopus 로고
    • Yessotoxin inhibits the complete degradation of E-cadherin
    • Callegari, F. and Rossini, G. P. (2008) Yessotoxin inhibits the complete degradation of E-cadherin Toxicology 244, 133-144
    • (2008) Toxicology , vol.244 , pp. 133-144
    • Callegari, F.1    Rossini, G.P.2
  • 46
    • 0032906630 scopus 로고    scopus 로고
    • Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin
    • Ishidoh, K., Takeda-Ezaki, M., Watanabe, S., Sato, N., Aihara, M., Imagawa, K., Kikuchi, M., and Kominami, E. (1999) Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin J. Biochem. 125, 770-779
    • (1999) J. Biochem. , vol.125 , pp. 770-779
    • Ishidoh, K.1    Takeda-Ezaki, M.2    Watanabe, S.3    Sato, N.4    Aihara, M.5    Imagawa, K.6    Kikuchi, M.7    Kominami, E.8
  • 47
    • 0029096635 scopus 로고
    • Identification of five molecular forms of cathepsin D in bovine milk
    • Larsen, L. B. and Petersen, T. E. (1995) Identification of five molecular forms of cathepsin D in bovine milk Adv. Exp. Med. Biol. 362, 279-283
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 279-283
    • Larsen, L.B.1    Petersen, T.E.2
  • 48
    • 0142074855 scopus 로고    scopus 로고
    • Immunological similarity between Schistosoma and bovine cathepsin D
    • Valdivieso, E., Bermudez, H., Hoebeke, J., Noya, O., and Cesari, I. M. (2003) Immunological similarity between Schistosoma and bovine cathepsin D Imunol. Lett. 89, 81-88
    • (2003) Imunol. Lett. , vol.89 , pp. 81-88
    • Valdivieso, E.1    Bermudez, H.2    Hoebeke, J.3    Noya, O.4    Cesari, I.M.5
  • 49
    • 79959362171 scopus 로고    scopus 로고
    • The Use of Proteomics in the Study of Molecular Responses and Toxicity Pathways in Biological Systems
    • in (Fishbein, J. C. Ed.) Vol. pp, Elsevier, Amsterdam. - 109
    • Rossini, G. P., Sala, G. L., Ronzitti, G., and Bellocci, M. (2011) The Use of Proteomics in the Study of Molecular Responses and Toxicity Pathways in Biological Systems, in Advances in Molecular Toxicology (Fishbein, J. C., Ed.) Vol. 5, pp 45-109, Elsevier, Amsterdam.
    • (2011) Advances in Molecular Toxicology , vol.5 , pp. 45
    • Rossini, G.P.1    Sala, G.L.2    Ronzitti, G.3    Bellocci, M.4
  • 51
    • 0037194598 scopus 로고    scopus 로고
    • Cathepsin-D affects multiple tumor progression steps in vivo: Proliferation, angiogenesis and apoptosis
    • Berchem, G., Glondu, M., Gleizes, M., Brouillet, J.-P., Vignon, F., Garcia, M., and Liaudet-Coopman, E. (2002) Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis Oncogene 21, 5951-5955
    • (2002) Oncogene , vol.21 , pp. 5951-5955
    • Berchem, G.1    Glondu, M.2    Gleizes, M.3    Brouillet, J.-P.4    Vignon, F.5    Garcia, M.6    Liaudet-Coopman, E.7
  • 53
    • 84861671713 scopus 로고    scopus 로고
    • Lysosomal pathways to cell death and their therapeutic applications
    • Česen, M. H., Pegan, K., Špes, A., and Turk, B. (2012) Lysosomal pathways to cell death and their therapeutic applications Exp. Cell Res. 318, 1245-1251
    • (2012) Exp. Cell Res. , vol.318 , pp. 1245-1251
    • Česen, M.H.1    Pegan, K.2    Špes, A.3    Turk, B.4
  • 54
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinszstein, D. C., Codogno, P., and Levine, B. (2012) Autophagy modulation as a potential therapeutic target for diverse diseases Nat. Rev. Drug Discovery 11, 709-730
    • (2012) Nat. Rev. Drug Discovery , vol.11 , pp. 709-730
    • Rubinszstein, D.C.1    Codogno, P.2    Levine, B.3
  • 55
    • 33749643860 scopus 로고    scopus 로고
    • Lysosomes as the target of yessotoxin in invertebrate and vertebrate cell lines
    • Malagoli, D., Marchesini, E., and Ottaviani, E. (2006) Lysosomes as the target of yessotoxin in invertebrate and vertebrate cell lines Toxicol. Lett. 167, 75-83
    • (2006) Toxicol. Lett. , vol.167 , pp. 75-83
    • Malagoli, D.1    Marchesini, E.2    Ottaviani, E.3
  • 56
    • 66249137151 scopus 로고    scopus 로고
    • The algal metabolite yessotoxin affects heterogeneous nuclear ribonucleoproteins in HepG2 cells
    • Young, C., Truman, P., Boucher, M., Keyzers, R. A., Northcote, P., and Jordan, T. W. (2009) The algal metabolite yessotoxin affects heterogeneous nuclear ribonucleoproteins in HepG2 cells Proteomics 9, 2529-2542
    • (2009) Proteomics , vol.9 , pp. 2529-2542
    • Young, C.1    Truman, P.2    Boucher, M.3    Keyzers, R.A.4    Northcote, P.5    Jordan, T.W.6
  • 58
    • 79955024761 scopus 로고    scopus 로고
    • Combined oral toxicity of azaspiracid-1 and yessotoxin in female NMRI mice
    • Aasen, J. A. B., Espenes, A., Miles, C. O., Samdal, I. A., Hess, P., and Aune, T. (2011) Combined oral toxicity of azaspiracid-1 and yessotoxin in female NMRI mice Toxicon 57, 909-917
    • (2011) Toxicon , vol.57 , pp. 909-917
    • Aasen, J.A.B.1    Espenes, A.2    Miles, C.O.3    Samdal, I.A.4    Hess, P.5    Aune, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.