메뉴 건너뛰기




Volumn 33, Issue 3, 2003, Pages 443-455

Destruxins, cyclodepsipeptides, block the formation of actin rings and prominent clear zones and ruffled borders in osteoclasts

Author keywords

Actin ring; Bone resorption; Destruxin; Osteoclast; Ruffled border

Indexed keywords

ACTIN; CYCLODEPSIPEPTIDE; DESTRUXIN; DEXTRUXIN B; DEXTRUXIN E; UNCLASSIFIED DRUG;

EID: 10744222548     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/S8756-3282(03)00201-1     Document Type: Article
Times cited : (37)

References (43)
  • 1
    • 85003152202 scopus 로고
    • Modulation of osteoclast differentiation
    • Suda T., Takahashi N., Martin T.J. Modulation of osteoclast differentiation. Endocr Rev. 13:1992;66-80.
    • (1992) Endocr Rev , vol.13 , pp. 66-80
    • Suda, T.1    Takahashi, N.2    Martin, T.J.3
  • 2
    • 0024327043 scopus 로고
    • Molecular mechanisms of bone resorption by the osteoclast
    • Baron R. Molecular mechanisms of bone resorption by the osteoclast. Anat Rec. 224:1989;317-324.
    • (1989) Anat Rec , vol.224 , pp. 317-324
    • Baron, R.1
  • 5
    • 0030752553 scopus 로고    scopus 로고
    • Integrin function in osteoclasts
    • Rodan S.B., Rodan G.A. Integrin function in osteoclasts. J Endocrinol. 154:1997;S47-56.
    • (1997) J Endocrinol , vol.154 , pp. 47-56
    • Rodan, S.B.1    Rodan, G.A.2
  • 8
    • 0036241632 scopus 로고    scopus 로고
    • Calcitonin for the long-term prevention and treatment of postmenopausal osteoporosis
    • Body J.J. Calcitonin for the long-term prevention and treatment of postmenopausal osteoporosis. Bone. 30:2002;75S-79S.
    • (2002) Bone , vol.30
    • Body, J.J.1
  • 9
    • 0015992581 scopus 로고
    • The effects of parathyroid hormone, colchicine, and calcitonin on the ultrastructure and the activity of osteoclasts in organ culture
    • Holtrop M.E., Raisz L.G., Simmons H.A. The effects of parathyroid hormone, colchicine, and calcitonin on the ultrastructure and the activity of osteoclasts in organ culture. J Cell Biol. 60:1974;346-355.
    • (1974) J Cell Biol , vol.60 , pp. 346-355
    • Holtrop, M.E.1    Raisz, L.G.2    Simmons, H.A.3
  • 10
    • 0024801643 scopus 로고
    • Comparison between the effects of forskolin and calcitonin on bone resorption and osteoclast morphology in vitro
    • Lerner U.H., Ransjo M., Klaushofer K., Horandner H., Hoffmann O., Czerwenka E., Koller K., Peterlik M. Comparison between the effects of forskolin and calcitonin on bone resorption and osteoclast morphology in vitro. Bone. 10:1989;377-387.
    • (1989) Bone , vol.10 , pp. 377-387
    • Lerner, U.H.1    Ransjo, M.2    Klaushofer, K.3    Horandner, H.4    Hoffmann, O.5    Czerwenka, E.6    Koller, K.7    Peterlik, M.8
  • 11
    • 0029825378 scopus 로고    scopus 로고
    • Calcitonin-induced changes in the cytoskeleton are mediated by a signal pathway associated with protein kinase A in osteoclasts
    • Suzuki H., Nakamura I., Takahashi N., Ikuhara T., Matsuzaki K., Isogai Y., Hori M., Suda T. Calcitonin-induced changes in the cytoskeleton are mediated by a signal pathway associated with protein kinase A in osteoclasts. Endocrinology. 137:1996;4685-4690.
    • (1996) Endocrinology , vol.137 , pp. 4685-4690
    • Suzuki, H.1    Nakamura, I.2    Takahashi, N.3    Ikuhara, T.4    Matsuzaki, K.5    Isogai, Y.6    Hori, M.7    Suda, T.8
  • 12
    • 0030069243 scopus 로고    scopus 로고
    • Physiological levels of calcitonin regulate the mouse osteoclast calcitonin receptor by a protein kinase Alpha-mediated mechanism
    • Wada S., Udagawa N., Nagata N., Martin T.J., Findlay D.M. Physiological levels of calcitonin regulate the mouse osteoclast calcitonin receptor by a protein kinase Alpha-mediated mechanism. Endocrinology. 137:1996;312-320.
    • (1996) Endocrinology , vol.137 , pp. 312-320
    • Wada, S.1    Udagawa, N.2    Nagata, N.3    Martin, T.J.4    Findlay, D.M.5
  • 13
    • 0028799760 scopus 로고
    • Downregulation of calcitonin receptor mRNA expression by calcitonin during human osteoclast-like cell differentiation
    • Takahashi S., Goldring S., Katz M., Hilsenbeck S., Williams R., Roodman G.D. Downregulation of calcitonin receptor mRNA expression by calcitonin during human osteoclast-like cell differentiation. J Clin Invest. 95:1995;167-171.
    • (1995) J Clin Invest , vol.95 , pp. 167-171
    • Takahashi, S.1    Goldring, S.2    Katz, M.3    Hilsenbeck, S.4    Williams, R.5    Roodman, G.D.6
  • 14
    • 0000809207 scopus 로고
    • Toxic Substances to Insects, Produced by Aspergillus ochraceus and Oopsra destructor
    • Kodaira Y. Toxic Substances to Insects, Produced by Aspergillus ochraceus and Oopsra destructor. Agr Biol Chem. 25:1961;261-262.
    • (1961) Agr Biol Chem , vol.25 , pp. 261-262
    • Kodaira, Y.1
  • 15
    • 0023184635 scopus 로고
    • Metabolites produced by alternaria brassicae, the black spot pathogen of canola. Part 1, the phytotoxic components
    • Ayer W.A., Pena-Rodriguez L.M. Metabolites produced by alternaria brassicae, the black spot pathogen of canola. Part 1, the phytotoxic components. J Nat Prod. 50:1987;400-407.
    • (1987) J Nat Prod , vol.50 , pp. 400-407
    • Ayer, W.A.1    Pena-Rodriguez, L.M.2
  • 17
    • 0032714454 scopus 로고    scopus 로고
    • Osteoblastic cells induce fusion and activation of osteoclasts through a mechanism independent of macrophage-colony-stimulating factor production
    • Takami M., Woo J.T., Nagai K. Osteoblastic cells induce fusion and activation of osteoclasts through a mechanism independent of macrophage-colony-stimulating factor production. Cell Tissue Res. 298:1999;327-334.
    • (1999) Cell Tissue Res , vol.298 , pp. 327-334
    • Takami, M.1    Woo, J.T.2    Nagai, K.3
  • 18
    • 0025184110 scopus 로고
    • Omega-Conotoxin GVIA and nifedipine inhibit the depolarizing action of the fungal metabolite, destruxin B on muscle from the tobacco budworm (Heliothis virescens)
    • Bradfisch G.A., Harmer S.L. omega-Conotoxin GVIA and nifedipine inhibit the depolarizing action of the fungal metabolite, destruxin B on muscle from the tobacco budworm (Heliothis virescens). Toxicon. 28:1990;1249-1254.
    • (1990) Toxicon , vol.28 , pp. 1249-1254
    • Bradfisch, G.A.1    Harmer, S.L.2
  • 19
    • 0035895229 scopus 로고    scopus 로고
    • In planta sequential hydroxylation and glycosylation of a fungal phytotoxin: Avoiding cell death and overcoming the fungal invader
    • Pedras M.S., Zaharia I.L., Gai Y., Zhou Y., Ward D.E. In planta sequential hydroxylation and glycosylation of a fungal phytotoxin avoiding cell death and overcoming the fungal invader . Proc Natl Acad Sci USA. 98:2001;747-752.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 747-752
    • Pedras, M.S.1    Zaharia, I.L.2    Gai, Y.3    Zhou, Y.4    Ward, D.E.5
  • 20
    • 0034726061 scopus 로고    scopus 로고
    • Comparison of the phytotoxic activity of the phytotoxin destruxin B and four natural analogs
    • Pedras M.S., Biesenthal C.J., Zaharia I.L. Comparison of the phytotoxic activity of the phytotoxin destruxin B and four natural analogs. Plant Sci. 156:2000;185-192.
    • (2000) Plant Sci , vol.156 , pp. 185-192
    • Pedras, M.S.1    Biesenthal, C.J.2    Zaharia, I.L.3
  • 21
    • 0026561816 scopus 로고
    • In vitro effect of fungal cyclodepsipeptides on leukemic cells: Study of destruxins A, B and E
    • Odier F., Vey A., Bureau J.P. In vitro effect of fungal cyclodepsipeptides on leukemic cells study of destruxins A, B and E . Biol Cell. 74:1992;267-271.
    • (1992) Biol Cell , vol.74 , pp. 267-271
    • Odier, F.1    Vey, A.2    Bureau, J.P.3
  • 22
    • 0021062258 scopus 로고
    • Cytotoxicity of cyclodepsipeptides on murine lymphocytes and on L 1210 leukemia cells
    • Morel E., Pais M., Turpin M., Guyot M. Cytotoxicity of cyclodepsipeptides on murine lymphocytes and on L 1210 leukemia cells. Biomed Pharmacother. 37:1983;184-185.
    • (1983) Biomed Pharmacother , vol.37 , pp. 184-185
    • Morel, E.1    Pais, M.2    Turpin, M.3    Guyot, M.4
  • 23
    • 0030965148 scopus 로고    scopus 로고
    • Suppressive effects of destruxin B on hepatitis B virus surface antigen gene expression in human hepatoma cells
    • Chen H.C., Chou C.K., Sun C.M., Yeh S.F. Suppressive effects of destruxin B on hepatitis B virus surface antigen gene expression in human hepatoma cells. Antiviral Res. 34:1997;137-144.
    • (1997) Antiviral Res , vol.34 , pp. 137-144
    • Chen, H.C.1    Chou, C.K.2    Sun, C.M.3    Yeh, S.F.4
  • 24
    • 0030569509 scopus 로고    scopus 로고
    • Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells
    • Yeh S.F., Pan W., Ong G.T., Chiou A.J., Chuang C.C., Chiou S.H., Wu S.H. Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells. Biochem Biophys Res Commun. 229:1996;65-72.
    • (1996) Biochem Biophys Res Commun , vol.229 , pp. 65-72
    • Yeh, S.F.1    Pan, W.2    Ong, G.T.3    Chiou, A.J.4    Chuang, C.C.5    Chiou, S.H.6    Wu, S.H.7
  • 25
    • 0028324558 scopus 로고
    • Suppressive effects of metabolites from Alternaria brassicaea on the hepatitis B surface antigen
    • Sun C.M., Chen H.C., Yeh S.F. Suppressive effects of metabolites from Alternaria brassicaea on the hepatitis B surface antigen. Planta Med. 60:1994;87-88.
    • (1994) Planta Med , vol.60 , pp. 87-88
    • Sun, C.M.1    Chen, H.C.2    Yeh, S.F.3
  • 28
    • 0034062795 scopus 로고    scopus 로고
    • Compactin suppresses bone resorption by inhibiting the fusion of prefusion osteoclasts and disrupting the actin ring in osteoclasts
    • Woo J.T., Kasai S., Stern P.H., Nagai K. Compactin suppresses bone resorption by inhibiting the fusion of prefusion osteoclasts and disrupting the actin ring in osteoclasts. J Bone Miner Res. 15:2000;650-662.
    • (2000) J Bone Miner Res , vol.15 , pp. 650-662
    • Woo, J.T.1    Kasai, S.2    Stern, P.H.3    Nagai, K.4
  • 31
    • 0345333706 scopus 로고    scopus 로고
    • Effects of destruxins, cyclic depsipeptide mycotoxins, on calcium balance and phosphorylation of intracellular proteins in lepidopteran cell lines
    • Dumas C., Matha V., Quiot J.M., Vey A. Effects of destruxins, cyclic depsipeptide mycotoxins, on calcium balance and phosphorylation of intracellular proteins in lepidopteran cell lines. Comp Biochem Physiol C. 114:1996;213-219.
    • (1996) Comp Biochem Physiol C , vol.114 , pp. 213-219
    • Dumas, C.1    Matha, V.2    Quiot, J.M.3    Vey, A.4
  • 33
    • 0035830615 scopus 로고    scopus 로고
    • Effects of efrapeptin and destruxin, metabolites of entomogenous fungi, on the hydrolytic activity of a vacuolar type ATPase identified on the brush border membrane vesicles of Galleria mellonella midgut and on plant membrane bound hydrolytic enzymes
    • Bandani A.R., Amiri B., Butt T.M., Gordon-Weeks R. Effects of efrapeptin and destruxin, metabolites of entomogenous fungi, on the hydrolytic activity of a vacuolar type ATPase identified on the brush border membrane vesicles of Galleria mellonella midgut and on plant membrane bound hydrolytic enzymes. Biochim Biophys Acta. 1510:2001;367-377.
    • (2001) Biochim Biophys Acta , vol.1510 , pp. 367-377
    • Bandani, A.R.1    Amiri, B.2    Butt, T.M.3    Gordon-Weeks, R.4
  • 34
  • 35
    • 0026643011 scopus 로고
    • Inhibition of the accumulation of lipid droplets in macrophage J774 by bafilomycin B1 and destruxin E
    • Naganuma S., Kuzuya N., Sakai K., Hasumi K., Endo A. Inhibition of the accumulation of lipid droplets in macrophage J774 by bafilomycin B1 and destruxin E. Biochim Biophys Acta. 1126:1992;41-48.
    • (1992) Biochim Biophys Acta , vol.1126 , pp. 41-48
    • Naganuma, S.1    Kuzuya, N.2    Sakai, K.3    Hasumi, K.4    Endo, A.5
  • 36
    • 0031929430 scopus 로고    scopus 로고
    • Destruxin-A4 chlorohydrin, a novel destruxin from fungus OS-F68576: Isolation, structure determination, and biological activity as an inducer of erythropoietin
    • Cai P., Smith D., Katz B., Pearce C., Venables D., Houck D. Destruxin-A4 chlorohydrin, a novel destruxin from fungus OS-F68576 isolation, structure determination, and biological activity as an inducer of erythropoietin . J Nat Prod. 61:1998;290-293.
    • (1998) J Nat Prod , vol.61 , pp. 290-293
    • Cai, P.1    Smith, D.2    Katz, B.3    Pearce, C.4    Venables, D.5    Houck, D.6
  • 37
    • 0032774207 scopus 로고    scopus 로고
    • Non-cyclic AMP-dependent, positive inotropic cyclodepsipeptides with negative chronotropy
    • Tsunoo A., Kamijo M. Non-cyclic AMP-dependent, positive inotropic cyclodepsipeptides with negative chronotropy. J Pharmacol Exp Ther. 290:1999;1006-1012.
    • (1999) J Pharmacol Exp Ther , vol.290 , pp. 1006-1012
    • Tsunoo, A.1    Kamijo, M.2
  • 39
    • 0028046746 scopus 로고
    • Blockade of osteoclast-mediated bone resorption through occupancy of the integrin receptor: A potential approach to the therapy of osteoporosis
    • Dresner-Pollak R., Rosenblatt M. Blockade of osteoclast-mediated bone resorption through occupancy of the integrin receptor a potential approach to the therapy of osteoporosis . J Cell Biochem. 56:1994;323-330.
    • (1994) J Cell Biochem , vol.56 , pp. 323-330
    • Dresner-Pollak, R.1    Rosenblatt, M.2
  • 40
    • 0027336839 scopus 로고
    • Herbimycin A, a pp60c-src tyrosine kinase inhibitor, inhibits osteoclastic bone resorption in vitro and hypercalcemia in vivo
    • Yoneda T., Lowe C., Lee C.H., Gutierrez G., Niewolna M., Williams P.J., Izbicka E., Uehara Y., Mundy G.R. Herbimycin A, a pp60c-src tyrosine kinase inhibitor, inhibits osteoclastic bone resorption in vitro and hypercalcemia in vivo. J Clin Invest. 91:1993;2791-2795.
    • (1993) J Clin Invest , vol.91 , pp. 2791-2795
    • Yoneda, T.1    Lowe, C.2    Lee, C.H.3    Gutierrez, G.4    Niewolna, M.5    Williams, P.J.6    Izbicka, E.7    Uehara, Y.8    Mundy, G.R.9
  • 41
    • 0028282668 scopus 로고
    • Evidence that c-src is involved in the process of osteoclastic bone resorption
    • Hall T.J., Schaeublin M., Missbach M. Evidence that c-src is involved in the process of osteoclastic bone resorption. Biochem Biophys Res Commun. 199:1994;1237-1244.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1237-1244
    • Hall, T.J.1    Schaeublin, M.2    Missbach, M.3
  • 42
    • 0032938495 scopus 로고    scopus 로고
    • Rac-GTPase, osteoclast cytoskeleton and bone resorption
    • Razzouk S., Lieberherr M., Cournot G. Rac-GTPase, osteoclast cytoskeleton and bone resorption. Eur J Cell Biol. 78:1999;249-255.
    • (1999) Eur J Cell Biol , vol.78 , pp. 249-255
    • Razzouk, S.1    Lieberherr, M.2    Cournot, G.3
  • 43
    • 0033930168 scopus 로고    scopus 로고
    • Protein geranylgeranylation is required for osteoclast formation, function, and survival: Inhibition by bisphosphonates and GGTI-298
    • Coxon F.P., Helfrich M.H., Van't Hof R., Sebti S., Ralston S.H., Hamilton A., Rogers M.J. Protein geranylgeranylation is required for osteoclast formation, function, and survival inhibition by bisphosphonates and GGTI-298 . J Bone Miner Res. 15:2000;1467-1476.
    • (2000) J Bone Miner Res , vol.15 , pp. 1467-1476
    • Coxon, F.P.1    Helfrich, M.H.2    Van't Hof, R.3    Sebti, S.4    Ralston, S.H.5    Hamilton, A.6    Rogers, M.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.