메뉴 건너뛰기




Volumn 1790, Issue 2, 2009, Pages 101-109

Binding of Silurus asotus lectin to Gb3 on Raji cells causes disappearance of membrane-bound form of HSP70

Author keywords

Burkitt's lymphoma cell; Catfish (Silurus asotus); Cholesterol rich microdomain; Globotriaosylceramide; Heat shock protein; Membrane bound form; Rhamnose binding lectin

Indexed keywords

GLOBOTRIAOSYLCERAMIDE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 70; LECTIN;

EID: 58149180102     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.10.005     Document Type: Article
Times cited : (20)

References (43)
  • 2
    • 0022976650 scopus 로고
    • Cellular and biochemical events in mammalian cells during and after recovery from physiological stress
    • Welch W.J., and Suhan J.P. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J. Cell Biol. 103 (1986) 2035-2052
    • (1986) J. Cell Biol. , vol.103 , pp. 2035-2052
    • Welch, W.J.1    Suhan, J.P.2
  • 3
    • 0026460892 scopus 로고
    • Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch W.J. Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease. Physiol. Rev. 72 (1992) 1063-1081
    • (1992) Physiol. Rev. , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 4
    • 11444263900 scopus 로고    scopus 로고
    • Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis
    • Bausero M.A., Page D.T., Osinaga E., and Asea A. Surface expression of Hsp25 and Hsp72 differentially regulates tumor growth and metastasis. Tumor Biol. 25 (2004) 243-251
    • (2004) Tumor Biol. , vol.25 , pp. 243-251
    • Bausero, M.A.1    Page, D.T.2    Osinaga, E.3    Asea, A.4
  • 6
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea A., Kraeft S.K., Kurt-Jones E.A., Stevenson M.A., Chen L.B., Finberg R.W., Koo G.C., and Calderwood S.K. HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine. Nat. Med. 6 (2000) 435-442
    • (2000) Nat. Med. , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 7
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T., Hartl F.U., and Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J. Cell Biol. 158 (2002) 1277-1285
    • (2002) J. Cell Biol. , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 8
    • 0037177825 scopus 로고    scopus 로고
    • Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4
    • Asea A., Rehli M., Kabingu E., Boch J.A., Bare O., Auron P.E., Stevenson M.A., and Calderwood S.K. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J. Biol. Chem. 277 (2002) 15028-15034
    • (2002) J. Biol. Chem. , vol.277 , pp. 15028-15034
    • Asea, A.1    Rehli, M.2    Kabingu, E.3    Boch, J.A.4    Bare, O.5    Auron, P.E.6    Stevenson, M.A.7    Calderwood, S.K.8
  • 10
    • 0037484291 scopus 로고    scopus 로고
    • Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release
    • Broquet A.H., Thomas G., Masliah J., Trugnan G., and Bachelet M. Expression of the molecular chaperone Hsp70 in detergent-resistant microdomains correlates with its membrane delivery and release. J. Biol. Chem. 278 (2003) 21601-21606
    • (2003) J. Biol. Chem. , vol.278 , pp. 21601-21606
    • Broquet, A.H.1    Thomas, G.2    Masliah, J.3    Trugnan, G.4    Bachelet, M.5
  • 12
    • 0035808322 scopus 로고    scopus 로고
    • The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids
    • Mamelak D., and Lingwood C. The ATPase domain of hsp70 possesses a unique binding specificity for 3′-sulfogalactolipids. J. Biol. Chem. 276 (2001) 449-456
    • (2001) J. Biol. Chem. , vol.276 , pp. 449-456
    • Mamelak, D.1    Lingwood, C.2
  • 13
    • 0002830651 scopus 로고
    • Egg lectins of invertebrates and lower vertebrates: properties and biological function
    • Krajhanzl A. Egg lectins of invertebrates and lower vertebrates: properties and biological function. Adv. Lectin Res. 3 (1990) 83-131
    • (1990) Adv. Lectin Res. , vol.3 , pp. 83-131
    • Krajhanzl, A.1
  • 14
    • 77956721412 scopus 로고    scopus 로고
    • The nonspecific immune system: humoral defense
    • Iwama G. (Ed), Academic Press, New York
    • Yano T. The nonspecific immune system: humoral defense. In: Iwama G. (Ed). Pathogen and Environment (1996), Academic Press, New York 105-157
    • (1996) Pathogen and Environment , pp. 105-157
    • Yano, T.1
  • 17
    • 0027366926 scopus 로고
    • Apoptosis induced in Burkitt's lymphoma cells via Gb3/CD77, a glycolipid antigen
    • Mangeney M., Lingwood C.A., Taga S., Caillou B., Tursz T., and Wiels J. Apoptosis induced in Burkitt's lymphoma cells via Gb3/CD77, a glycolipid antigen. Cancer Res. 53 (1993) 5314-5319
    • (1993) Cancer Res. , vol.53 , pp. 5314-5319
    • Mangeney, M.1    Lingwood, C.A.2    Taga, S.3    Caillou, B.4    Tursz, T.5    Wiels, J.6
  • 18
    • 0037192785 scopus 로고    scopus 로고
    • Expression of the Gb3/CD77 synthase gene in megakaryoblastic leukemia cells: implication in the sensitivity to verotoxins
    • Furukawa K., Yokoyama K., Sato T., Wiels J., Hirayama Y., Ohta M., and Furukawa K. Expression of the Gb3/CD77 synthase gene in megakaryoblastic leukemia cells: implication in the sensitivity to verotoxins. J. Biol. Chem. 277 (2002) 11247-11254
    • (2002) J. Biol. Chem. , vol.277 , pp. 11247-11254
    • Furukawa, K.1    Yokoyama, K.2    Sato, T.3    Wiels, J.4    Hirayama, Y.5    Ohta, M.6    Furukawa, K.7
  • 19
    • 18244384389 scopus 로고    scopus 로고
    • Catfish egg lectin causes rapid activation of multidrug resistance 1 P-glycoprotein as a lipid translocase
    • Sugawara S., Hosono M., Ogawa Y., Takayanagi M., and Nitta K. Catfish egg lectin causes rapid activation of multidrug resistance 1 P-glycoprotein as a lipid translocase. Biol. Pharm. Bull. 28 (2005) 434-441
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 434-441
    • Sugawara, S.1    Hosono, M.2    Ogawa, Y.3    Takayanagi, M.4    Nitta, K.5
  • 20
    • 24344485120 scopus 로고    scopus 로고
    • Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus)
    • Hosono M., Sugawara S., Ogawa Y., Kohno T., Takayanagi M., and Nitta K. Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus). Biochim. Biophys. Acta 1725 (2005) 160-173
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 160-173
    • Hosono, M.1    Sugawara, S.2    Ogawa, Y.3    Kohno, T.4    Takayanagi, M.5    Nitta, K.6
  • 22
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl
    • Martin S.J., Reutelingsperger C.P., McGahon A.J., Rader J.A., van Schie R.C., LaFace D.M., and Green D.R. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med. 182 (1995) 1545-1556
    • (1995) J. Exp. Med. , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    van Schie, R.C.5    LaFace, D.M.6    Green, D.R.7
  • 23
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled annexin V
    • Vermes I., Haanen C., Steffens-Nakken H., and Reutelingsperger C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled annexin V. J. Immunol. Methods 184 (1995) 39-51
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 24
    • 0142043395 scopus 로고    scopus 로고
    • Interaction of glycosphingolipids with signal transducers and membrane proteins in glycosphingolipid-enriched microdomains
    • Hakomori S., and Handa K. Interaction of glycosphingolipids with signal transducers and membrane proteins in glycosphingolipid-enriched microdomains. Methods Enzymol. 363 (2003) 191-207
    • (2003) Methods Enzymol. , vol.363 , pp. 191-207
    • Hakomori, S.1    Handa, K.2
  • 25
    • 0035114098 scopus 로고    scopus 로고
    • Serum heat shock protein and anti-heat shock protein antibody levels in aging
    • Rea I.M., McNerlan S., and Pockley A.G. Serum heat shock protein and anti-heat shock protein antibody levels in aging. Exp. Gerontol. 36 (2001) 341-352
    • (2001) Exp. Gerontol. , vol.36 , pp. 341-352
    • Rea, I.M.1    McNerlan, S.2    Pockley, A.G.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227 (1970) 680-685
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 2142654948 scopus 로고    scopus 로고
    • Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein
    • Wakasugi K., Nakano T., Kitatsuji C., and Morishima I. Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein. Biochem. Biophys. Res. Commun. 318 (2004) 453-460
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 453-460
    • Wakasugi, K.1    Nakano, T.2    Kitatsuji, C.3    Morishima, I.4
  • 29
    • 0026740788 scopus 로고
    • Extrajunctional distribution of N-cadherin in cultured human endothelial cells
    • Salomon D., Ayalon O., Patel-King R., Hynes R.O., and Geiger B. Extrajunctional distribution of N-cadherin in cultured human endothelial cells. J. Cell. Sci. 102 (1992) 7-17
    • (1992) J. Cell. Sci. , vol.102 , pp. 7-17
    • Salomon, D.1    Ayalon, O.2    Patel-King, R.3    Hynes, R.O.4    Geiger, B.5
  • 30
    • 0842291512 scopus 로고    scopus 로고
    • Inhibitory effect of heat shock protein 70 on apoptosis induced by photodynamic therapy in vitro
    • Nonaka M., Ikeda H., and Inokuchi T. Inhibitory effect of heat shock protein 70 on apoptosis induced by photodynamic therapy in vitro. Photochem. Photobiol. 79 (2004) 94-98
    • (2004) Photochem. Photobiol. , vol.79 , pp. 94-98
    • Nonaka, M.1    Ikeda, H.2    Inokuchi, T.3
  • 31
    • 4544250815 scopus 로고    scopus 로고
    • Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13
    • Toledo M.S., Suzuki E., Handa K., and Hakomori S. Cell growth regulation through GM3-enriched microdomain (glycosynapse) in human lung embryonal fibroblast WI38 and its oncogenic transformant VA13. J. Biol. Chem. 279 (2004) 34655-34664
    • (2004) J. Biol. Chem. , vol.279 , pp. 34655-34664
    • Toledo, M.S.1    Suzuki, E.2    Handa, K.3    Hakomori, S.4
  • 32
    • 11944262115 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits shrinkage-induced programmed cell death via mechanisms independent of effects on cell volume-regulatory membrane transport proteins
    • Nylandsted J., Jäättelä M., Hoffmann E.K., and Pedersen S.F. Heat shock protein 70 inhibits shrinkage-induced programmed cell death via mechanisms independent of effects on cell volume-regulatory membrane transport proteins. Pflugers Arch. 449 (2004) 175-185
    • (2004) Pflugers Arch. , vol.449 , pp. 175-185
    • Nylandsted, J.1    Jäättelä, M.2    Hoffmann, E.K.3    Pedersen, S.F.4
  • 33
    • 0028314945 scopus 로고
    • Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription
    • Sistonen L., Sarge K.D., and Morimoto R.I. Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription. Mol. Cell. Biol. 14 (1994) 2087-2099
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2087-2099
    • Sistonen, L.1    Sarge, K.D.2    Morimoto, R.I.3
  • 34
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • Arispe N., Doh M., Simakova O., Kurganov B., and De Maio A. Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J. 18 (2004) 1636-1645
    • (2004) FASEB J. , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 35
    • 0028953056 scopus 로고
    • A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells
    • Multhoff G., Botzler C., Wiesnet M., Muller E., Meier T., Wilmanns W., and Issels R.D. A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int. J. Cancer 61 (1995) 272-279
    • (1995) Int. J. Cancer , vol.61 , pp. 272-279
    • Multhoff, G.1    Botzler, C.2    Wiesnet, M.3    Muller, E.4    Meier, T.5    Wilmanns, W.6    Issels, R.D.7
  • 36
    • 0030022121 scopus 로고    scopus 로고
    • Induction of autologous tumor killing by heat treatment of fresh human tumor cells: involvement of gamma delta T cells and heat shock protein 70
    • Wei Y., Zhao X., Kariya Y., Fukata H., Teshigawara K., and Uchida A. Induction of autologous tumor killing by heat treatment of fresh human tumor cells: involvement of gamma delta T cells and heat shock protein 70. Cancer Res. 56 (1996) 1104-1110
    • (1996) Cancer Res. , vol.56 , pp. 1104-1110
    • Wei, Y.1    Zhao, X.2    Kariya, Y.3    Fukata, H.4    Teshigawara, K.5    Uchida, A.6
  • 37
    • 0034353117 scopus 로고    scopus 로고
    • HSP70 peptidembearing and peptide-negative preparations act as chaperokines
    • Asea A., Kabingu E., Stevenson M.A., and Calderwood S.K. HSP70 peptidembearing and peptide-negative preparations act as chaperokines. Cell Stress Chaperones 5 (2000) 425-431
    • (2000) Cell Stress Chaperones , vol.5 , pp. 425-431
    • Asea, A.1    Kabingu, E.2    Stevenson, M.A.3    Calderwood, S.K.4
  • 40
    • 44849084963 scopus 로고    scopus 로고
    • Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages
    • Vega V.L., Rodríguez-Silva M., Frey T., Gehrmann M., Diaz J.C., Steinem C., Multhoff G., Arispe N., and De Maio A. Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J. Immunol. 180 (2008) 4299-4307
    • (2008) J. Immunol. , vol.180 , pp. 4299-4307
    • Vega, V.L.1    Rodríguez-Silva, M.2    Frey, T.3    Gehrmann, M.4    Diaz, J.C.5    Steinem, C.6    Multhoff, G.7    Arispe, N.8    De Maio, A.9
  • 42
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler R., Zou J., and Voellmy R. Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1 (1996) 33-39
    • (1996) Cell Stress Chaperones , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.