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Volumn 287, Issue 42, 2012, Pages 35341-35350

Clathrin pit-mediated endocytosis of neutrophil elastase and cathepsin G by cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

CANCER CELLS; CELL SURFACE RECEPTORS; CELL SURFACES; CHONDROITIN; CLATHRINS; DISSOCIATION CONSTANT; DYNAMIN; ELASTASE; ENDOSOMES; HEPARAN SULFATES; INTRACELLULAR SUBSTRATE; LUNG CANCER CELLS; PROTEOGLYCANS; SERINE PROTEINASE; SUBSTRATE SPECIFICITY; TUMOR CELLS;

EID: 84867407206     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.385617     Document Type: Article
Times cited : (47)

References (30)
  • 1
    • 0017262795 scopus 로고
    • Human leukocyte granule elastase: Rapid isolation and characterization
    • Baugh, R. J., and Travis, J. (1976) Human leukocyte granule elastase: rapid isolation and characterization. Biochemistry 15, 836-841
    • (1976) Biochemistry , vol.15 , pp. 836-841
    • Baugh, R.J.1    Travis, J.2
  • 2
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • DOI 10.1038/nm0598-615
    • Belaaouaj, A., McCarthy, R., Baumann, M., Gao, Z., Ley, T. J., Abraham, S. N., and Shapiro, S. D. (1998) Mice lacking neutrophil elastase reveal impaired host defense against Gram-negative bacterial sepsis. Nat. Med. 4, 615-618 (Pubitemid 28237363)
    • (1998) Nature Medicine , vol.4 , Issue.5 , pp. 615-618
    • Belaaouaj, A.1    Mccarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6    Shapiro, S.D.7
  • 3
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
    • Belaaouaj, A., Kim, K. S., and Shapiro, S. D. (2000) Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 289, 1185-1188
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.A.2    Shapiro, S.D.3
  • 4
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • DOI 10.1038/417091a
    • Weinrauch, Y., Drujan, D., Shapiro, S. D., Weiss, J., and Zychlinsky, A. (2002) Neutrophil elastase targets virulence factors of enterobacteria. Nature 417, 91-94 (Pubitemid 34498822)
    • (2002) Nature , vol.417 , Issue.6884 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 7
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002) Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 8
    • 0345708448 scopus 로고    scopus 로고
    • Neutrophil elastase cleaves PML-RARα and is important for the development of acute promyelocytic leukemia in mice
    • DOI 10.1016/S0092-8674(03)00852-3
    • Lane, A. A., and Ley, T. J. (2003) Neutrophil elastase cleaves PML-RARα and is important for the development of acute promyelocytic leukemia in mice. Cell 115, 305-318 (Pubitemid 37487704)
    • (2003) Cell , vol.115 , Issue.3 , pp. 305-318
    • Lane, A.A.1    Ley, T.J.2
  • 9
    • 0036724121 scopus 로고    scopus 로고
    • Neutrophil elastase induces mucin production by ligand-dependent epidermal growth factor receptor activation
    • Kohri, K., Ueki, I. F., and Nadel, J. A. (2002) Neutrophil elastase induces mucin production by ligand-dependent epidermal growth factor receptor activation. Am. J. Physiol. Lung Cell Mol. Physiol. 283, L531-540
    • (2002) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.283
    • Kohri, K.1    Ueki, I.F.A.2    Nadel, J.A.3
  • 12
    • 0017669252 scopus 로고
    • The induction of pulmonary emphysema with human leukocyte elastase
    • Senior, R. M., Tegner, H., Kuhn, C., Ohlsson, K., Starcher, B. C., and Pierce, J. A. (1977) The induction of pulmonary emphysema with human leukocyte elastase. Am. Rev. Respir. Dis. 116, 469-475 (Pubitemid 8181304)
    • (1977) American Review of Respiratory Disease , vol.116 , Issue.3 , pp. 469-475
    • Senior, R.M.1    Tegner, H.2    Kuhn, C.3
  • 13
    • 0030587118 scopus 로고    scopus 로고
    • Quantum Proteolysis Resulting from Release of Single Granules by Human Neutrophils: A Novel, Nonoxidative Mechanism of Extracellular Proteolytic Activity
    • Liou, T. G., and Campbell, E. J. (1996) Quantum proteolysis resulting from release of single granules by human neutrophils: a novel, nonoxidative mechanism of extracellular proteolytic activity. J. Immunol. 157, 2624-2631 (Pubitemid 126450478)
    • (1996) Journal of Immunology , vol.157 , Issue.6 , pp. 2624-2631
    • Liou, T.G.1    Campbell, E.J.2
  • 14
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, nonoxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen, C. A., Campbell, M. A., Sannes, P. L., Boukedes, S. S., and Campbell, E. J. (1995) Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, nonoxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131, 775-789
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.A.4    Campbell, E.J.5
  • 15
    • 34347271912 scopus 로고    scopus 로고
    • The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
    • DOI 10.1074/jbc.M608346200
    • Campbell, E. J., and Owen, C. A. (2007) The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G. J. Biol. Chem. 282, 14645-14654 (Pubitemid 47100453)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14645-14654
    • Campbell, E.J.1    Owen, C.A.2
  • 17
    • 79251493819 scopus 로고    scopus 로고
    • Insulin receptor substrate regulation of phosphoinositide 3-kinase
    • Metz, H. E., and Houghton, A. M. (2011) Insulin receptor substrate regulation of phosphoinositide 3-kinase. Clin. Cancer Res. 17, 206-211
    • (2011) Clin. Cancer Res. , vol.17 , pp. 206-211
    • Metz, H.E.1    Houghton, A.M.2
  • 20
    • 0032493727 scopus 로고    scopus 로고
    • Mutants of the CMP-sialic acid transporter causing the Lec2 phenotype
    • DOI 10.1074/jbc.273.32.20189
    • Eckhardt, M., Gotza, B., and Gerardy-Schahn, R. (1998) Mutants of the CMP-sialic acid transporter causing the Lec2 phenotype. J. Biol. Chem. 273, 20189-20195 (Pubitemid 28377579)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20189-20195
    • Eckhardt, M.1    Gotza, B.2    Gerardy-Schahn, R.3
  • 23
    • 0034635387 scopus 로고    scopus 로고
    • Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes
    • DOI 10.1074/jbc.275.6.3745
    • Rubino, M., Miaczynska, M., Lippé, R., and Zerial, M. (2000) Selective membrane recruitment of EEA-1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. J. Biol. Chem. 275, 3745-3748 (Pubitemid 30094593)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3745-3748
    • Rubino, M.1    Miaczynska, M.2    Lippe, R.3    Zerial, M.4
  • 24
    • 33646892646 scopus 로고    scopus 로고
    • Dynasore, a Cell-Permeable Inhibitor of Dynamin
    • DOI 10.1016/j.devcel.2006.04.002, PII S1534580706001638
    • Macia, E., Ehrlich, M., Massol, R., Boucrot, E., Brunner, C., and Kirchhausen, T. (2006) Dynasore, a cell-permeable inhibitor of dynamin. Dev. Cell 10, 839-850 (Pubitemid 43779110)
    • (2006) Developmental Cell , vol.10 , Issue.6 , pp. 839-850
    • Macia, E.1    Ehrlich, M.2    Massol, R.3    Boucrot, E.4    Brunner, C.5    Kirchhausen, T.6
  • 25
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • DOI 10.1083/jcb.200302028
    • Nabi, I. R., and Le, P. U. (2003) Caveolae/raft-dependent endocytosis. J. Cell Biol. 161, 673-677 (Pubitemid 36648749)
    • (2003) Journal of Cell Biology , vol.161 , Issue.4 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 26
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon, H. T., and Boucrot, E. (2011) Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 12, 517-533
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 517-533
    • McMahon, H.T.A.1    Boucrot, E.2
  • 27
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • DOI 10.1038/ncb1342, PII N1342
    • Glebov, O. O., Bright, N. A., and Nichols, B. J. (2006) Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat. Cell Biol. 8, 46-54 (Pubitemid 43064796)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 29
    • 0035027897 scopus 로고    scopus 로고
    • Cd150 (SLAM) is a receptor for measles virus but is not involved in viral contact-mediated proliferation inhibition
    • DOI 10.1128/JVI.75.10.4499-4505.2001
    • Erlenhoefer, C., Wurzer, W. J., Löffler, S., Schneider-Schaulies, S., ter Meulen, V., and Schneider-Schaulies, J. (2001) CD150 (SLAM) is a receptor for measles virus but is not involved in viral contact-mediated proliferation inhibition. J. Virol. 75, 4499-4505 (Pubitemid 32381492)
    • (2001) Journal of Virology , vol.75 , Issue.10 , pp. 4499-4505
    • Erlenhoefer, C.1    Wurzer, W.J.2    Loffler, S.3    Schneider-Schaulies, S.4    Ter, M.V.5    Schneider-Schaulies, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.