메뉴 건너뛰기




Volumn 291, Issue 6, 2016, Pages 2917-2930

Biochemical and structural characterization of the interaction between the siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated lipocalin/lipocalin 2) and the N-terminal domain of its endocytic receptor SLC22A17

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84957991271     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.685644     Document Type: Article
Times cited : (41)

References (47)
  • 1
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacte-riostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz, D. H., and Holmes., M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., and Strong, R. K. (2002) The neutrophil lipocalin NGAL is a bacte-riostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10, 1033-1043
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 2
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T. H., and Smith., K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., and Aderem, A. (2004) Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432, 917-921
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6    Akira, S.7    Aderem, A.8
  • 4
    • 50249098214 scopus 로고    scopus 로고
    • The siderocalin/enterobactin interaction: A link between Mammalian immunity and bacterial iron transport
    • Abergel, R. J., and Clifton., M. C., Pizarro, J. C., Warner, J. A., Shuh, D. K., Strong, R. K., and Raymond, K. N. (2008) The siderocalin/enterobactin interaction: a link between mammalian immunity and bacterial iron transport. J. Am. Chem. Soc. 130, 11524-11534
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 11524-11534
    • Abergel, R.J.1    Clifton, M.C.2    Pizarro, J.C.3    Warner, J.A.4    Shuh, D.K.5    Strong, R.K.6    Raymond, K.N.7
  • 5
    • 33748051446 scopus 로고    scopus 로고
    • Microbial evasion of the immune system: Structural modifications of enterobactin impair siderocalin recognition
    • Abergel, R. J., and Moore., E. G., Strong, R. K., and Raymond, K. N. (2006) Microbial evasion of the immune system: structural modifications of enterobactin impair siderocalin recognition. J. Am. Chem. Soc. 128, 10998-10999
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10998-10999
    • Abergel, R.J.1    Moore, E.G.2    Strong, R.K.3    Raymond, K.N.4
  • 7
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy, L. R., Gazin, C., Zhu, X., and Green, M. R. (2005) A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 123, 1293-1305
    • (2005) Cell , vol.123 , pp. 1293-1305
    • Devireddy, L.R.1    Gazin, C.2    Zhu, X.3    Green, M.R.4
  • 9
    • 70349234521 scopus 로고    scopus 로고
    • Increased adipose tissue expression of lipocalin-2 in obesity is related to inflammation and matrix metalloproteinase-2 and metalloproteinase-9 activities in humans
    • Catalán, V., Gómez-Ambrosi, J., Rodríguez, A., Ramírez, B., Silva, C., Rotellar, F., Gil, M. J., Cienfuegos, J. A., Salvador, J., and Frühbeck, G. (2009) Increased adipose tissue expression of lipocalin-2 in obesity is related to inflammation and matrix metalloproteinase-2 and metalloproteinase-9 activities in humans. J. Mol. Med. 87, 803-813
    • (2009) J. Mol. Med. , vol.87 , pp. 803-813
    • Catalán, V.1    Gómez-Ambrosi, J.2    Rodríguez, A.3    Ramírez, B.4    Silva, C.5    Rotellar, F.6    Gil, M.J.7    Cienfuegos, J.A.8    Salvador, J.9    Frühbeck, G.10
  • 10
    • 73449084865 scopus 로고    scopus 로고
    • Mucosal lipocalin 2 has proinflammatory and iron-sequestering effects in response to bacterial enterobactin
    • Bachman, M. A., and Miller., V. L., and Weiser, J. N. (2009) Mucosal lipocalin 2 has proinflammatory and iron-sequestering effects in response to bacterial enterobactin. PLoS Pathog. 5, e1000622
    • (2009) PLoS Pathog , vol.5
    • Bachman, M.A.1    Miller, V.L.2    Weiser, J.N.3
  • 12
    • 58149291540 scopus 로고    scopus 로고
    • Lipocalin 2 promotes lung metastasis of murine breast cancer cells
    • Shi, H., Gu, Y., Yang, J., Xu, L., Mi, W., and Yu, W. (2008) Lipocalin 2 promotes lung metastasis of murine breast cancer cells. J. Exp. Clin. Cancer Res. 27, 83
    • (2008) J. Exp. Clin. Cancer Res. , vol.27 , pp. 83
    • Shi, H.1    Gu, Y.2    Yang, J.3    Xu, L.4    Mi, W.5    Yu, W.6
  • 13
    • 0026746638 scopus 로고
    • A 25-kDa α2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase
    • Triebel, S., Bläser, J., Reinke, H., and Tschesche, H. (1992) A 25-kDa α2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase. FEBS Lett. 314, 386-388
    • (1992) FEBS Lett , vol.314 , pp. 386-388
    • Triebel, S.1    Bläser, J.2    Reinke, H.3    Tschesche, H.4
  • 15
    • 77953690176 scopus 로고    scopus 로고
    • A Mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production
    • Devireddy, L. R., and Hart., D. O., Goetz, D. H., and Green, M. R. (2010) A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production. Cell 141, 1006-1017
    • (2010) Cell , vol.141 , pp. 1006-1017
    • Devireddy, L.R.1    Hart, D.O.2    Goetz, D.H.3    Green, M.R.4
  • 16
    • 0035800508 scopus 로고    scopus 로고
    • Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation
    • Devireddy, L. R., and Teodoro., J. G., Richard, F. A., and Green, M. R. (2001) Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation. Science 293, 829-834
    • (2001) Science , vol.293 , pp. 829-834
    • Devireddy, L.R.1    Teodoro, J.G.2    Richard, F.A.3    Green, M.R.4
  • 18
    • 84896039268 scopus 로고    scopus 로고
    • Differential transcytosis and toxicity of the hNGAL receptor ligands cadmium-metallothionein and cadmium-phytochelatin in colon-like caco-2 cells: Implications for in vivo cadmium toxicity
    • Langelueddecke, C, and Lee., W. K., and Thévenod, F. (2014) Differential transcytosis and toxicity of the hNGAL receptor ligands cadmium-metallothionein and cadmium-phytochelatin in colon-like Caco-2 cells: implications for in vivo cadmium toxicity. Toxicol. Lett. 226, 228-235
    • (2014) Toxicol. Lett , vol.226 , pp. 228-235
    • Langelueddecke, C.1    Lee, W.K.2    Thévenod, F.3
  • 19
    • 84855259370 scopus 로고    scopus 로고
    • Lipocalin-2 (24p3/neutrophil gelatinase-associated lipocalin (NGAL)) receptor is expressed in distal nephron and mediates protein endocytosis
    • Langelueddecke, C, Roussa, E., Fenton, R. A., Wolff, N. A., Lee, W. K., and Thévenod, F. (2012) Lipocalin-2 (24p3/neutrophil gelatinase-associated lipocalin (NGAL)) receptor is expressed in distal nephron and mediates protein endocytosis. J. Biol. Chem. 287, 159-169
    • (2012) J. Biol. Chem. , vol.287 , pp. 159-169
    • Langelueddecke, C.1    Roussa, E.2    Fenton, R.A.3    Wolff, N.A.4    Lee, W.K.5    Thévenod, F.6
  • 20
    • 84881086883 scopus 로고    scopus 로고
    • Expression and function of the lipocalin-2 (24p3/NGAL) receptor in rodent and human intestinal epithelia
    • Langelueddecke, C, Roussa, E., Fenton, R. A., and Thévenod, F. (2013) Expression and function of the lipocalin-2 (24p3/NGAL) receptor in rodent and human intestinal epithelia. PloS ONE 8, e71586
    • (2013) PloS ONE , vol.8
    • Langelueddecke, C.1    Roussa, E.2    Fenton, R.A.3    Thévenod, F.4
  • 22
    • 84875181483 scopus 로고    scopus 로고
    • The SLC22 family with transporters of organic cations, anions, and zwitterions
    • Koepsell, H. (2013) The SLC22 family with transporters of organic cations, anions, and zwitterions. Mol. Aspects Med. 34, 413-435
    • (2013) Mol. Aspects Med. , vol.34 , pp. 413-435
    • Koepsell, H.1
  • 23
    • 21944434991 scopus 로고    scopus 로고
    • Structure and function of renal organic cation transporters
    • Koepsell, H, Busch, A., Gorboulev, V., and Arndt, P. (1998) Structure and function of renal organic cation transporters. News Physiol. Sci 13, 11-16
    • (1998) News Physiol. Sci , vol.13 , pp. 11-16
    • Koepsell, H.1    Busch, A.2    Gorboulev, V.3    Arndt, P.4
  • 25
    • 84881258864 scopus 로고    scopus 로고
    • Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin
    • Kurzbach, D., Platzer, G., Schwarz, T. C, Henen, M. A., Konrat, R., and Hinderberger, D. (2013) Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin. Biochemistry 52, 5167-5175
    • (2013) Biochemistry , vol.52 , pp. 5167-5175
    • Kurzbach, D.1    Platzer, G.2    Schwarz, T.C.3    Henen, M.A.4    Konrat, R.5    Hinderberger, D.6
  • 26
    • 77749233830 scopus 로고    scopus 로고
    • Stem cell-specific activation of an ancestral myc protooncogene with conserved basic functions in the early metazoan hydra
    • Hartl, M., and Mitterstiller., A. M., Valovka, T., Breuker, K., Hobmayer, B., and Bister, K. (2010) Stem cell-specific activation of an ancestral myc protooncogene with conserved basic functions in the early metazoan Hydra. Proc. Natl. Acad. Sci. U.S.A. 107, 4051-4056
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 4051-4056
    • Hartl, M.1    Mitterstiller, A.M.2    Valovka, T.3    Breuker, K.4    Hobmayer, B.5    Bister, K.6
  • 27
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 29
    • 77955304413 scopus 로고    scopus 로고
    • Non-uniform frequency domain for optimal exploitation of non-uniform sampling
    • Kazimierczuk, K., Zawadzka-Kazimierczuk, A., and Kozmins̈ki, W. (2010) Non-uniform frequency domain for optimal exploitation of non-uniform sampling. J. Magn. Reson. 205, 286-292
    • (2010) J. Magn. Reson , vol.205 , pp. 286-292
    • Kazimierczuk, K.1    Zawadzka-Kazimierczuk, A.2    Kozmins̈ki, W.3
  • 30
    • 77951666994 scopus 로고    scopus 로고
    • Iterative algorithm of discrete fourier transform for processing randomly sampled NMR data sets
    • Stanek, J., and Kozmins̈ki, W. (2010) Iterative algorithm of discrete Fourier transform for processing randomly sampled NMR data sets. J. Biomol. NMR 47, 65-77
    • (2010) J. Biomol. NMR , vol.47 , pp. 65-77
    • Stanek, J.1    Kozmins̈ki, W.2
  • 31
    • 84863104592 scopus 로고    scopus 로고
    • High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
    • Zawadzka-Kazimierczuk, A., Kozmins̈ki, W., Sanderová, H., and Krásný, L. (2012) High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins. J. Biomol. NMR 52, 329-337
    • (2012) J. Biomol. NMR , vol.52 , pp. 329-337
    • Zawadzka-Kazimierczuk, A.1    Kozmins̈ki, W.2    Sanderová, H.3    Krásný, L.4
  • 32
    • 62149109695 scopus 로고    scopus 로고
    • Narrow peaks and high dimensionalities: Exploiting the advantages of random sampling
    • Kazimierczuk, K., Zawadzka, A., and Kozmins̈ki, W. (2009) Narrow peaks and high dimensionalities: exploiting the advantages of random sampling. J. Magn. Reson. 197, 219-228
    • (2009) J. Magn. Reson , vol.197 , pp. 219-228
    • Kazimierczuk, K.1    Zawadzka, A.2    Kozmins̈ki, W.3
  • 33
    • 33750998508 scopus 로고    scopus 로고
    • Random sampling of evolution time space and fourier transform processing
    • Kazimierczuk, K., Zawadzka, A., Kozmins̈ki, W., and Zhukov, I. (2006) Random sampling of evolution time space and Fourier transform processing. J. Biomol. NMR 36, 157-168
    • (2006) J. Biomol. NMR , vol.36 , pp. 157-168
    • Kazimierczuk, K.1    Zawadzka, A.2    Kozmins̈ki, W.3    Zhukov, I.4
  • 34
    • 84865654046 scopus 로고    scopus 로고
    • TSAR: A program for automatic resonance assignment using 2D crosssections of high dimensionality, high-resolution spectra
    • Zawadzka-Kazimierczuk, A., Kozmins̈ki, W., and Billeter, M. (2012) TSAR: a program for automatic resonance assignment using 2D crosssections of high dimensionality, high-resolution spectra. J. Biomol. NMR 54, 81-95
    • (2012) J. Biomol. NMR , vol.54 , pp. 81-95
    • Zawadzka-Kazimierczuk, A.1    Kozmins̈ki, W.2    Billeter, M.3
  • 38
    • 34548613879 scopus 로고    scopus 로고
    • Knockdown of endosomal/lysosomal divalent metal transporter 1 by RNA interference prevents cadmium-metallothionein-1 cytotoxicity in renal proximal tubule cells
    • Abouhamed, M., and Wolff., N. A., Lee, W. K., Smith, C. P., and Thévenod, F. (2007) Knockdown of endosomal/lysosomal divalent metal transporter 1 by RNA interference prevents cadmium-metallothionein-1 cytotoxicity in renal proximal tubule cells. Am. J. Physiol. Renal Physiol. 293, F705-F712
    • (2007) Am. J. Physiol. Renal Physiol , vol.293 , pp. F705-F712
    • Abouhamed, M.1    Wolff, N.A.2    Lee, W.K.3    Smith, C.P.4    Thévenod, F.5
  • 39
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D., and Duhr, S. (2010) Protein-binding assays in biological liquids using microscale thermophoresis. Nat. Commun. 1, 100
    • (2010) Nat. Commun , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 40
    • 33845917564 scopus 로고    scopus 로고
    • Why molecules move along a temperature gradient
    • Duhr, S., and Braun, D. (2006) Why molecules move along a temperature gradient. Proc. Natl. Acad. Sci. U.S.A. 103, 19678-19682
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 19678-19682
    • Duhr, S.1    Braun, D.2
  • 41
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., and Grimshaw., S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38, 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 42
    • 84885421330 scopus 로고    scopus 로고
    • Does electron capture dissociation cleave protein disulfide bonds?
    • Ganisl, B., and Breuker, K. (2012) Does electron capture dissociation cleave protein disulfide bonds? Chemistry Open 10.1002/open.201200038
    • (2012) Chemistry Open
    • Ganisl, B.1    Breuker, K.2
  • 43
    • 84866704850 scopus 로고    scopus 로고
    • Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins
    • Tamiola, K., and Mulder, F. A. (2012) Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins. Biochem. Soc. Trans. 40, 1014-1020
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1014-1020
    • Tamiola, K.1    Mulder, F.A.2
  • 44
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore, G. M., and Iwahara, J. (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem. Rev. 109, 4108-4139
    • (2009) Chem. Rev , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 46
    • 84921835922 scopus 로고    scopus 로고
    • Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR
    • Schneider, R., Maurin, D., Communie, G., Kragelj, J., and Hansen., D. F., Ruigrok, R. W., Jensen, M. R., and Blackledge, M. (2015) Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. J. Am. Chem. Soc. 137, 1220-1229
    • (2015) J. Am. Chem. Soc , vol.137 , pp. 1220-1229
    • Schneider, R.1    Maurin, D.2    Communie, G.3    Kragelj, J.4    Hansen, D.F.5    Ruigrok, R.W.6    Jensen, M.R.7    Blackledge, M.8
  • 47
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions
    • Tompa, P., and Fuxreiter, M. (2008) Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33, 2-8
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.