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Volumn 23, Issue 8, 2014, Pages 1013-1022

The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated

Author keywords

Angiogenesis; Ferritin; Intrinsically unstructured protein; Kininogen; Metal ions; Protein interaction

Indexed keywords

FERRITIN; HEAVY METAL; HIGH MOLECULAR WEIGHT KININOGEN; INTRINSICALLY DISORDERED PROTEIN;

EID: 84906860338     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2486     Document Type: Article
Times cited : (5)

References (61)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan D, Weinberg RA (2011) Hallmarks of cancer: The next generation. Cell 144:646-674.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 4
    • 0024579549 scopus 로고
    • Conformation of high molecular weight kininogen: Effects of kallikrein and factor XIA cleavage
    • Villanueva GB, Leung L, Bradford H, Colman RW (1989) Conformation of high molecular weight kininogen: effects of kallikrein and factor XIa cleavage. Biochem Biophys Res Commun 158:72-79.
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 72-79
    • Villanueva, G.B.1    Leung, L.2    Bradford, H.3    Colman, R.W.4
  • 5
    • 0034651013 scopus 로고    scopus 로고
    • Domain 5 of high molecular weight kininogen (kininostatin) down-regulates endothelial cell proliferation and migration and inhibits angiogenesis
    • Colman RW, Jameson BA, Lin Y, Johnson D, Mousa SA (2000) Domain 5 of high molecular weight kininogen (kininostatin) down-regulates endothelial cell proliferation and migration and inhibits angiogenesis. Blood 95: 543-550.
    • (2000) Blood , vol.95 , pp. 543-550
    • Colman, R.W.1    Jameson, B.A.2    Lin, Y.3    Johnson, D.4    Mousa, S.A.5
  • 6
    • 0033669311 scopus 로고    scopus 로고
    • Two-chain high molecular weight kininogen induces endothelial cell apoptosis and inhibits angiogenesis: Partial activity within domain 5
    • Zhang JC, Claffey K, Sakthivel R, Darzynkiewicz Z, Shaw DE, Leal J, Wang YC, Lu FM, McCrae KR (2000) Two-chain high molecular weight kininogen induces endothelial cell apoptosis and inhibits angiogenesis: partial activity within domain 5. FASEB J 14:2589-2600.
    • (2000) FASEB J , vol.14 , pp. 2589-2600
    • Zhang, J.C.1    Claffey, K.2    Sakthivel, R.3    Darzynkiewicz, Z.4    Shaw, D.E.5    Leal, J.6    Wang, Y.C.7    Lu, F.M.8    McCrae, K.R.9
  • 7
    • 0035572887 scopus 로고    scopus 로고
    • Kininostatin, an angiogenic inhibitor, inhibits proliferation and induces apoptosis of human endothelial cells
    • Guo YL, Wang S, Colman RW (2001) Kininostatin, an angiogenic inhibitor, inhibits proliferation and induces apoptosis of human endothelial cells. Arterioscler Thromb Vasc Biol 21:1427-1433.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1427-1433
    • Guo, Y.L.1    Wang, S.2    Colman, R.W.3
  • 8
    • 38949121713 scopus 로고    scopus 로고
    • The inhibition of tube formation in a collagen-fibrinogen, three-dimensional gel by cleaved kininogen (HKA) and HK domain 5 (D5) is dependent on SRC family kinases
    • Liu Y, Sainz IM, Wu Y, Pixley R, Espinola RG, Hassan S, Khan MM, Colman RW (2008) The inhibition of tube formation in a collagen-fibrinogen, three-dimensional gel by cleaved kininogen (HKa) and HK domain 5 (D5) is dependent on Src family kinases. Exp Cell Res 314:774- 788.
    • (2008) Exp Cell Res , vol.314 , pp. 774-788
    • Liu, Y.1    Sainz, I.M.2    Wu, Y.3    Pixley, R.4    Espinola, R.G.5    Hassan, S.6    Khan, M.M.7    Colman, R.W.8
  • 9
    • 52749088168 scopus 로고    scopus 로고
    • The inhibitory effect of HKA in endothelial cell tube formation is mediated by disrupting the UPA-UPAR complex and inhibiting its signaling and internalization
    • Liu Y, Cao DJ, Sainz IM, Guo YL, Colman RW (2008) The inhibitory effect of HKa in endothelial cell tube formation is mediated by disrupting the uPA-uPAR complex and inhibiting its signaling and internalization. Am J Physiol Cell Physiol 295:257-267.
    • (2008) Am J Physiol Cell Physiol , vol.295 , pp. 257-267
    • Liu, Y.1    Cao, D.J.2    Sainz, I.M.3    Guo, Y.L.4    Colman, R.W.5
  • 10
    • 0032577485 scopus 로고    scopus 로고
    • Human H-kininogen is a ferritin-binding protein
    • Torti SV, Torti FM (1998) Human H-kininogen is a ferritin-binding protein. J Biol Chem 273:13630-13635.
    • (1998) J Biol Chem , vol.273 , pp. 13630-13635
    • Torti, S.V.1    Torti, F.M.2
  • 12
    • 0036646141 scopus 로고    scopus 로고
    • Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release
    • Parthasarathy N, Torti SV, Torti FM (2002) Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release. Biochem J 365: 279-286.
    • (2002) Biochem J , vol.365 , pp. 279-286
    • Parthasarathy, N.1    Torti, S.V.2    Torti, F.M.3
  • 14
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes
    • Kakhlon O, Cabantchik ZI (2002) The labile iron pool: characterization, measurement, and participation in cellular processes. Free Radic Biol Med 33:1037-1046.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 16
    • 0024245282 scopus 로고
    • Mechanism of ferritin iron uptake: Activity of the h-chain and deletion mapping of the ferro-oxidase site A study of iron uptake and ferro-oxidase activity of human liver, recombinant h-chain ferritins, and of two h-chain deletion mutants
    • Levi S, Luzzago A, Cesareni G, Cozzi A, Franceschinelli F, Albertini A, Arosio P (1988) Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site. A study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants. J Biol Chem 263:18086-18092.
    • (1988) J Biol Chem , vol.263 , pp. 18086-18092
    • Levi, S.1    Luzzago, A.2    Cesareni, G.3    Cozzi, A.4    Franceschinelli, F.5    Albertini, A.6    Arosio, P.7
  • 18
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • Arosio P, Ingrassia R, Cavadini P (2009) Ferritins: A family of molecules for iron storage, antioxidation and more. Biochim Biophys Acta 1790:589-599.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 20
    • 67749120517 scopus 로고    scopus 로고
    • Process of accumulation of metal ions on the interior surface of apo-ferritin: Crystal structures of a series of apoferritins containing variable quantities of pd(II) ions
    • Ueno T, Abe M, Hirata K, Abe S, Suzuki M, Shimizu N, Yamamoto M, Takata M, Watanabe Y (2009) Process of accumulation of metal ions on the interior surface of apo-ferritin: crystal structures of a series of apoferritins containing variable quantities of Pd(II) ions. J Am Chem Soc 131:5094-5100.
    • (2009) J Am Chem Soc , vol.131 , pp. 5094-5100
    • Ueno, T.1    Abe, M.2    Hirata, K.3    Abe, S.4    Suzuki, M.5    Shimizu, N.6    Yamamoto, M.7    Takata, M.8    Watanabe, Y.9
  • 22
    • 0030823246 scopus 로고    scopus 로고
    • Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor
    • Colman RW, Pixley RA, Najamunnisa S, Yan W, Wang J, Mazar A, McCrae KR (1997) Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor. J Clin Invest 100:1481-1487.
    • (1997) J Clin Invest , vol.100 , pp. 1481-1487
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3    Yan, W.4    Wang, J.5    Mazar, A.6    McCrae, K.R.7
  • 23
    • 0028200808 scopus 로고
    • The shape of high molecular weight kininogen organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy
    • Weisel JW, Nagaswami C, Woodhead JL, DeLa Cadena RA, Page JD, Colman RW, (1994) The shape of high molecular weight kininogen. Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy. J Biol Chem 269:10100-10106.
    • (1994) J Biol Chem , vol.269 , pp. 10100-10106
    • Weisel, J.W.1    Nagaswami, C.2    Woodhead, J.L.3    Dela Cadena, R.A.4    Page, J.D.5    Colman, R.W.6
  • 24
    • 0026478716 scopus 로고
    • Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor
    • Habazettl J, Gondol D, Wiltscheck R, Otlewski J, Schleicher M, Holak TA (1992) Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor. Nature 359:855-858.
    • (1992) Nature , vol.359 , pp. 855-858
    • Habazettl, J.1    Gondol, D.2    Wiltscheck, R.3    Otlewski, J.4    Schleicher, M.5    Holak, T.A.6
  • 27
    • 0027241814 scopus 로고
    • Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
    • Fink AL, Calciano LJ, Goto Y, Nishimura M, Swedberg SA (1993) Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease. Protein Sci 2:1155-1160.
    • (1993) Protein Sci , vol.2 , pp. 1155-1160
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Nishimura, M.4    Swedberg, S.A.5
  • 28
    • 48449106792 scopus 로고    scopus 로고
    • The JPRED 3 secondary structure prediction server
    • Cole C, Barber JD, Barton GJ (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36:197-201.
    • (2008) Nucleic Acids Res , vol.36 , pp. 197-201
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 29
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti FM, Torti SV (2002) Regulation of ferritin genes and protein. Blood 99:3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 30
    • 0023926495 scopus 로고
    • The binding of high molecular weight kininogen to cultured human endothelial cells
    • van Iwaarden, F, de Groot, PG, Bouma, BN (1988) The binding of high molecular weight kininogen to cultured human endothelial cells. J Biol Chem 263:4698-4703.
    • (1988) J Biol Chem , vol.263 , pp. 4698-4703
    • Van Iwaarden, F.1    De Groot, P.G.2    Bouma, B.N.3
  • 31
    • 52249089383 scopus 로고    scopus 로고
    • The relative binding affinities of PDZ partners for CFTR: A biochemical basis for efficient endocytic recycling
    • Cushing PR, Fellows A, Villone D, Boisguerin P, Madden DR (2008) The relative binding affinities of PDZ partners for CFTR: A biochemical basis for efficient endocytic recycling. Biochemistry 47:10084- 10098.
    • (2008) Biochemistry , vol.47 , pp. 10084-10098
    • Cushing, P.R.1    Fellows, A.2    Villone, D.3    Boisguerin, P.4    Madden, D.R.5
  • 32
    • 78650663242 scopus 로고    scopus 로고
    • Fluorescence polarization (FP) assays for monitoring peptide-protein or nucleic acidprotein binding
    • Moerke NJ (2009) Fluorescence polarization (FP) assays for monitoring peptide-protein or nucleic acidprotein binding. Curr Protoc Chem Biol 1:1-15.
    • (2009) Curr Protoc Chem Biol , vol.1 , pp. 1-15
    • Moerke, N.J.1
  • 34
    • 84863628119 scopus 로고    scopus 로고
    • Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKA) on adhesion and survival signaling in endothelial cells
    • Tesfay L, Huhn AJ, Hatcher H, Torti FM, Torti SV (2012) Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells. PLoS One 7:e40030.
    • (2012) PLoS One , vol.7
    • Tesfay, L.1    Huhn, A.J.2    Hatcher, H.3    Torti, F.M.4    Torti, S.V.5
  • 36
    • 50049097448 scopus 로고    scopus 로고
    • Intrinsic disorder in scaffold proteins: Getting more from less
    • Cortese MS, Uversky VN, Dunker AK (2008) Intrinsic disorder in scaffold proteins: getting more from less. Prog Biophys Mol Biol 98:85-106.
    • (2008) Prog Biophys Mol Biol , vol.98 , pp. 85-106
    • Cortese, M.S.1    Uversky, V.N.2    Dunker, A.K.3
  • 43
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 44
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P (2005) The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 579:3346-3354.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 46
    • 84979198890 scopus 로고    scopus 로고
    • Iron deficiency is not associated with increased blood cadmium in infants
    • Park JH, Park S, Kim Y (2014) Iron deficiency is not associated with increased blood cadmium in infants. Ann Occup Environ Med 26:3.
    • (2014) Ann Occup Environ Med , vol.26 , pp. 3
    • Park, J.H.1    Park, S.2    Kim, Y.3
  • 47
    • 84885321061 scopus 로고    scopus 로고
    • Blood manganese concentration is elevated in infants with iron deficiency
    • Park S, Sim CS, Lee H, Kim Y (2013) Blood manganese concentration is elevated in infants with iron deficiency. Biol Trace Elem Res 155:184-189.
    • (2013) Biol Trace Elem Res , vol.155 , pp. 184-189
    • Park, S.1    Sim, C.S.2    Lee, H.3    Kim, Y.4
  • 51
    • 68949206278 scopus 로고    scopus 로고
    • Short communication: Bovine alpha-casein is a ferritin-binding protein and inhibitory factor of milk ferritin immunoassay
    • Sugawara G, Inoue R, Watanabe K, Ohtsuka H, Orino K (2009) Short communication: bovine alpha-casein is a ferritin-binding protein and inhibitory factor of milk ferritin immunoassay. J Dairy Sci 92:3810-3814.
    • (2009) J Dairy Sci , vol.92 , pp. 3810-3814
    • Sugawara, G.1    Inoue, R.2    Watanabe, K.3    Ohtsuka, H.4    Orino, K.5
  • 52
    • 83555165130 scopus 로고    scopus 로고
    • Heme-mediated binding of alpha-casein to ferritin: Evidence for preferential alphacasein binding to ferrous iron
    • Usami A, Tanaka M, Yoshikawa Y, Watanabe K, Ohtsuka H, Orino K, (2011) Heme-mediated binding of alpha-casein to ferritin: evidence for preferential alphacasein binding to ferrous iron. Biometals 24:1217-1224.
    • (2011) Biometals , vol.24 , pp. 1217-1224
    • Usami, A.1    Tanaka, M.2    Yoshikawa, Y.3    Watanabe, K.4    Ohtsuka, H.5    Orino, K.6
  • 54
    • 0028127053 scopus 로고
    • Alpha 2-macroglobulin: A ferritinbinding protein
    • Massover WH (1994) Alpha 2-macroglobulin: A ferritinbinding protein. Ann N Y Acad Sci 737:468-471.
    • (1994) Ann N Y Acad Sci , vol.737 , pp. 468-471
    • Massover, W.H.1
  • 55
    • 0027673430 scopus 로고
    • Fibrinogen as a ferritin-binding protein in horse plasma
    • Orino K, Yamamoto S, Watanabe K (1993) Fibrinogen as a ferritin-binding protein in horse plasma. J Vet Med Sci 55:785-787.
    • (1993) J Vet Med Sci , vol.55 , pp. 785-787
    • Orino, K.1    Yamamoto, S.2    Watanabe, K.3
  • 57
    • 0000195671 scopus 로고
    • Natural abundance N-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G, Ruben DJ (1980) Natural abundance N-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185-189.
    • (1980) Chem Phys Lett , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 59
    • 34249765651 scopus 로고
    • NMR view-A computer-program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA (1994) NMR view-a computer-program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 60
    • 0019217679 scopus 로고
    • A study of the mechanism of ferritin formation The effect of PH, ionic strength and temperature, inhibition by imidazole and kinetic analysis
    • Pagues E, Paques A, Crichton RR (1980) A study of the mechanism of ferritin formation. The effect of pH, ionic strength and temperature, inhibition by imidazole and kinetic analysis. Eur J Biochem 107:447-453.
    • (1980) Eur J Biochem , vol.107 , pp. 447-453
    • Pagues, E.1    Paques, A.2    Crichton, R.R.3
  • 61
    • 0030337874 scopus 로고    scopus 로고
    • Fluorescence anisotropy: Rapid, quantitative assay for protein- DNA and protein-protein interaction
    • Heyduk T, Ma Y, Tang H, Ebright RH (1996) Fluorescence anisotropy: rapid, quantitative assay for protein- DNA and protein-protein interaction. Methods Enzymol 274:492-503.
    • (1996) Methods Enzymol , vol.274 , pp. 492-503
    • Heyduk, T.1    Ma, Y.2    Tang, H.3    Ebright, R.H.4


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