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Volumn 6, Issue 11, 1997, Pages 2324-2335

Oxidation of apolipoprotein(a) inhibits kringle-associated lysine binding: The loss of intrinsic protein fluorescence suggests a role for tryptophan residues in the lysine binding site

Author keywords

Apolipoprotein(a); Essential tryptophans; Kringles; Lipoprotein(a); Lysine binding site affinities; Oxidation; Protein fluorescence

Indexed keywords

APOLIPOPROTEIN A; LIPOPROTEIN A; LYSINE; PROTEIN; TRYPTOPHAN;

EID: 0030711735     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061105     Document Type: Article
Times cited : (5)

References (51)
  • 1
    • 0025233989 scopus 로고
    • Heterogeneity of human lipoprotein Lp(a): Cytochemical and biochemical studies on the interaction of two Lp(a) species with the LDL receptor
    • Armstrong VW, Harrach B, Robenek H, Helmhold M, Walli AK, Seidel D. 1990. Heterogeneity of human lipoprotein Lp(a): Cytochemical and biochemical studies on the interaction of two Lp(a) species with the LDL receptor. J Lipid Res 31:429-441.
    • (1990) J Lipid Res , vol.31 , pp. 429-441
    • Armstrong, V.W.1    Harrach, B.2    Robenek, H.3    Helmhold, M.4    Walli, A.K.5    Seidel, D.6
  • 2
    • 0027288125 scopus 로고
    • Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin
    • Arni RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A. 1993. Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin. Biochemistry 32:4727-4737.
    • (1993) Biochemistry , vol.32 , pp. 4727-4737
    • Arni, R.K.1    Padmanabhan, K.2    Padmanabhan, K.P.3    Wu, T.P.4    Tulinsky, A.5
  • 3
    • 47649091099 scopus 로고
    • A new serum type system in man: The Lp(a) system
    • Berg K. 1963. A new serum type system in man: The Lp(a) system. Acta Pathol Microbiol Scand 59:369-382.
    • (1963) Acta Pathol Microbiol Scand , vol.59 , pp. 369-382
    • Berg, K.1
  • 5
    • 0026052923 scopus 로고
    • Lipoprotein(a) is a substrate for Factor XIIIa and tissue transglutaminase
    • Borth W, Chang V, Bishop P, Harpel PC. 1991. Lipoprotein(a) is a substrate for Factor XIIIa and tissue transglutaminase. J Biol Chem 266:18149-18153.
    • (1991) J Biol Chem , vol.266 , pp. 18149-18153
    • Borth, W.1    Chang, V.2    Bishop, P.3    Harpel, P.C.4
  • 8
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies KJA. 1987. Protein damage and degradation by oxygen radicals. I. General aspects. J Biol Chem 262:9895-9901.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 9
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies KJA, Delsignore ME, Lin SW. 1987. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J Biol Chem 262:9902-9907.
    • (1987) J Biol Chem , vol.262 , pp. 9902-9907
    • Davies, K.J.A.1    Delsignore, M.E.2    Lin, S.W.3
  • 10
    • 0025866654 scopus 로고
    • Free radical damage to proteins: The influence of the relative localization of radical generation, antioxidants, and target proteins
    • Dean RT, Hunt JV, Grant AJ, Yamamoto Y, Niki E. 1991. Free radical damage to proteins: The influence of the relative localization of radical generation, antioxidants, and target proteins. Free Radical Biology & Medicine 11:161-168.
    • (1991) Free Radical Biology & Medicine , vol.11 , pp. 161-168
    • Dean, R.T.1    Hunt, J.V.2    Grant, A.J.3    Yamamoto, Y.4    Niki, E.5
  • 11
    • 0016167076 scopus 로고
    • The direct linear plot. a new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal R, Comish-Bowden A. 1974. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem J 139:115-720.
    • (1974) Biochem J , vol.139 , pp. 115-720
    • Eisenthal, R.1    Comish-Bowden, A.2
  • 12
    • 0024584235 scopus 로고
    • A spectrophotometric assay for lipid peroxides in serum lipoproteins using a commercially available reagent
    • El-Saadani M, Esterbauer H, El-Sayed M, Goher M, Nassar AY, Jurgens G. 1989. A spectrophotometric assay for lipid peroxides in serum lipoproteins using a commercially available reagent. J Lipid Res 30:621-630.
    • (1989) J Lipid Res , vol.30 , pp. 621-630
    • El-Saadani, M.1    Esterbauer, H.2    El-Sayed, M.3    Goher, M.4    Nassar, A.Y.5    Jurgens, G.6
  • 13
    • 0028009959 scopus 로고
    • Polymorphic forms of Lp(a) with different structural and functional properties: Cold-induced self-association and binding to fibrin and lysine-Sepharose
    • Fless GM, Snyder ML. 1994. Polymorphic forms of Lp(a) with different structural and functional properties: Cold-induced self-association and binding to fibrin and lysine-Sepharose. Chem Phys Lipids 67/68:69-79.
    • (1994) Chem Phys Lipids , vol.67-68 , pp. 69-79
    • Fless, G.M.1    Snyder, M.L.2
  • 14
    • 0023129537 scopus 로고
    • Isolation and characterization of the two major apoproteins in human lipoprotein(a)
    • Gaubatz JW, Chari MV, Nava ML, Guyton JR, Morrisett JD. 1987. Isolation and characterization of the two major apoproteins in human lipoprotein(a). J Lipid Res 28:69-19.
    • (1987) J Lipid Res , vol.28 , pp. 69-119
    • Gaubatz, J.W.1    Chari, M.V.2    Nava, M.L.3    Guyton, J.R.4    Morrisett, J.D.5
  • 15
    • 0025289843 scopus 로고
    • Polymorphic forms of human apolipoprotein(a): Inheritance and relationship of their molecular weights to plasma levels of lipoprotein(a)
    • Gaubatz JW, Ghanem HI, Guevara J Jr, Nava ML, Patsch W, Morrisett JD. 1990. Polymorphic forms of human apolipoprotein(a): Inheritance and relationship of their molecular weights to plasma levels of lipoprotein(a). J Lipid Res 31:603-613.
    • (1990) J Lipid Res , vol.31 , pp. 603-613
    • Gaubatz, J.W.1    Ghanem, H.I.2    Guevara Jr., J.3    Nava, M.L.4    Patsch, W.5    Morrisett, J.D.6
  • 17
    • 0026486960 scopus 로고
    • Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein(a) to fibrin: A potential biochemical link between thrombosis, atherogenesis and sulfhydryl compound metabolism
    • Harpel PC, Chang VT, Borth W. 1992. Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein(a) to fibrin: A potential biochemical link between thrombosis, atherogenesis and sulfhydryl compound metabolism. Proc Natl Acad Sci USA 89:10193-10197.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10193-10197
    • Harpel, P.C.1    Chang, V.T.2    Borth, W.3
  • 18
    • 0012600414 scopus 로고
    • Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin
    • Harpel PC, Gordon BR, Parker TS. 1989. Plasmin catalyzes binding of lipoprotein (a) to immobilized fibrinogen and fibrin. Proc Natl Acad Sci USA 86:3847-3851.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3847-3851
    • Harpel, P.C.1    Gordon, B.R.2    Parker, T.S.3
  • 20
    • 0001585042 scopus 로고
    • Investigation of hydrogen bonding and proton transfer of aromatic alcohols in nonaqueous solvents by steady-state and time-resolved fluorescence
    • Hasselbacher CA, Waxman E, Galati LT, Contino PB, Ross JBA, Laws WR. 1991. Investigation of hydrogen bonding and proton transfer of aromatic alcohols in nonaqueous solvents by steady-state and time-resolved fluorescence. J Phys Chem 95:2995-3005.
    • (1991) J Phys Chem , vol.95 , pp. 2995-3005
    • Hasselbacher, C.A.1    Waxman, E.2    Galati, L.T.3    Contino, P.B.4    Ross, J.B.A.5    Laws, W.R.6
  • 21
    • 0028786755 scopus 로고
    • Multiple binding with identical linkage: A mechanism that explains the effect of lipoprotein(a) on fibrinolysis
    • Hervio L, Durlach V, Girard-Globa A, Angles-Cano E. 1995. Multiple binding with identical linkage: A mechanism that explains the effect of lipoprotein(a) on fibrinolysis. Biochemistry 34:13353-13358.
    • (1995) Biochemistry , vol.34 , pp. 13353-13358
    • Hervio, L.1    Durlach, V.2    Girard-Globa, A.3    Angles-Cano, E.4
  • 22
    • 0027772240 scopus 로고
    • Comparison of the lysine binding functions of lipoprotein(a) and plasminogen
    • Hoover-Plow JL, Miles LA, Fless GM, Scanu AM, Plow EF. 1993. Comparison of the lysine binding functions of lipoprotein(a) and plasminogen. Biochemistry 32:13681-13687.
    • (1993) Biochemistry , vol.32 , pp. 13681-13687
    • Hoover-Plow, J.L.1    Miles, L.A.2    Fless, G.M.3    Scanu, A.M.4    Plow, E.F.5
  • 23
    • 0026770852 scopus 로고
    • Multiple members of the plasminogen-apolipoprotein(a) gene family associated with thrombosis
    • Ichinose A. 1992. Multiple members of the plasminogen-apolipoprotein(a) gene family associated with thrombosis. Biochemistry 31:3113-3118.
    • (1992) Biochemistry , vol.31 , pp. 3113-3118
    • Ichinose, A.1
  • 24
    • 0030015524 scopus 로고    scopus 로고
    • Evidence that the fibrinogen binding domain of apo(a) is outside the lysine binding site of kringle IV-10
    • Klezovitch O, Edelstein C, Scanu AM. 1996. Evidence that the fibrinogen binding domain of apo(a) is outside the lysine binding site of kringle IV-10. J Clin Invest 98:185-191.
    • (1996) J Clin Invest , vol.98 , pp. 185-191
    • Klezovitch, O.1    Edelstein, C.2    Scanu, A.M.3
  • 25
    • 0029976013 scopus 로고    scopus 로고
    • Lys and fibrinogen binding of wild-type (Trp 72) and mutant (Arg 72) human apo(a) kringle IV-10 expressed in E. coli and CHO cells
    • Klezovitch O, Scanu A. 1996. Lys and fibrinogen binding of wild-type (Trp 72) and mutant (Arg 72) human apo(a) kringle IV-10 expressed in E. coli and CHO cells. Arterioscler Thromb Vasc Biol 16:392-398.
    • (1996) Arterioscler Thromb Vasc Biol , vol.16 , pp. 392-398
    • Klezovitch, O.1    Scanu, A.2
  • 26
    • 0025812777 scopus 로고
    • Apolipoprotein(a): Expression and characterization of a recombinant form of the protein in mammalian cells
    • Koschinsky ML, Tomlinson JE, Zioncheck TF, Schwartz K, Eaton DL, Lawn RM. 1991. Apolipoprotein(a): Expression and characterization of a recombinant form of the protein in mammalian cells. Biochemistry 30:5044-5051.
    • (1991) Biochemistry , vol.30 , pp. 5044-5051
    • Koschinsky, M.L.1    Tomlinson, J.E.2    Zioncheck, T.F.3    Schwartz, K.4    Eaton, D.L.5    Lawn, R.M.6
  • 27
    • 0026656766 scopus 로고
    • Lysine-binding heterogeneity of Lp(a): Consequences for fibrin binding and inhibition of plaminogen activation
    • Leerink CB, Duif P, Gimpel JA, Kortlandt W, Bouma BN, van Rijn HJM. 1992. Lysine-binding heterogeneity of Lp(a): Consequences for fibrin binding and inhibition of plaminogen activation. Thromb Haemostas 68:185-188.
    • (1992) Thromb Haemostas , vol.68 , pp. 185-188
    • Leerink, C.B.1    Duif, P.2    Gimpel, J.A.3    Kortlandt, W.4    Bouma, B.N.5    Van Rijn, H.J.M.6
  • 29
    • 0028590147 scopus 로고
    • Amino acid residues of the kringle-4 and kringle-5 domains of human plasminogen that stabilize their interactions with ω-amino acid ligands
    • McCance SG, Menhart N, Castellino FJ. 1994. Amino acid residues of the kringle-4 and kringle-5 domains of human plasminogen that stabilize their interactions with ω-amino acid ligands. J Biol Chem 269:32405-32410.
    • (1994) J Biol Chem , vol.269 , pp. 32405-32410
    • McCance, S.G.1    Menhart, N.2    Castellino, F.J.3
  • 31
    • 0021859293 scopus 로고
    • Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)
    • McMullen BA, Fujikawa K. 1985. Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J Biol Chem 260:5328-5341.
    • (1985) J Biol Chem , vol.260 , pp. 5328-5341
    • McMullen, B.A.1    Fujikawa, K.2
  • 32
    • 0029996089 scopus 로고    scopus 로고
    • Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: Existence of novel and expected binding modes
    • Mikol V, LoGrasso PV, Boettcher BR. 1996. Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: Existence of novel and expected binding modes. J Mol Biol 256:751-761.
    • (1996) J Mol Biol , vol.256 , pp. 751-761
    • Mikol, V.1    Lograsso, P.V.2    Boettcher, B.R.3
  • 33
    • 0024554547 scopus 로고
    • A potential basis for the thrombotic risks associated with lipoprotein(a)
    • Miles LA, Fless GM, Levin EG, Scanu AM, Plow EF. 1989. A potential basis for the thrombotic risks associated with lipoprotein(a). Nature 339:301-303.
    • (1989) Nature , vol.339 , pp. 301-303
    • Miles, L.A.1    Fless, G.M.2    Levin, E.G.3    Scanu, A.M.4    Plow, E.F.5
  • 34
    • 0025289037 scopus 로고
    • Lp(a): An interloper into the fibrinolytic system?
    • Miles LA, Plow EF. 1990. Lp(a): An interloper into the fibrinolytic system? Thromb Haemostas 65:331-335.
    • (1990) Thromb Haemostas , vol.65 , pp. 331-335
    • Miles, L.A.1    Plow, E.F.2
  • 36
    • 0026480941 scopus 로고
    • Oxidative modification of lipoprotein(a) and the effect of β-carotene
    • Naruszewicz M, Selinger E, Davignon J. 1992. Oxidative modification of lipoprotein(a) and the effect of β-carotene. Metabolism 41:1215-1224.
    • (1992) Metabolism , vol.41 , pp. 1215-1224
    • Naruszewicz, M.1    Selinger, E.2    Davignon, J.3
  • 37
    • 0025082043 scopus 로고
    • Free radical initiators as source of water- Or lipid-soluble peroxyl radicals
    • Niki E. 1990. Free radical initiators as source of water-or lipid-soluble peroxyl radicals. Methods Enzymol 186:100-108.
    • (1990) Methods Enzymol , vol.186 , pp. 100-108
    • Niki, E.1
  • 39
    • 0026723854 scopus 로고
    • Apolipoprotein(a) and plasminogen interactions with fibrin: A study with recombinant apolipoprotein(a) and isolated plasminogen fragments
    • Rouy D, Loschinsky ML, Fleury V, Chapman J, Angles-Cano E. 1992. Apolipoprotein(a) and plasminogen interactions with fibrin: A study with recombinant apolipoprotein(a) and isolated plasminogen fragments. Biochemistry 31:6333-6339.
    • (1992) Biochemistry , vol.31 , pp. 6333-6339
    • Rouy, D.1    Loschinsky, M.L.2    Fleury, V.3    Chapman, J.4    Angles-Cano, E.5
  • 40
    • 0027982357 scopus 로고
    • Apolipoprotein(a): Structural and functional consequences of mutations in kringle type 10 (or kringle 4-37)
    • Scanu AM, Edelstein C. 1994. Apolipoprotein(a): Structural and functional consequences of mutations in kringle type 10 (or kringle 4-37). Clinical Genetics 46:42-45.
    • (1994) Clinical Genetics , vol.46 , pp. 42-45
    • Scanu, A.M.1    Edelstein, C.2
  • 41
    • 0028948608 scopus 로고
    • Kringle-dependent structural and functional polymorphism of apolipoprotein(a)
    • Scanu AM, Edelstein C. 1995. Kringle-dependent structural and functional polymorphism of apolipoprotein(a). Biochem Biophys Acta 1256:1-12.
    • (1995) Biochem Biophys Acta , vol.1256 , pp. 1-12
    • Scanu, A.M.1    Edelstein, C.2
  • 43
    • 0027946694 scopus 로고
    • A single point mutation (Trp72-Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a)
    • Scanu AM, Pfaffinger D, Lee JC, Hinman J. 1994. A single point mutation (Trp72-Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a). Biochem Biophys Acta 1227:41-45.
    • (1994) Biochem Biophys Acta , vol.1227 , pp. 41-45
    • Scanu, A.M.1    Pfaffinger, D.2    Lee, J.C.3    Hinman, J.4
  • 46
    • 0000325568 scopus 로고
    • The primary structure of human plasminogen: Isolation ot two lysine-binding fragments and one "mini-" plasminogen (MW, 38,000) by elastase-catalyzed-specific limited proteolysis
    • Davidson JF, Rowan RM, Samama MM, Desnoyers PC, eds. New York: Raven Press
    • Sottrup-Jensen L, Claeys H, Zajdel M, Petersen TE, Magnusson S. 1978. The primary structure of human plasminogen: Isolation ot two lysine-binding fragments and one "mini-" plasminogen (MW, 38,000) by elastase-catalyzed-specific limited proteolysis. In: Davidson JF, Rowan RM, Samama MM, Desnoyers PC, eds. Progress in chemical fibrinolysis and thrombolysis. New York: Raven Press. pp 191-209.
    • (1978) Progress in Chemical Fibrinolysis and Thrombolysis , pp. 191-209
    • Sottrup-Jensen, L.1    Claeys, H.2    Zajdel, M.3    Petersen, T.E.4    Magnusson, S.5
  • 47
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. 1992. Protein oxidation and aging. Science 257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 49
    • 0024362630 scopus 로고
    • The mysteries of lipoprotein(a)
    • Utermann G. 1989. The mysteries of lipoprotein(a). Science 246:904-910.
    • (1989) Science , vol.246 , pp. 904-910
    • Utermann, G.1
  • 50
    • 0026333959 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • Witztum JL, Steinberg D. 1991. Role of oxidized low density lipoprotein in atherogenesis. J Clin Invest 88:1785-1792.
    • (1991) J Clin Invest , vol.88 , pp. 1785-1792
    • Witztum, J.L.1    Steinberg, D.2
  • 51
    • 0026360041 scopus 로고
    • The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4
    • Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM. 1991. The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4. Biochemistry 30:10586-10594.
    • (1991) Biochemistry , vol.30 , pp. 10586-10594
    • Wu, T.P.1    Padmanabhan, K.2    Tulinsky, A.3    Mulichak, A.M.4


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