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Volumn 97, Issue 4, 2008, Pages 1368-1385

The interaction of heparin/polyanions with bovine, porcine, and human growth hormone

Author keywords

Circular dichroism; Fluorescence; Growth hormone; Heparin; Isothermal titration calorimetry; Polyanion; Stability; Thermodynamics

Indexed keywords

DEXTRAN SULFATE; GROWTH HORMONE; HEPARIN; HUMAN GROWTH HORMONE; PHYTIC ACID; POLYANION; SODIUM CHLORIDE;

EID: 43249095250     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21056     Document Type: Article
Times cited : (22)

References (45)
  • 1
    • 0022721745 scopus 로고
    • Structural features of prolactins and growth hormones that can be related to their biological properties
    • Nicoll CS, Mayer GL, Russell SM. 1986. Structural features of prolactins and growth hormones that can be related to their biological properties. Endocr Rev 7:169-203.
    • (1986) Endocr Rev , vol.7 , pp. 169-203
    • Nicoll, C.S.1    Mayer, G.L.2    Russell, S.M.3
  • 2
    • 0025871852 scopus 로고
    • A heuristic approach to predicting the tertiary structure of bovine somatotropin
    • Carlacci L, Chou KC, Maggiora GM. 1991. A heuristic approach to predicting the tertiary structure of bovine somatotropin. Biochemistry 30:4389-4398.
    • (1991) Biochemistry , vol.30 , pp. 4389-4398
    • Carlacci, L.1    Chou, K.C.2    Maggiora, G.M.3
  • 4
    • 0028217202 scopus 로고
    • The crystal structure of affinity-matured human growth hormone at 2 A resolution
    • Ultsch MH, Somers W, Kossiakoff AA, de Vos AM. 1994. The crystal structure of affinity-matured human growth hormone at 2 A resolution. J Mol Biol 236:286-299.
    • (1994) J Mol Biol , vol.236 , pp. 286-299
    • Ultsch, M.H.1    Somers, W.2    Kossiakoff, A.A.3    de Vos, A.M.4
  • 6
    • 17644386823 scopus 로고    scopus 로고
    • Stabilization of soma-tropin by heparin
    • Zamiri C, Groves MJ. 2005. Stabilization of soma-tropin by heparin. J Pharm Pharmacol 57:555-564.
    • (2005) J Pharm Pharmacol , vol.57 , pp. 555-564
    • Zamiri, C.1    Groves, M.J.2
  • 7
    • 0027197880 scopus 로고
    • Effect of polyanions on the unfolding of acidic fibro-blast growth factor
    • Burke CJ, Volkin DB, Mach H, Middaugh CR. 1993. Effect of polyanions on the unfolding of acidic fibro-blast growth factor. Biochemistry 32:6419-6426.
    • (1993) Biochemistry , vol.32 , pp. 6419-6426
    • Burke, C.J.1    Volkin, D.B.2    Mach, H.3    Middaugh, C.R.4
  • 11
    • 0036784648 scopus 로고    scopus 로고
    • Stabilization of proteins by low molecular weight multiions
    • Maclean DS, Qian Q, Middaugh CR. 2002. Stabilization of proteins by low molecular weight multiions. J Pharm Sci 91:2220-2229.
    • (2002) J Pharm Sci , vol.91 , pp. 2220-2229
    • Maclean, D.S.1    Qian, Q.2    Middaugh, C.R.3
  • 15
    • 33645014175 scopus 로고    scopus 로고
    • A positively charged cluster in the epidermal growth factor-like domain of Factor VII-activating protease (FSAP) is essential for polyanion binding
    • Altincicek B, Shibamiya A, Trusheim H, Tzima E, Niepmann M, Linder D, Preissner KT, Kanse SM. 2006. A positively charged cluster in the epidermal growth factor-like domain of Factor VII-activating protease (FSAP) is essential for polyanion binding. Biochem J 394:687-692.
    • (2006) Biochem J , vol.394 , pp. 687-692
    • Altincicek, B.1    Shibamiya, A.2    Trusheim, H.3    Tzima, E.4    Niepmann, M.5    Linder, D.6    Preissner, K.T.7    Kanse, S.M.8
  • 16
    • 0021235057 scopus 로고
    • In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E
    • Hojima Y, Cochrane CG, Wiggins RC, Austen KF, Stevens RL. 1984. In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood 63:1453-1459.
    • (1984) Blood , vol.63 , pp. 1453-1459
    • Hojima, Y.1    Cochrane, C.G.2    Wiggins, R.C.3    Austen, K.F.4    Stevens, R.L.5
  • 18
    • 0347994109 scopus 로고    scopus 로고
    • Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles
    • Baerga-Ortiz A, Bergqvist S, Mandell JG, Komives EA. 2004. Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles. Protein Sci 13:166-176.
    • (2004) Protein Sci , vol.13 , pp. 166-176
    • Baerga-Ortiz, A.1    Bergqvist, S.2    Mandell, J.G.3    Komives, E.A.4
  • 19
    • 0036199093 scopus 로고    scopus 로고
    • Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions
    • Carneiro FA, Bianconi ML, Weissmuller G, Stauffer F, Da Poian AT. 2002. Membrane recognition by vesicular stomatitis virus involves enthalpy-driven protein-lipid interactions. J Virol 76:3756-3764.
    • (2002) J Virol , vol.76 , pp. 3756-3764
    • Carneiro, F.A.1    Bianconi, M.L.2    Weissmuller, G.3    Stauffer, F.4    Da Poian, A.T.5
  • 20
    • 0035979335 scopus 로고    scopus 로고
    • Kinetic and calorimetric evidence for two distinct scaffolding protein binding populations within the bacteriophage P22 procapsid
    • Parker MH, Brouillette CG, Prevelige PE, Jr. 2001. Kinetic and calorimetric evidence for two distinct scaffolding protein binding populations within the bacteriophage P22 procapsid. Biochemistry 40: 8962-8970.
    • (2001) Biochemistry , vol.40 , pp. 8962-8970
    • Parker, M.H.1    Brouillette, C.G.2    Prevelige Jr., P.E.3
  • 21
    • 0027363792 scopus 로고
    • Restricted mobility of the sole tryptophan in membrane-bound melittin
    • Chattopadhyay A, Rukmini R. 1993. Restricted mobility of the sole tryptophan in membrane-bound melittin. FEBS Lett 335:341-344.
    • (1993) FEBS Lett , vol.335 , pp. 341-344
    • Chattopadhyay, A.1    Rukmini, R.2
  • 22
    • 0036363969 scopus 로고    scopus 로고
    • The red-edge effects: 30 years of exploration
    • Demchenko AP. 2002. The red-edge effects: 30 years of exploration. Luminescence 17:19-42.
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 23
    • 0035824832 scopus 로고    scopus 로고
    • Dielectric relaxation in a single tryptophan protein
    • Ghose M, Mandal S, Roy D, Mandal RK, Basu G. 2001. Dielectric relaxation in a single tryptophan protein. FEBS Lett 509:337-340.
    • (2001) FEBS Lett , vol.509 , pp. 337-340
    • Ghose, M.1    Mandal, S.2    Roy, D.3    Mandal, R.K.4    Basu, G.5
  • 24
    • 0029841539 scopus 로고    scopus 로고
    • Tubulin conformation and dynamics: A red edge excitation shift study
    • Guha S, Rawat SS, Chattopadhyay A, Bhattacharyya B. 1996. Tubulin conformation and dynamics: A red edge excitation shift study. Biochemistry 35:13426-13433.
    • (1996) Biochemistry , vol.35 , pp. 13426-13433
    • Guha, S.1    Rawat, S.S.2    Chattopadhyay, A.3    Bhattacharyya, B.4
  • 25
    • 0031567108 scopus 로고    scopus 로고
    • Energetics of target peptide recognition by calmodulin: A calorimetric study
    • Wintrode PL, Privalov PL. 1997. Energetics of target peptide recognition by calmodulin: A calorimetric study. J Mol Biol 266:1050-1062.
    • (1997) J Mol Biol , vol.266 , pp. 1050-1062
    • Wintrode, P.L.1    Privalov, P.L.2
  • 26
    • 0024579448 scopus 로고
    • Interaction of heparin with human basic fibroblast growth factor: Protection of the angiogenic protein from proteolytic degradation by a glycosaminoglycan
    • Sommer A, Rifkin DB. 1989. Interaction of heparin with human basic fibroblast growth factor: Protection of the angiogenic protein from proteolytic degradation by a glycosaminoglycan. J Cell Physiol 138:215-220.
    • (1989) J Cell Physiol , vol.138 , pp. 215-220
    • Sommer, A.1    Rifkin, D.B.2
  • 28
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M. 2000. Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Cell 101:413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 29
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M. 1999. Structural basis for FGF receptor dimerization and activation. Cell 98:641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 31
    • 33745439311 scopus 로고    scopus 로고
    • The biological relevance of chemokine-proteoglycan interactions
    • Proudfoot AE. 2006. The biological relevance of chemokine-proteoglycan interactions. Biochem Soc Trans 34:422-426.
    • (2006) Biochem Soc Trans , vol.34 , pp. 422-426
    • Proudfoot, A.E.1
  • 32
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel TM, Johnson Z, Crown SE, Lau EK, Proudfoot AE. 2005. Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu Rev Biochem 74:385-410.
    • (2005) Annu Rev Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 35
    • 0042532200 scopus 로고    scopus 로고
    • Neshich G, Togawa RC, Mancini AL, Kuser PR, Yamagishi ME, Pappas G, Jr., Torres WV, Fonseca e Campos T, Ferreira LL, Luna FM, Oliveira AG, Miura RT, Inoue MK, Horita LG, de Souza DF, Dominiquini F, Alvaro A, Lima CS, Ogawa FO, Gomes GB, Palandrani JF, dos Santos GF, de Freitas EM, Mattiuz AE, Costa IC, de Almeida CL, Souza S, Baudet C, Higa RH. 2003. STING Millennium: A web-based suite of programs for comprehensive and simultaneous analysis of protein structure and sequence. Nucleic Acids Res 31:3386-3392.
    • Neshich G, Togawa RC, Mancini AL, Kuser PR, Yamagishi ME, Pappas G, Jr., Torres WV, Fonseca e Campos T, Ferreira LL, Luna FM, Oliveira AG, Miura RT, Inoue MK, Horita LG, de Souza DF, Dominiquini F, Alvaro A, Lima CS, Ogawa FO, Gomes GB, Palandrani JF, dos Santos GF, de Freitas EM, Mattiuz AE, Costa IC, de Almeida CL, Souza S, Baudet C, Higa RH. 2003. STING Millennium: A web-based suite of programs for comprehensive and simultaneous analysis of protein structure and sequence. Nucleic Acids Res 31:3386-3392.
  • 36
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos AM, Ultsch M, Kossiakoff AA. 1992. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science 255:306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • de Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 37
    • 0031057518 scopus 로고    scopus 로고
    • The role of receptor dimerization domain residues in growth hormone signaling
    • Chen C, Brinkworth R, Waters MJ. 1997. The role of receptor dimerization domain residues in growth hormone signaling. J Biol Chem 272: 5133-5140.
    • (1997) J Biol Chem , vol.272 , pp. 5133-5140
    • Chen, C.1    Brinkworth, R.2    Waters, M.J.3
  • 38
    • 0029319092 scopus 로고
    • Structure of the growth hormone-receptor complex and mechanism of receptor signaling
    • Kossiakoff AA. 1995. Structure of the growth hormone-receptor complex and mechanism of receptor signaling. J Nucl Med 36:14S-16S.
    • (1995) J Nucl Med , vol.36
    • Kossiakoff, A.A.1
  • 39
    • 0033226506 scopus 로고    scopus 로고
    • Molecular recognition events involved in the activation of the growth hormone receptor by growth hormone
    • Behncken SN, Waters MJ. 1999. Molecular recognition events involved in the activation of the growth hormone receptor by growth hormone. J Mol Recognit 12:355-362.
    • (1999) J Mol Recognit , vol.12 , pp. 355-362
    • Behncken, S.N.1    Waters, M.J.2
  • 40
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham BC, Ultsch M, De Vos AM, Mulkerrin MG, Clauser KR, Wells JA. 1991. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254:821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 42
    • 16544375435 scopus 로고    scopus 로고
    • The structural basis for biological signaling, regulation, and specificity in the growth hormone-prolactin system of hormones and receptors
    • Kossiakoff AA. 2004. The structural basis for biological signaling, regulation, and specificity in the growth hormone-prolactin system of hormones and receptors. Adv Protein Chem 68:147-169.
    • (2004) Adv Protein Chem , vol.68 , pp. 147-169
    • Kossiakoff, A.A.1
  • 43
    • 10344238099 scopus 로고    scopus 로고
    • The high- and low-affinity receptor binding sites of growth hormone are allosterically coupled
    • Walsh ST, Sylvester JE, Kossiakoff AA. 2004. The high- and low-affinity receptor binding sites of growth hormone are allosterically coupled. Proc Natl Acad Sci USA 101:17078-17083.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17078-17083
    • Walsh, S.T.1    Sylvester, J.E.2    Kossiakoff, A.A.3
  • 44
    • 0032570710 scopus 로고    scopus 로고
    • Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling
    • Rowlinson SW, Behncken SN, Rowland JE, Clarkson RW, Strasburger CJ, Wu Z, Baumbach W, Waters MJ. 1998. Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling. J Biol Chem 273:5307-5314.
    • (1998) J Biol Chem , vol.273 , pp. 5307-5314
    • Rowlinson, S.W.1    Behncken, S.N.2    Rowland, J.E.3    Clarkson, R.W.4    Strasburger, C.J.5    Wu, Z.6    Baumbach, W.7    Waters, M.J.8
  • 45
    • 9644260490 scopus 로고    scopus 로고
    • A conformationally sensitive GHR [growth hormone (GH) receptor] antibody: Impact on GH signaling and GHR proteolysis
    • Jiang J, Wang X, He K, Li X, Chen C, Sayeski PP, Waters MJ, Frank SJ. 2004. A conformationally sensitive GHR [growth hormone (GH) receptor] antibody: impact on GH signaling and GHR proteolysis. Mol Endocrinol 18:2981-2996.
    • (2004) Mol Endocrinol , vol.18 , pp. 2981-2996
    • Jiang, J.1    Wang, X.2    He, K.3    Li, X.4    Chen, C.5    Sayeski, P.P.6    Waters, M.J.7    Frank, S.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.