메뉴 건너뛰기




Volumn 287, Issue 49, 2012, Pages 41152-41164

Identification of key residues essential for the structural fold and receptor selectivity within the A-chain of human gene-2 (H2) relaxin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION MECHANISMS; BINDING MECHANISMS; CLINICAL TRIAL; COLLAGEN DEPOSITION; CROSS-REACTIVITY; DISULFIDE BONDS; HEART FAILURE; IN-PHASE; IN-VITRO; KEY RESIDUES; LEUCINE-RICH REPEATS; SECONDARY INTERACTIONS; TRANSMEMBRANES; TWO CHAINS;

EID: 84870365074     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.409284     Document Type: Article
Times cited : (18)

References (49)
  • 1
    • 0028091261 scopus 로고
    • Human relaxins. Chemistry and biology
    • Bryant-Greenwood, G. D., and Schwabe, C. (1994) Human relaxins. Chemistry and biology. Endocr. Rev. 15, 5-26
    • (1994) Endocr. Rev. , vol.15 , pp. 5-26
    • Bryant-Greenwood, G.D.1    Schwabe, C.2
  • 2
    • 79951599232 scopus 로고    scopus 로고
    • The relaxin peptide family. Structure, function, and clinical applications
    • Chan, L. J., Hossain, M. A., Samuel, C. S., Separovic, F., and Wade, J. D. (2011) The relaxin peptide family. Structure, function, and clinical applications. Protein Pept. Lett. 18, 220-229
    • (2011) Protein Pept. Lett. , vol.18 , pp. 220-229
    • Chan, L.J.1    Hossain, M.A.2    Samuel, C.S.3    Separovic, F.4    Wade, J.D.5
  • 4
    • 76849113368 scopus 로고    scopus 로고
    • Cardiovascular effects of relaxin. From basic science to clinical therapy
    • Du, X. J., Bathgate, R. A., Samuel, C. S., Dart, A. M., and Summers, R. J. (2010) Cardiovascular effects of relaxin. From basic science to clinical therapy. Nat. Rev. Cardiol. 7, 48-58
    • (2010) Nat. Rev. Cardiol. , vol.7 , pp. 48-58
    • Du, X.J.1    Bathgate, R.A.2    Samuel, C.S.3    Dart, A.M.4    Summers, R.J.5
  • 5
    • 65249190276 scopus 로고    scopus 로고
    • Relaxin for the treatment of patients with acute heart failure (Pre-RELAX-AHF). A multicentre, randomised, placebo-controlled, parallel-group, dose-finding phase IIb study
    • Teerlink, J. R., Metra, M., Felker, G. M., Ponikowski, P., Voors, A. A., Weatherley, B. D., Marmor, A., Katz, A., Grzybowski, J., Unemori, E., Teichman, S. L., and Cotter, G. (2009) Relaxin for the treatment of patients with acute heart failure (Pre-RELAX-AHF). A multicentre, randomised, placebo-controlled, parallel-group, dose-finding phase IIb study. Lancet 373, 1429-1439
    • (2009) Lancet , vol.373 , pp. 1429-1439
    • Teerlink, J.R.1    Metra, M.2    Felker, G.M.3    Ponikowski, P.4    Voors, A.A.5    Weatherley, B.D.6    Marmor, A.7    Katz, A.8    Grzybowski, J.9    Unemori, E.10    Teichman, S.L.11    Cotter, G.12
  • 6
    • 33644589069 scopus 로고    scopus 로고
    • International Union of Pharmacology LVII. Recommendations for the nomenclature of receptors for relaxin family peptides
    • Bathgate, R. A., Ivell, R., Sanborn, B. M., Sherwood, O. D., and Summers, R. J. (2006) International Union of Pharmacology LVII. Recommendations for the nomenclature of receptors for relaxin family peptides. Pharmacol. Rev. 58, 7-31
    • (2006) Pharmacol. Rev. , vol.58 , pp. 7-31
    • Bathgate, R.A.1    Ivell, R.2    Sanborn, B.M.3    Sherwood, O.D.4    Summers, R.J.5
  • 9
    • 0037424265 scopus 로고    scopus 로고
    • H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2
    • DOI 10.1074/jbc.M212457200
    • Sudo, S., Kumagai, J., Nishi, S., Layfield, S., Ferraro, T., Bathgate, R. A., and Hsueh, A. J. (2003) H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2. J. Biol. Chem. 278, 7855-7862 (Pubitemid 36800520)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7855-7862
    • Sudo, S.1    Kumagai, J.2    Nishi, S.3    Layfield, S.4    Ferraro, T.5    Bathgate, R.A.D.6    Hsueh, A.J.W.7
  • 10
    • 33845933437 scopus 로고    scopus 로고
    • Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules
    • DOI 10.1074/jbc.M602728200
    • Scott, D. J., Layfield, S., Yan, Y., Sudo, S., Hsueh, A. J., Tregear, G. W., and Bathgate, R. A. (2006) Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules. J. Biol. Chem. 281, 34942-34954 (Pubitemid 46036533)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 34942-34954
    • Scott, D.J.1    Layfield, S.2    Yan, Y.3    Sudo, S.4    Hsueh, A.J.W.5    Tregear, G.W.6    Bathgate, R.A.D.7
  • 11
    • 0034634628 scopus 로고    scopus 로고
    • The relaxin receptor-binding site geometry suggests a novel gripping mode of interaction
    • Büllesbach, E. E., and Schwabe, C. (2000) The relaxin receptor-binding site geometry suggests a novel gripping mode of interaction. J. Biol. Chem. 275, 35276-35280
    • (2000) J. Biol. Chem. , vol.275 , pp. 35276-35280
    • Büllesbach, E.E.1    Schwabe, C.2
  • 12
    • 17144426920 scopus 로고    scopus 로고
    • The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7
    • DOI 10.1074/jbc.M500030200
    • Büllesbach, E. E., and Schwabe, C. (2005) The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7. J. Biol. Chem. 280, 14051-14056 (Pubitemid 40517306)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14051-14056
    • Bullesbach, E.E.1    Schwabe, C.2
  • 15
    • 64549145456 scopus 로고    scopus 로고
    • Modeling the primary hormone-binding site of RXFP1 and RXFP2
    • Scott, D. J., Tregear, G. W., and Bathgate, R. A. (2009) Modeling the primary hormone-binding site of RXFP1 and RXFP2. Ann. N.Y. Acad. Sci. 1160, 74-77
    • (2009) Ann. N.Y. Acad. Sci. , vol.1160 , pp. 74-77
    • Scott, D.J.1    Tregear, G.W.2    Bathgate, R.A.3
  • 16
    • 77949568522 scopus 로고    scopus 로고
    • Membrane receptors. Structure and function of the relaxin family peptide receptors
    • Kong, R. C., Shilling, P. J., Lobb, D. K., Gooley, P. R., and Bathgate, R. A. (2010) Membrane receptors. Structure and function of the relaxin family peptide receptors. Mol. Cell. Endocrinol. 320, 1-15
    • (2010) Mol. Cell. Endocrinol. , vol.320 , pp. 1-15
    • Kong, R.C.1    Shilling, P.J.2    Lobb, D.K.3    Gooley, P.R.4    Bathgate, R.A.5
  • 17
    • 11244347812 scopus 로고    scopus 로고
    • Relaxin-3/insulin-like peptide 5 chimeric peptide, a selective ligand for G protein-coupled receptor (GPCR)135 and GPCR142 over leucine-rich repeat-containing G protein-coupled receptor 7
    • DOI 10.1124/mol.104.006700
    • Liu, C., Chen, J., Kuei, C., Sutton, S., Nepomuceno, D., Bonaventure, P., and Lovenberg, T. W. (2005) Relaxin-3/insulin-like peptide 5 chimeric peptide, a selective ligand for G protein-coupled receptor (GPCR)135 and GPCR142 over leucine-rich repeat-containing G protein-coupled receptor 7. Mol. Pharmacol. 67, 231-240 (Pubitemid 40069983)
    • (2005) Molecular Pharmacology , vol.67 , Issue.1 , pp. 231-240
    • Liu, C.1    Chen, J.2    Kuei, C.3    Sutton, S.4    Nepomuceno, D.5    Bonaventure, P.6    Lovenberg, T.W.7
  • 21
    • 84859806494 scopus 로고    scopus 로고
    • Chimeric relaxin peptides highlight the role of the A-chain in the function of H2 relaxin
    • Hossain, M. A., Wade, J. D., and Bathgate, R. A. (2012) Chimeric relaxin peptides highlight the role of the A-chain in the function of H2 relaxin. Peptides 35, 102-106
    • (2012) Peptides , vol.35 , pp. 102-106
    • Hossain, M.A.1    Wade, J.D.2    Bathgate, R.A.3
  • 22
    • 17644415042 scopus 로고    scopus 로고
    • LGR8 signal activation by the relaxin-like factor
    • DOI 10.1074/jbc.M414443200
    • Büllesbach, E. E., and Schwabe, C. (2005) LGR8 signal activation by the relaxin-like factor. J. Biol. Chem. 280, 14586-14590 (Pubitemid 40562802)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14586-14590
    • Bullesbach, E.E.1    Schwabe, C.2
  • 26
    • 57349180472 scopus 로고    scopus 로고
    • Simultaneous post-cysteine (S-Acm) group removal quenching of iodine and isolation of peptide by one step ether precipitation
    • Zhang, S., Lin, F., Hossain, M. A., Shabanpoor, F., Tregear, G. W., and Wade, J. D. (2008) Simultaneous post-cysteine (S-Acm) group removal quenching of iodine and isolation of peptide by one step ether precipitation. Int. J. Pept. Res. Ther. 14, 301-305
    • (2008) Int. J. Pept. Res. Ther. , vol.14 , pp. 301-305
    • Zhang, S.1    Lin, F.2    Hossain, M.A.3    Shabanpoor, F.4    Tregear, G.W.5    Wade, J.D.6
  • 28
    • 84859425760 scopus 로고    scopus 로고
    • Site-specific conjugation of a lanthanide chelator and its effects on the chemical synthesis and receptor binding affinity of human relaxin-2 hormone
    • Shabanpoor, F., Bathgate, R. A., Belgi, A., Chan, L. J., Nair, V. B., Wade, J. D., and Hossain, M. A. (2012) Site-specific conjugation of a lanthanide chelator and its effects on the chemical synthesis and receptor binding affinity of human relaxin-2 hormone. Biochem. Biophys. Res. Commun. 420, 253-256
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 253-256
    • Shabanpoor, F.1    Bathgate, R.A.2    Belgi, A.3    Chan, L.J.4    Nair, V.B.5    Wade, J.D.6    Hossain, M.A.7
  • 29
  • 30
    • 0028947365 scopus 로고
    • A colorimetric assay for measuring activation of Gs- and Gq-coupled signaling pathways
    • Chen, W., Shields, T. S., Stork, P. J., and Cone, R. D. (1995) A colorimetric assay for measuring activation of Gs- and Gq-coupled signaling pathways. Anal. Biochem. 226, 349-354
    • (1995) Anal. Biochem. , vol.226 , pp. 349-354
    • Chen, W.1    Shields, T.S.2    Stork, P.J.3    Cone, R.D.4
  • 31
    • 0025302162 scopus 로고
    • Relaxin modulates synthesis and secretion of procollagenase and collagen by human dermal fibroblasts
    • Unemori, E. N., and Amento, E. P. (1990) Relaxin modulates synthesis and secretion of procollagenase and collagen by human dermal fibroblasts. J. Biol. Chem. 265, 10681-10685
    • (1990) J. Biol. Chem. , vol.265 , pp. 10681-10685
    • Unemori, E.N.1    Amento, E.P.2
  • 32
    • 4344606223 scopus 로고    scopus 로고
    • Relaxin modulates cardiac fibroblast proliferation, differentiation, and collagen production and reverses cardiac fibrosis in vivo
    • DOI 10.1210/en.2004-0209
    • Samuel, C. S., Unemori, E. N., Mookerjee, I., Bathgate, R. A., Layfield, S. L., Mak, J., Tregear, G. W., and Du, X. J. (2004) Relaxin modulates cardiac fibroblast proliferation, differentiation, and collagen production and reverses cardiac fibrosis in vivo. Endocrinology 145, 4125-4133 (Pubitemid 39120561)
    • (2004) Endocrinology , vol.145 , Issue.9 , pp. 4125-4133
    • Samuel, C.S.1    Unemori, E.N.2    Mookerjee, I.3    Bathgate, R.A.D.4    Layfield, S.L.5    Mak, J.6    Tregear, G.W.7    Du, X.-J.8
  • 33
    • 24944542890 scopus 로고    scopus 로고
    • The antifibrotic effects of relaxin in human renal fibroblasts are mediated in part by inhibition of the Smad2 pathway
    • DOI 10.1111/j.1523-1755.2005.00384.x, PII 4494567
    • Heeg, M. H., Koziolek, M. J., Vasko, R., Schaefer, L., Sharma, K., Müller, G. A., and Strutz, F. (2005) The antifibrotic effects of relaxin in human renal fibroblasts are mediated in part by inhibition of the Smad2 pathway. Kidney Int. 68, 96-109 (Pubitemid 43181367)
    • (2005) Kidney International , vol.68 , Issue.1 , pp. 96-109
    • Heeg, M.H.J.1    Koziolek, M.J.2    Vasko, R.3    Schaefer, L.4    Sharma, K.5    Muller, G.A.6    Strutz, F.7
  • 34
    • 0033614998 scopus 로고    scopus 로고
    • Creation of human tumour cells with defined genetic elements
    • DOI 10.1038/22780
    • Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., and Weinberg, R. A. (1999) Creation of human tumour cells with defined genetic elements. Nature 400, 464-468 (Pubitemid 29361801)
    • (1999) Nature , vol.400 , Issue.6743 , pp. 464-468
    • Hahn, W.C.1    Counter, C.M.2    Lundberg, A.S.3    Beijersbergen, R.L.4    Brooks, M.W.5    Weinberg, R.A.6
  • 36
    • 77957281721 scopus 로고    scopus 로고
    • Antifibrotic properties of relaxin. In vivo mechanism of action in experimental renal tubulointerstitial fibrosis
    • Hewitson, T. D., Ho, W. Y., and Samuel, C. S. (2010) Antifibrotic properties of relaxin. In vivo mechanism of action in experimental renal tubulointerstitial fibrosis. Endocrinology 151, 4938-4948
    • (2010) Endocrinology , vol.151 , pp. 4938-4948
    • Hewitson, T.D.1    Ho, W.Y.2    Samuel, C.S.3
  • 37
    • 70350159176 scopus 로고    scopus 로고
    • Isoproterenol-induced myocardial injury and diastolic dysfunction in mice. Structural and functional correlates
    • Brooks, W. W., and Conrad, C. H. (2009) Isoproterenol-induced myocardial injury and diastolic dysfunction in mice. Structural and functional correlates. Comp. Med. 59, 339-343
    • (2009) Comp. Med. , vol.59 , pp. 339-343
    • Brooks, W.W.1    Conrad, C.H.2
  • 39
    • 60349084581 scopus 로고    scopus 로고
    • Determination of collagen content, concentration, and sub-types in kidney tissue
    • Samuel, C. S. (2009) Determination of collagen content, concentration, and sub-types in kidney tissue. Methods Mol. Biol. 466, 223-235
    • (2009) Methods Mol. Biol. , vol.466 , pp. 223-235
    • Samuel, C.S.1
  • 41
    • 0020648375 scopus 로고
    • 1H NMR spectra of polypeptides and proteins
    • 1H NMR spectra of polypeptides and proteins. Biopolymers 22, 131-138
    • (1983) Biopolymers , vol.22 , pp. 131-138
    • Wüthrich, K.1
  • 42
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects. J. Biomol. NMR 5, 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 45
    • 57649131054 scopus 로고    scopus 로고
    • Regulation of receptor signaling by relaxin A chain motifs. Derivation of panspecific and LGR7-specific human specific analogs
    • Park, J. I., Semyonov, J., Yi, W., Chang, C. L., and Hsu, S. Y. (2008) Regulation of receptor signaling by relaxin A chain motifs. Derivation of panspecific and LGR7-specific human specific analogs. J. Biol. Chem. 283, 32099-32109
    • (2008) J. Biol. Chem. , vol.283 , pp. 32099-32109
    • Park, J.I.1    Semyonov, J.2    Yi, W.3    Chang, C.L.4    Hsu, S.Y.5
  • 48
    • 79951731907 scopus 로고    scopus 로고
    • The roles of the A- And B-chains of human relaxin-2 and -3 on their biological activity
    • Hossain, M. A., and Wade, J. D. (2010) The roles of the A- and B-chains of human relaxin-2 and -3 on their biological activity. Curr. Protein Pept. Sci. 11, 719-724
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 719-724
    • Hossain, M.A.1    Wade, J.D.2
  • 49
    • 79951939642 scopus 로고    scopus 로고
    • H3 relaxin demonstrates antifibrotic properties via the RXFP1 receptor
    • Hossain, M. A., Man, B. C., Zhao, C., Xu, Q., Du, X. J., Wade, J. D., and Samuel, C. S. (2011) H3 relaxin demonstrates antifibrotic properties via the RXFP1 receptor. Biochemistry 50, 1368-1375
    • (2011) Biochemistry , vol.50 , pp. 1368-1375
    • Hossain, M.A.1    Man, B.C.2    Zhao, C.3    Xu, Q.4    Du, X.J.5    Wade, J.D.6    Samuel, C.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.