메뉴 건너뛰기




Volumn 35, Issue 1, 2012, Pages 102-106

Chimeric relaxin peptides highlight the role of the A-chain in the function of H2 relaxin

Author keywords

GPCR; Peptide; Relaxin; RXFP1

Indexed keywords

CHIMERIC PROTEIN; G PROTEIN COUPLED RECEPTOR; H1A RELAXIN; H2 RELAXIN; H2B RELAXIN; H3A RELAXIN; HUMAN GENE 2 RELAXIN; PEPTIDE DERIVATIVE; RELAXIN; RELAXIN FAMILY PEPTIDE RECEPTOR 1; RELAXIN FAMILY PEPTIDE RECEPTOR 2; UNCLASSIFIED DRUG;

EID: 84859806494     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2012.02.021     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 0031021409 scopus 로고    scopus 로고
    • Relaxin: A pleiotropic hormone
    • DOI 10.1016/S0306-3623(96)00171-1, PII S0306362396001711
    • Bani D. Relaxin: a pleiotropic hormone. General Pharmacology 1997;28:13-22. (Pubitemid 27016053)
    • (1997) General Pharmacology , vol.28 , Issue.1 , pp. 13-22
    • Bani, D.1
  • 2
    • 33644589069 scopus 로고    scopus 로고
    • International Union of Pharmacology LVII: Recommendations for the nomenclature of receptors for relaxin family peptides
    • Bathgate RA, Ivell R, Sanborn BM, Sherwood OD, Summers RJ. International Union of Pharmacology LVII: recommendations for the nomenclature of receptors for relaxin family peptides. Pharmacological Reviews 2006;58:7-31.
    • (2006) Pharmacological Reviews , vol.58 , pp. 7-31
    • Bathgate, R.A.1    Ivell, R.2    Sanborn, B.M.3    Sherwood, O.D.4    Summers, R.J.5
  • 6
    • 84884002531 scopus 로고    scopus 로고
    • Physiology and molecular biology of the relaxin peptide family
    • Knobil, Neill, editors. San Diego: Academic Press
    • Bathgate RAD, Hsueh AJW, Sherwood OD. Physiology and molecular biology of the relaxin peptide family. In: Knobil, Neill, editors. Physiology of reproduction. San Diego: Academic Press; 2006. p. 679-768.
    • (2006) Physiology of Reproduction , pp. 679-768
    • Bathgate, R.A.D.1    Hsueh, A.J.W.2    Sherwood, O.D.3
  • 7
    • 0023656067 scopus 로고
    • Relaxin structure. Quasi allosteric effect of the NH2-terminal A-chain helix
    • Bullesbach EE, Schwabe C. Relaxin structure. Quasi allosteric effect of the NH2-terminal A-chain helix. The Journal of Biological Chemistry 1987;262:12496-501.
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 12496-12501
    • Bullesbach, E.E.1    Schwabe, C.2
  • 8
    • 0025870325 scopus 로고
    • Total synthesis of human relaxin human relaxin derivatives by solid-phase peptide synthesis and site-directed chain combination
    • Bullesbach EE, Schwabe C. Total synthesis of human relaxin and human relaxin derivatives by solid-phase peptide synthesis and site-directed chain combination. The Journal of Biological Chemistry 1991;266:10754-61. (Pubitemid 21906868)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 10754-10761
    • Bullesbach, E.E.1    Schwabe, C.2
  • 9
    • 0034634628 scopus 로고    scopus 로고
    • The relaxin receptor-binding site geometry suggests a novel gripping mode of interaction
    • Bullesbach EE, Schwabe C. The relaxin receptor-binding site geometry suggests a novel gripping mode of interaction. The Journal of Biological Chemistry 2000;275:35276-80.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 35276-35280
    • Bullesbach, E.E.1    Schwabe, C.2
  • 10
    • 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
    • Bullesbach EE, Schwabe C. The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7. The Journal of Biological Chemistry 2005;280:14051-6. (Pubitemid 40517306)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14051-14056
    • Bullesbach, E.E.1    Schwabe, C.2
  • 11
    • 0026497638 scopus 로고
    • The receptor-binding site of human relaxin II. A dual prong-binding mechanism
    • Bullesbach EE, Yang S, Schwabe C. The receptor-binding site of human relaxin II. A dual prong-binding mechanism. The Journal of Biological Chemistry 1992;267:22957-60.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 22957-22960
    • Bullesbach, E.E.1    Yang, S.2    Schwabe, C.3
  • 13
    • 33744955536 scopus 로고    scopus 로고
    • Analogs of insulin-like peptide 3 (INSL3) B-chain are LGR8 antagonists in vitro and in vivo
    • DOI 10.1074/jbc.M600472200
    • Del Borgo MP, Hughes RA, Bathgate RA, Lin F, Kawamura K, Wade JD. Analogs of insulin-like peptide 3 (INSL3) B-chain are LGR8 antagonists in vitro and in vivo. The Journal of Biological Chemistry 2006;281:13068-74. (Pubitemid 43855216)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13068-13074
    • Del, B.M.P.1    Hughes, R.A.2    Bathgate, R.A.D.3    Lin, F.4    Kawamura, K.5    Wade, J.D.6
  • 14
    • 33748091739 scopus 로고    scopus 로고
    • Relaxin-a pleiotropic hormone and its emerging role for experimental and clinical therapeutics
    • DOI 10.1016/j.pharmthera.2006.03.004, PII S0163725806000416
    • Dschietzig T, Bartsch C, Baumann G, Stangl K. Relaxin - a pleiotropic hormone and its emerging role for experimental and clinical therapeutics. Pharmacology & Therapeutics 2006;112:38-56. (Pubitemid 44301484)
    • (2006) Pharmacology and Therapeutics , vol.112 , Issue.1 , pp. 38-56
    • Dschietzig, T.1    Bartsch, C.2    Baumann, G.3    Stangl, K.4
  • 17
    • 67650684255 scopus 로고    scopus 로고
    • Use of a temporary solubilizing peptide tag for the Fmoc solid-phase synthesis of human insulin glargine via use of regioselective disulfide bond formation
    • Hossain MA, Belgi A, Lin F, Zhang S, Shabanpoor F, Chan L, et al. Use of a temporary solubilizing peptide tag for the Fmoc solid-phase synthesis of human insulin glargine via use of regioselective disulfide bond formation. Bioconjugate Chemistry 2009;20:1390-6.
    • (2009) Bioconjugate Chemistry , vol.20 , pp. 1390-1396
    • Hossain, M.A.1    Belgi, A.2    Lin, F.3    Zhang, S.4    Shabanpoor, F.5    Chan, L.6
  • 18
    • 47749116027 scopus 로고    scopus 로고
    • The A-chain of human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors
    • Hossain MA, Rosengren KJ, Haugaard-Jonsson LM, Zhang S, Layfield S, Ferraro T, et al. The A-chain of human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors. The Journal of Biological Chemistry 2008;283:17287-97.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 17287-17297
    • Hossain, M.A.1    Rosengren, K.J.2    Haugaard-Jonsson, L.M.3    Zhang, S.4    Layfield, S.5    Ferraro, T.6
  • 20
    • 64149101159 scopus 로고    scopus 로고
    • Solid phase synthesis and structural analysis of novel A-chain dicarbaanalogs of human relaxin-3 (INSL7) that exhibit full biological activity
    • Hossain MA, Rosengren KJ, Zhang S, Bathgate RA, Tregear GW, van Lierop BJ, et al. Solid phase synthesis and structural analysis of novel A-chain dicarbaanalogs of human relaxin-3 (INSL7) that exhibit full biological activity. Organic & Biomolecular Chemistry 2009;7:1547-53.
    • (2009) Organic & Biomolecular Chemistry , vol.7 , pp. 1547-1553
    • Hossain, M.A.1    Rosengren, K.J.2    Zhang, S.3    Bathgate, R.A.4    Tregear, G.W.5    Van Lierop, B.J.6
  • 22
    • 79951731907 scopus 로고    scopus 로고
    • The roles of the A- And B-chains of human relaxin-2 and -3 on their biological activity
    • Hossain MA, Wade JD. The roles of the A- and B-chains of human relaxin-2 and -3 on their biological activity. Current Protein & Peptide Science 2010;11:719-24.
    • (2010) Current Protein & Peptide Science , vol.11 , pp. 719-724
    • Hossain, M.A.1    Wade, J.D.2
  • 26
    • 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, et al. 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. Molecular Pharmacology 2005;67:231-40. (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
  • 31
    • 0031796489 scopus 로고    scopus 로고
    • Fetal development of Leydig cell activity in the mouse is independent of pituitary gonadotroph function
    • DOI 10.1210/en.139.3.1141
    • O'Shaughnessy PJ, Baker P, Sohnius U, Haavisto AM, Charlton HM, Huhtaniemi I. Fetal development of Leydig cell activity in the mouse is independent of pituitary gonadotroph function. Endocrinology 1998;139:1141-6. (Pubitemid 28510133)
    • (1998) Endocrinology , vol.139 , Issue.3 , pp. 1141-1146
    • O'Shaughnessy, P.J.1    Baker, P.2    Sohnius, U.3    Haavisto, A.-M.4    Charlton, H.M.5    Huhtaniemi, I.6
  • 32
    • 57649131054 scopus 로고    scopus 로고
    • Regulation of receptor signaling by relaxin A chain motifs: Derivation of pan-specific and LGR7-specific human relaxin analogs
    • Park JI, Semyonov J, Yi W, Chang CL, Hsu SY. Regulation of receptor signaling by relaxin A chain motifs: derivation of pan-specific and LGR7-specific human relaxin analogs. The Journal of Biological Chemistry 2008;283:32099-109.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 32099-32109
    • Park, J.I.1    Semyonov, J.2    Yi, W.3    Chang, C.L.4    Hsu, S.Y.5
  • 33
    • 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 DJ, Layfield S, Yan Y, Sudo S, Hsueh AJ, Tregear GW, et al. Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules. The Journal of Biological Chemistry 2006;281:34942-54. (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
  • 36
    • 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 RA, et al. H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2. The Journal of Biological Chemistry 2003;278:7855-62. (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
  • 37
    • 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 JR, Metra M, Felker GM, Ponikowski P, Voors AA, Weatherley BD, et al. 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 2009;373:1429-39.
    • (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
  • 39
    • 77955661052 scopus 로고    scopus 로고
    • Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2
    • Zhang S, Hughes RA, Bathgate RA, Shabanpoor F, Hossain MA, Lin F, et al. Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2. Peptides 2010;31:1730-6.
    • (2010) Peptides , vol.31 , pp. 1730-1736
    • Zhang, S.1    Hughes, R.A.2    Bathgate, R.A.3    Shabanpoor, F.4    Hossain, M.A.5    Lin, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.