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Science 26 August 1977:
Vol. 197. no. 4306, pp. 914 - 915
DOI: 10.1126/science.887933
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Articles

Science, Vol 197, Issue 4306, 914-915
Copyright © 1977 by American Association for the Advancement of Science

articles

Relaxin: a disulfide homolog of insulin

C Schwabe and JK McDonald

Relaxin, a peptide hormone responsible for the widening of the birth canal in mammals, has been purified from the ovaries of pregnant hogs. The amino acid sequences of its constituent A and B chains were determined, and the positions of the disulfide cross-links were established. Relaxin was shown to be identical to insulin with respect to its disulfide bond distribution, but significant homology was lacking in other positions. These findings suggest that relaxin and insulin were derived from a common ancestral gene. Since the intrauterine mode of propagation is synonymous with the development of mammals, the genetic distance between insulin and relaxin should therefore permit an estimate of the earliest possible time of commitment of one evolutionary branch to the development of mammals. This event was estimated to have occurred about 5 X 10(8) years ago.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structure of the R3/I5 Chimeric Relaxin Peptide, a Selective GPCR135 and GPCR142 Agonist.
L. M. Haugaard-Jonsson, M. A. Hossain, N. L. Daly, R. A. D. Bathgate, J. D. Wade, D. J. Craik, and K. J. Rosengren (2008)
J. Biol. Chem. 283, 23811-23818
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The A-chain of Human Relaxin Family Peptides Has Distinct Roles in the Binding and Activation of the Different Relaxin Family Peptide Receptors.
M. A. Hossain, K. J. Rosengren, L. M. Haugaard-Jonsson, S. Zhang, S. Layfield, T. Ferraro, N. L. Daly, G. W. Tregear, J. D. Wade, and R. A. D. Bathgate (2008)
J. Biol. Chem. 283, 17287-17297
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International Union of Pharmacology LVII: Recommendations for the Nomenclature of Receptors for Relaxin Family Peptides..
R. A. Bathgate, R. Ivell, B. M. Sanborn, O. D. Sherwood, and R. J. Summers (2006)
Pharmacol. Rev. 58, 7-31
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Multiple Binding Sites Revealed by Interaction of Relaxin Family Peptides with Native and Chimeric Relaxin Family Peptide Receptors 1 and 2 (LGR7 and LGR8).
M. L. Halls, C. P. Bond, S. Sudo, J. Kumagai, T. Ferraro, S. Layfield, R. A. D. Bathgate, and R. J. Summers (2005)
J. Pharmacol. Exp. Ther. 313, 677-687
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INSL5 Is a High Affinity Specific Agonist for GPCR142 (GPR100).
C. Liu, C. Kuei, S. Sutton, J. Chen, P. Bonaventure, J. Wu, D. Nepomuceno, F. Kamme, D.-T. Tran, J. Zhu, et al. (2005)
J. Biol. Chem. 280, 292-300
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Regulation of DAF-2 receptor signaling by human insulin and ins-1, a member of the unusually large and diverse C. elegans insulin gene family.
S. B. Pierce, M. Costa, R. Wisotzkey, S. Devadhar, S. A. Homburger, A. R. Buchman, K. C. Ferguson, J. Heller, D. M. Platt, A. A. Pasquinelli, et al. (2001)
Genes & Dev. 15, 672-686
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The Relaxin Receptor-binding Site Geometry Suggests a Novel Gripping Mode of Interaction.
E. E. Bullesbach and C. Schwabe (2000)
J. Biol. Chem. 275, 35276-35280
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