Relaxin and Related Peptides

Fifth International Conference, Volume 1160
1. Auflage 2009
ISBN: 978-1-57331-721-4
Verlag: Wiley

Buch, Englisch, 352 Seiten, Format (B × H): 175 mm x 251 mm, Gewicht: 839 g

Relaxin is a protein hormone, produced and secreted during pregnancy in mammalian species, having superficial structural features resembling those of insulin. Since its initial isolation from the ovaries of pregnant pigs in 1976, increasing interest in relaxin has led to increased understanding of the chemistry, synthesis, secretion, biological roles, mechanisms of action, and potential clinical applications of relaxin in humans and domestic animals.

In pigs, rats, and mice, relaxin promotes growth and softening of the cervix, enabling rapid and safe delivery of the fetuses. In these species relaxin also promotes growth and development of the mammary apparatus.

Recently, biological effects of relaxin in the heart, kidney, liver, and brain have been identified, and these discoveries have triggered additional interest in possible clinical applications for relaxin. In 2002, a second form of relaxin, which is found primarily in the brain, was discovered.

Relaxin-like factor (also called insulin 3), which was discovered in 1993, is produced in the fetal testis and plays a major role in testicular descent during development. The recent identification of the receptors for both relaxin and relaxin-like factor has enabled more rigorous studies of the target tissues and mechanisms of action of these hormones.

This volume contains a description of recent advances and future research and clinical possibilities in the field of relaxin and related peptides.

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Autoren/Hrsg.

Bryant-Greenwood, Gillian D

Bagnell, Carol A

Bathgate, Ross

Sherwood, O David

Fachgebiete

• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Klinische und Innere Medizin Endokrinologie
• Naturwissenschaften Biowissenschaften Tierkunde / Zoologie Tiergenetik, Reproduktion
• Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Vorklinische Medizin: Grundlagenfächer Biochemie (med.)

Inhaltsverzeichnis

Preface (G. Bryant-Greenwood).

Tribute. Bernard G. Steinetz, Jr.: A Most Tenacious Relaxinologist (O. David Sherwood).

Part I: Relaxin and Related Peptides: Structure and Function.

1. Structure and Activity in the Relaxin Family of Peptides (Geoffrey Tregear et al.).

2. The Chemical Synthesis of Relaxin and Related Peptides: A Historical Perspective (John D. Wade et al.).

3. De Novo Design and Synthesis of Cyclic and Linear Peptides to Mimic the Binding Cassette of Human Relaxin (Mohammed Akhter Hossain et al.).

4. Structural Insights into the Function of Relaxins (K.Johan Rosengren et al.).

5. Structural Properties of Relaxin Chimeras: NMR Characterization of the R3/I5 Relaxin Peptide (Linda Haugaard-Jonsson et al.).

6. Probing the Functional Domains of Relaxin-3 and the Creation of a Selective Antagonist for RXFP3/GPCR135 over Relaxin Receptor RXFP1/LGR7 (Changlu Liu et al.).

7. Degradation of Relaxin Family Peptides by Insulin-Degrading Enzyme (Robert Bennett et al.).

8. The Relationship between Relaxin Family Genes in Humans and Teleosts Revealed Through Bioinformatic Analyses and the Expression of Three RLN Genes in Teleosts Verified (Sergey Yegorov et al.).

Part II: Relaxin Family Receptors.

9. Structural Basis of Allosteric Ligand-Receptor Interactions in the Insulin/Relaxin Peptide Family: Implications for other receptor Tyrosine Kinases and G Protein-Coupled Receptors (Pierre De Meyts et al.).

10. Dimerization and Negative Cooperativity in the Relaxin Family Peptide (RXFP) Receptors (Angel Svendsen et al.).

11. Mechanism of Relaxin Receptor (LGR7/RXFP1) Expression and Function (Andras Kern et al.).

12. Resolving the Unconventional Mechanisms Underlying RXFP1 and RXFP2 Receptor Function (Brigham J. Hartley et al.).

13. Modeling the Primary Hormone Binding Site of RXFP1 and RXFP2 (Daniel Scott et al.).

14. Activation of Relaxin Related Receptors by Short, Linear Peptides Deriv

Über Autor(innen)

O. David Sherwood, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.

Phillip A. Fields, University of South Alabama, Mobile, Alabama, USA.

Bernard G. Steinetz, Nelson Institute of Environmental Science of New York University Medical Center, Tuxedo, New York, USA.