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Relaxin: an insulin-related growth factor
Progress in Clinical and Biological Research
|January 1, 1979
Summary
Relaxin, an ovarian peptide, aids childbirth by altering birth canal tissues. Structural analysis reveals its similarity to insulin, suggesting a shared evolutionary origin and potential shared mechanisms of action.
Area of Science:
- Reproductive Biology
- Endocrinology
- Molecular Biology
Background:
- Relaxin is a crucial ovarian peptide released during parturition.
- It facilitates fetal delivery by modifying birth canal tissues.
- Previous research focused on its role in parturition.
Purpose of the Study:
- To investigate the structural relationship between relaxin and other hormones.
- To explore the evolutionary connections of relaxin.
- To hypothesize about relaxin's mechanism of action.
Main Methods:
- Detailed structural analysis of relaxin's polypeptide chains.
- Comparative sequence analysis with known hormones, particularly insulin.
- Three-dimensional structural modeling to assess sequence compatibility.
Main Results:
- Relaxin comprises two polypeptide chains linked by three disulfide bonds.
- Relaxin exhibits 25% sequence identity with insulin and shares a similar disulfide bond pattern.
- Relaxin's sequence integrates into insulin's 3D structure without major backbone distortion.
Conclusions:
- Relaxin is structurally related to insulin, indicating a shared ancestral gene.
- Relaxin joins nerve growth factor and insulin-like growth factor as insulin-related growth factors.
- This hormonal family may act via cell surface receptors and internalization.