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A novel Leydig cell cDNA-derived protein is a relaxin-like factor
1Department of Biochemistry and Molecular Biology Medical University of South Carolina, Charleston.
The Journal of Biological Chemistry
|July 7, 1995
Summary
Leydig cell insulin-like protein (LEY I-L) binds to relaxin receptors and enhances relaxin
Area of Science:
- Endocrinology and Reproductive Biology
- Molecular Endocrinology
- Protein Chemistry
Background:
- Leydig cells, crucial for testosterone production, express a gene for a novel protein within the insulin/relaxin family.
- This protein, termed Leydig cell insulin-like protein (LEY I-L), was identified based on its genetic message.
- Understanding LEY I-L's function is key to comprehending Leydig cell biology and potential endocrine roles.
Purpose of the Study:
- To synthesize human Leydig cell insulin-like protein (LEY I-L) based on its cDNA sequence.
- To investigate the potential target organs and biological activity of the synthesized LEY I-L.
- To determine if LEY I-L interacts with insulin or relaxin receptors and modulates their activity.
Main Methods:
- Chemical synthesis of human LEY I-L using the deduced amino acid sequence from published cDNA.
- Binding assays using crude membrane preparations from mouse uterus and brain.
- Receptor cross-reactivity studies with insulin and relaxin receptors.
- In vivo assessment of LEY I-L's effect on relaxin-mediated symphysis pubis widening in mice.
Main Results:
- Synthesized human LEY I-L specifically binds to membrane preparations of mouse uterus and brain.
- LEY I-L exhibits cross-reactivity with the relaxin receptor but not the insulin receptor.
- LEY I-L alone has no discernible effect, but it significantly potentiates relaxin-induced symphysis pubis widening.
Conclusions:
- Leydig cell insulin-like protein (LEY I-L) functions as a relaxin-like factor, not an insulin-like factor.
- LEY I-L's specific binding and interaction with the relaxin receptor suggest a role in relaxin signaling pathways.
- The potentiating effect of LEY I-L on relaxin activity indicates a novel mechanism for modulating reproductive tissue responses.