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Porcine relaxin: molecular cloning and cDNA structure
DNA (Mary Ann Liebert, Inc.)
|January 1, 1982
Summary
Researchers determined the nucleotide sequence for porcine relaxin, a pregnancy hormone. They identified the preprorelaxin coding region, revealing insights into hormone processing and the C-peptide
Area of Science:
- Molecular Biology
- Endocrinology
- Reproductive Biology
Background:
- Relaxin is a crucial peptide hormone produced during pregnancy to facilitate childbirth by softening pelvic ligaments and the cervix.
- Understanding the genetic basis of relaxin is essential for reproductive research and potential therapeutic applications.
Purpose of the Study:
- To determine the nucleotide sequence encoding porcine relaxin using recombinant DNA technology.
- To elucidate the structure and potential function of the relaxin precursor, preprorelaxin.
Main Methods:
- Isolation of total mRNA from pregnant pig ovaries and construction of a cDNA clone bank.
- Screening of clones using synthetic oligonucleotide primers specific to the porcine relaxin B chain.
- Nucleic acid sequence analysis of positive clones to identify the preprorelaxin coding region.
Main Results:
- A specific cDNA of approximately 300 nucleotides containing B chain and signal peptide sequences was identified.
- The complete preprorelaxin coding region was determined, including a signal peptide, B chain, a large C peptide, and an A chain.
- Sequence analysis revealed that prorelaxin processing likely involves chymotrypsin-like and trypsin-like enzymes.
- High homology was observed between porcine and rat preprorelaxin C regions, suggesting a functional role beyond disulfide bond formation.
Conclusions:
- The nucleotide sequence of porcine preprorelaxin has been successfully determined.
- The findings provide insights into the post-translational processing of relaxin and highlight the conserved nature of the C-peptide region across species.