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Characterization of multiple prohormone convertase PC1/3 transcripts in porcine ovary
G Dai1, S P Smeekens, D F Steiner
1Department of Obstetrics and Gynecology, Albert Einstein Medical Center, Philadelphia, PA 19141-3098, USA.
Biochimica Et Biophysica Acta
|October 17, 1995
Summary
Researchers isolated porcine prohormone convertase, PC1/3, cDNAs from sow ovaries. The analysis revealed a 753-amino acid precursor protein highly homologous to mammalian PC1/3, with variations in 3' untranslated regions.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Prohormone convertase 1/3 (PC1/3) is crucial for processing peptide hormones.
- Understanding species-specific variations in PC1/3 is important for comparative biology and potential therapeutic applications.
Purpose of the Study:
- To isolate and characterize complementary DNAs (cDNAs) encoding porcine prohormone convertase, PC1/3.
- To analyze the nucleotide sequence and predict the amino acid sequence of the porcine PC1/3 precursor.
- To investigate variations in the 3' untranslated regions of porcine PC1/3 transcripts.
Main Methods:
- Screening a pregnant sow ovary cDNA library using a mouse PC1/3 cDNA probe.
- Nucleotide sequencing of isolated cDNAs.
- Sequence homology analysis and identification of polyadenylation sites.
Main Results:
- Isolation of overlapping cDNAs encoding porcine PC1/3.
- Prediction of a 753-amino acid precursor protein with high homology (96-92%) to human, rat, and mouse PC1/3.
- Identification of five distinct polyadenylation sites, leading to length variations (40-440 bp) in the 3' untranslated regions.
Conclusions:
- The porcine PC1/3 precursor protein is highly conserved across mammalian species.
- Alternative polyadenylation significantly impacts the 3' untranslated regions of porcine PC1/3 transcripts.
- These findings contribute to the understanding of PC1/3 gene regulation and evolution in pigs.
