Structure and expression of the rat epididymal secretory protein I gene. An androgen-regulated member of the lipocalin superfamily with a rare splice donor site.

Abstract

The complete rat epididymal secretory protein I (ESP I) gene was isolated from a genomic library constructed in bacteriophage lambda Charon 4A. The complete nucleotide sequence of the gene and its immediate 5' and 3' flanking sequences were determined. Interesting features include the presence of a rare, but functional, splice donor site (...GC) and the presence of a putative androgen-receptor-binding element. A detailed analysis of ESP I regulation was carried out after castration and subsequent testosterone treatment, demonstrating the requirement for androgens. Efferent-duct ligation and cryptorchism, on the other hand, had no effect on the steady-state concentrations of ESP I transcripts. Comparison of the exon/intron organization of the ESP I gene with those of members of the lipocalin superfamily provides strong support for a common ancestral origin.

• Authors: M Girotti, R Jones, D C Emery, W Chia, L Hall
• Journal: The Biochemical journal (Biochem J) Vol. 281 ( Pt 1) Pg. 203-10 (Jan 01 1992) ISSN: 0264-6021 [Print] England
• PMID: 1731756 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Epididymal Secretory Proteins
• Metalloproteins
• Testicular Hormones
• Testosterone

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Epididymal Secretory Proteins
• Epididymis (drug effects, physiology)
• Exons
• Female
• Gene Expression Regulation (drug effects)
• Genes
• Genomic Library
• Male
• Metalloproteins (genetics)
• Molecular Sequence Data
• Multigene Family
• Orchiectomy
• RNA Splicing
• Rats
• Rats, Inbred Strains
• Restriction Mapping
• Sequence Homology, Nucleic Acid
• Testicular Hormones (genetics)
• Testosterone (pharmacology)