Back to Search
Start Over
Full-length complementary DNA and the derived amino acid sequence of horse uteroglobin
- Source :
- Biology of reproduction. 66(6)
- Publication Year :
- 2002
-
Abstract
- After its original description as a steroid-dependent protein in the rabbit uterus, uteroglobin became one of the best characterized proteins. However, detailed knowledge of its physiological role remains an enigma. In this study we investigate how its structure is phylogenetically conserved in the horse compared to other mammalian species. Northern blot analysis showed that in horses, the main expression of uteroglobin appears in lung, uterus, and prostate tissues. Western blot analysis demonstrated that the dimeric form of uteroglobin is found predominantly in biological compartments. Using a RACE-PCR technique, we cloned and sequenced the full-length cDNA (473 base pairs) that encodes equine uteroglobin. The nucleotide sequence was shown to characterize the primary structure of this protein. This enabled us to add equine uteroglobin to a comparative amino acid alignment of 8 other uteroglobin molecules, and finally, to unravel 14 evolutionary completely conserved amino acids. We summarize these results with a computer-based 3-D model of horse uteroglobin, and discuss new concepts on the physiological role of uteroglobin, in particular as a specific binding protein.
- Subjects :
- Models, Molecular
DNA, Complementary
Base Sequence
Blotting, Western
Molecular Sequence Data
Sequence Analysis, DNA
Blotting, Northern
Polymerase Chain Reaction
Evolution, Molecular
Species Specificity
Animals
Humans
Uteroglobin
Computer Simulation
Amino Acid Sequence
Horses
Sequence Alignment
Conserved Sequence
Phylogeny
Subjects
Details
- ISSN :
- 00063363
- Volume :
- 66
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Biology of reproduction
- Accession number :
- edsair.pmid..........b787174444a43bb4f0be304cd7e3dbc8