Abstract
The primary structure of a teleost prepro-urotensin II may be deduced from the nucleotide sequence of cloned DNA complementary to carp prepro-urotensin II mRNA but the pathway of post-translational processing of the precursor is unknown. In this study, we have isolated four peptides from an extract of flounder urophysis that are derived from prepro-urotensin II by proteolytic cleavage. The amino acid sequences of the peptides demonstrate that flounder prepro-urotensin II is cleaved at two monobasic processing sites (single arginine residues) to generate peptides with limited homology to carp prepro-urotensin II-(22-4l)-, -(42-87)- and -(88-110)-peptides. Cleavage at a tribasic residue processing site generates a urotensin II with the primary structure: Ala-Gly-Thr-Thr-Glu-Cys-Phe-Trp-Lys-Tyr-Cys-Val. Urotensin II-(4-12)-peptide represented a minor component in the extract.
| Original language | English |
|---|---|
| Pages (from-to) | 37-40 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 266 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published (in print/issue) - 18 Jun 1990 |
Funding
Acknowledgements: This work was supported in part by N.E.R.C. The authors wish to thank Dr P.C. Andrews, Department of Biochemistry, Purdue University, Indiana, USA for carrying out the mass spectrometry.
Keywords
- Flounder urophysis
- Post-translational processing
- Urotensin II