Post-translational processing of prepro-urotensin II

J. M. Conlon, D. Arnold-Reed, R. J. Balment

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)

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 languageEnglish
Pages (from-to)37-40
Number of pages4
JournalFEBS Letters
Volume266
Issue number1-2
DOIs
Publication statusPublished - Jun 18 1990
Externally publishedYes

Keywords

  • Flounder urophysis
  • Post-translational processing
  • Urotensin II

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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