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FEBS Lett. 1990 Jun 18;266(1-2):37-40.

Post-translational processing of prepro-urotensin II.

Author information

1
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178.

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-(22-41)-, -(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.

PMID:
2365069
DOI:
10.1016/0014-5793(90)81500-n
[Indexed for MEDLINE]
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