Post-translational processing of prepro-urotensin II.
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.
Conlon
J M
JM
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68178.
Arnold-Reed
D
D
Balment
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005432:Flounder; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D014579:Urotensins / Q000302:isolation & purification / Q000378:metabolism*
D010455:Peptides; D014579:Urotensins; C029677:urotensin II