POSTTRANSLATIONAL PROCESSING OF PREPRO-UROTENSIN-II

被引：46

作者：

CONLON, JM ^{[1
]}

ARNOLDREED, D ^{[1
]}

BALMENT, RJ ^{[1
]}

机构：

[1] UNIV MANCHESTER,SCH BIOL SCI,DEPT PHYSIOL SCI,MANCHESTER M13 9PT,LANCS,ENGLAND

来源：

FEBS LETTERS | 1990年 / 266卷 / 1-2期

关键词：

Flounder urophysis; Post-translational processing; Urotensin II;

D O I：

10.1016/0014-5793(90)81500-N

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：37 / 40

页数：4

共 14 条

[1] THE USE OF PLASMA DESORPTION TIME-OF-FLIGHT MASS-SPECTROMETRY TO SCREEN FOR PRODUCTS OF PROHORMONE PROCESSING IN CRUDE TISSUE-EXTRACTS [J].