Phosphorylation of high- and low-molecular-mass atrial natriuretic peptide analogs by cyclic AMP-dependent protein kinase.

Abstract:

:Synthetic high- and low-molecular-mass atrial peptides were phosphorylated in vitro by cyclic AMP-dependent protein kinase and [32P]ATP. From a series of atrial peptide analogs, it was deduced that the amino acid sequence, Arg101-Ser104 of atriopeptin was required for optimal phosphorylation. Phosphorylated AP(99-126) was less potent than the parent atriopeptin in vasorelaxant activity and receptor-binding properties. These results indicate that the presence of a phosphate group at the N-terminus of AP(99-126) decreases the interaction of the peptide with its receptor and, as a consequence, decreases bioactivity. These observations are in contrast to those of Rittenhouse et al. [(1986) J. Biol. Chem. 261, 7607-7610] who reported that phosphorylation of AP(101-126) enhanced the stimulation of Na/K/Cl cotransport in cultured vascular smooth muscle cells.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Olins GM,Mehta PP,Blehm DJ,Patton DR,Zupec ME,Whipple DE,Tjoeng FS,Adams SP,Olins PO,Gierse JK

doi

10.1016/0014-5793(87)80478-7

subject

Has Abstract

pub_date

1987-11-30 00:00:00

pages

325-30

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)80478-7

journal_volume

224

pub_type

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