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 Lettjournal_title
FEBS lettersauthors
Olins GM,Mehta PP,Blehm DJ,Patton DR,Zupec ME,Whipple DE,Tjoeng FS,Adams SP,Olins PO,Gierse JKdoi
10.1016/0014-5793(87)80478-7subject
Has Abstractpub_date
1987-11-30 00:00:00pages
325-30issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(87)80478-7journal_volume
224pub_type
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