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Phosphorylation of high‐ and low‐molecular‐mass atrial natriuretic peptide analogs by cyclic AMP‐dependent protein kinase
Author(s) -
Olins Gillian M.,
Mehta Pramod P.,
Blehm Delores J.,
Patton Dennis R.,
Zupec Mark E.,
Whipple Deborah E.,
Tjoeng Foe S.,
Adams Steven P.,
Olins Peter O.,
Gierse James K.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80478-7
Subject(s) - phosphorylation , peptide , atrial natriuretic peptide , npr2 , chemistry , molecular mass , receptor , protein kinase a , biochemistry , stimulation , peptide sequence , kinase , in vitro , peptide hormone , protein phosphorylation , natriuretic peptide , biology , medicine , endocrinology , enzyme , heart failure , gene
Synthetic high‐ and low‐molecular‐mass atrial peptides were phosphorylated in vitro by cyclic AMP‐dependent protein kinase and [ 32 P]ATP. From a series of atrial peptide analogs, it was deduced that the amino acid sequence, Arg 101 –Ser 104 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.