Premium
Participation of adenosine 5′‐triphosphate in the activation of membrane‐bound guanylate cyclase by the atrial natriuretic factor
Author(s) -
Kurose Hitoshi,
Inagami Tadashi,
Ui Michio
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)80256-9
Subject(s) - gucy1b3 , gtp' , gucy1a3 , guanylate cyclase 2c , chemistry , cyclase , gucy2d , allosteric regulation , biochemistry , adenosine triphosphate , divalent , phosphorylation , enzyme , organic chemistry
The addition of ANF to Percoll‐purified liver plasma membranes produced a slight activation of guanylate cyclase; the ANF‐stimulated cyclase activity was further increased upon the addition of ATP to the enzyme assay mixture. The effect of ATP to potentiate the cyclase activation was concentration‐dependent, required Mg 2+ as a divalent cation, and was seen with membranes from various tissues and cells. ATP increased the maximal velocity of the cyclase without a change in the affinity for GTP or ANF. Phosphorylation by ATP might not be involved since ANF‐stimulated guanylate cyclase was enhanced by non‐phosphorylating ATP analogues as well. Thus, an allosteric ATP binding site is suggested to participate in ANF‐induced regulation of membrane‐bound guanylate cyclase.