Structural requirements of ATP for activation of basal and atrial natriuretic factor-stimulated guanylate cyclase in rat lung membranes

doi:10.1016/0922-4106(90)90122-E

European Journal of Pharmacology: Molecular Pharmacology

Volume 189, Issues 4–5, 30 October 1990, Pages 293-298

https://doi.org/10.1016/0922-4106(90)90122-E Get rights and content

Abstract

ATP has been reported to increase basal and atrial natriuretic factor (ANF)-stimulated guanylate cyclase activity. The structural features of ATP involved in the activation of guanylate cyclase were examined by employing a variety of ATP analogs with modification either at the phosphate chain or at the ribose moiety. Among the natural adenme nucleotides, ATP and ADP were able to increase both basal and ANF-stimulated guanylate cyclase activities in rat lung membranes. AMP had no effect, ATP was more effective than AMPPCP (the non-hydrolyzable analog of ATP), and ADP was more effective than ADPβS and AMPCP (the hydrolysis-resistant analogs of ADP) to increase basal and ANF-stimulated guanylate cyclase activities. Removal of the oxygen atom from the ribose moiety of ATP or ADP significantly reduced their potency. Thus, the length of the phosphate chain and the hydroxyl groups at the ribose moiety are both determinants for nucleotide mediated guanylate cyclase activation.

References (21)

C.-H. Chang et al.
Characterization of ATP-stimulated guanylate cyclase activation in rat lung membranes
Biochim. Biophys. Acta
(1990)
T. Inagami
Atrial natriuretic factor
J. Biol. Chem.
(1989)
T. Kuno et al.
Co-purification of an atrial natriuretic factor receptor and particulate guanylate cyclase from rat lung
J. Biol. Chem.
(1986)
H. Kurose et al.
Participation of adenosine 5′-triphosphate in the activation of membrane-bound guanylate cyclase by the atrial natriuretic factor
FEBS Lett.
(1987)
D.C. Leitman et al.
Atrial natriuretic peptide binding, cross-linking and stimulation of cyclic GMP accumulation and particulate guanylate cyclase activity in cultured cells
J. Biol. Chem.
(1986)
D.C. Leitman et al.
Atrial natriuretic factor receptor heterogeneity and stimulation of particulate guanylate cyclase and cyclic GMP accumulation
Endocrinol. Metab. Clin. N. Am.
(1987)
D.-L. Song et al.
Brain natriuretic factor: Augmentation of cellular cyclic GMP, activation of particulate guanylate cyclase and receptor binding
FEBS Lett.
(1988)
A.L. Steiner et al.
Radioimmunoassay for cyclic nucleotides: Preparation of antibodies and iodinated cyclic nucleotides
J. Biol. Chem.
(1972)
R. Takayanagi et al.
Two distinct forms of receptors for atrial natriuretic factor in bovine adrenocortical cells
J. Biol. Chem.
(1987)
J. Tremblay et al.
The increase of cGMP by atrial natriuretic factor correlates with the distribution of particulate guanylate cyclase
FEBS Lett.
(1985)

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Structural requirements of mastoparan for activation of membrane-bound guanylate cyclase
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Mastoparan activated membrane-bound guanylate cyclase and potentiated the effect of atrial natriuretic factor (ANF) and ATP on guanylate cyclase activity in rat lung membranes. Mastoparan is a cationic, amphiphilic tetradecapeptide with an amidated carboxyl terminus. It takes the α-helical conformation upon interacting with the membrane. Several analogs were synthetized to study the role of the positive charges, the carboxyl amino group and the α-helical conformation of mastoparan in the activation of guanylate cyclase. The results showed that substitution of the C-terminal amide group of mastoparan with a carboxyl group significantly reduced its potency on the activation of guanylate cyclase. Replacement of three lysine residues of mastoparan with aspartic acid or serine residues completely abolished the stimulatory effect of mastoparan. When the alanine at position 10 of mastoparan was substituted by a proline, the resulting analog had no effect on guanylate cyclase activity. These results demonstrate that the positive charges and the helical structure of mastoparan are critical determinants for the activation of guanylate cyclase.
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Formycin A triphosphate (FTP), a fluorescent analog of ATP, slightly increased basal guanylate cyclase activity, but significantly potentiated guanylate cyclase activity stimulated by atrial natriuretic factor (ANF) in rat lung membranes. FTP potentiated ANF-stimulated guanylate cyclase activity with an EC₅₀ at about 90 μM and inhibited ATP-stimulated guanylate cyclase activity with an IC₅₀ at about 100 μM. These results indicate that FTP binds more tightly than ATP for the same binding site. Therefore, FTP would be an excellent tool for studying the ATP binding site.
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Structural requirements of ATP for activation of basal and atrial natriuretic factor-stimulated guanylate cyclase in rat lung membranes

Abstract

Biochim. Biophys. Acta

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.

J. Biol. Chem.

Endocrinol. Metab. Clin. N. Am.

FEBS Lett.

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.