Activation of guanylate cyclase by natriuretic peptides in mouse pituitary AtT20 cells is influenced by phosphorylation of ANP.
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Activation of guanylate cyclase by natriuretic peptides in mouse pituitary AtT20 cells is influenced by phosphorylation of ANP. / Jahn, Holger; Kiefer, F; Behl, C; Wiedemann, Klaus.
In: NEUROCHEM RES, Vol. 26, No. 5, 5, 2001, p. 473-478.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Activation of guanylate cyclase by natriuretic peptides in mouse pituitary AtT20 cells is influenced by phosphorylation of ANP.
AU - Jahn, Holger
AU - Kiefer, F
AU - Behl, C
AU - Wiedemann, Klaus
PY - 2001
Y1 - 2001
N2 - The discovery of free and membrane-bound ectokinases raises the question whether phosphorylation is another mechanism to modulate the action of distinct neuropeptides. Atrial-natriuretic-peptide (ANP) which is widespread found in the central nervous system (CNS) and involved in the modulation of stress reactions and emotional states like anxiety contains a recognition-motif for cAMP-dependent protein kinase A. We investigated the effect of phosphorylation of ANP and C-type natriuretic peptide (CNP), a related peptide without phosphorylation site, on their ability to activate their receptors in mouse pituitary AtT20 cells by measuring the formation of cyclic guanosinmonophosphate (cGMP). Phosphorylation with protein kinase A inactivated ANP. Coincubation experiments adding adenosintriphosphate (ATP), ATP-analogues or inhibitors of protein kinases to the medium pointed to the presence of an intrinsic protein kinase A like ectokinase-activity on AtT20 cells. The activity of CNP was unaffected in these experiments. Phosphorylation by ectokinases may be a physiological mechanism to regulate the biological activity of ANP in different tissues, such as pituitary and CNS.
AB - The discovery of free and membrane-bound ectokinases raises the question whether phosphorylation is another mechanism to modulate the action of distinct neuropeptides. Atrial-natriuretic-peptide (ANP) which is widespread found in the central nervous system (CNS) and involved in the modulation of stress reactions and emotional states like anxiety contains a recognition-motif for cAMP-dependent protein kinase A. We investigated the effect of phosphorylation of ANP and C-type natriuretic peptide (CNP), a related peptide without phosphorylation site, on their ability to activate their receptors in mouse pituitary AtT20 cells by measuring the formation of cyclic guanosinmonophosphate (cGMP). Phosphorylation with protein kinase A inactivated ANP. Coincubation experiments adding adenosintriphosphate (ATP), ATP-analogues or inhibitors of protein kinases to the medium pointed to the presence of an intrinsic protein kinase A like ectokinase-activity on AtT20 cells. The activity of CNP was unaffected in these experiments. Phosphorylation by ectokinases may be a physiological mechanism to regulate the biological activity of ANP in different tissues, such as pituitary and CNS.
M3 - SCORING: Zeitschriftenaufsatz
VL - 26
SP - 473
EP - 478
JO - NEUROCHEM RES
JF - NEUROCHEM RES
SN - 0364-3190
IS - 5
M1 - 5
ER -
