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Blood, Vol. 94 No. 12 (December 15), 1999:
pp. 4314-4320
Ontogeny of Catecholamine and Adenosine Receptor-Mediated cAMP
Signaling of Embryonic Red Blood Cells: Role of
cGMP-Inhibited Phosphodiesterase 3 and Hemoglobin
Rosemarie Baumann,
Christian Blass,
Robert Götz, and
Stefanie Dragon
From the Physiologisches Institut, Universität Regensburg,
Regensburg, Germany.
We have previously shown that the cAMP signaling pathway controls
major aspects of embryonic red blood cell (RBC) function in avian
embryos (Glombitza et al, Am J Physiol 271:R973, 1996; and
Dragon et al, Am J Physiol 271:R982, 1996) that
are important for adaptation of the RBC gas transport properties to the
progressive hypercapnia and hypoxia of later stages of avian embryonic
development. Data about the ontogeny of receptor-mediated cAMP
signaling are lacking. We have analyzed the response of primitive and
definitive chick embryo RBC harvested from day 3 to 18 of development
towards forskolin,  -adrenergic, and A2 receptor agonists. The
results show a strong response of immature definitive and primitive RBC to adenosine A2 and -adrenergic receptor agonists, which is
drastically reduced in the last stage of development, coincident with
the appearance of mature, transcriptionally inactive RBC. Modulation of
cGMP-inhibited phosphodiesterase 3 (PDE3) has a controlling influence
on cAMP accumulation in definitive RBC. Under physiological conditions,
PDE3 is inhibited due to activation of soluble guanylyl cyclase (sGC).
Inhibition of sGC with the specific inhibitor ODQ decreases
receptor-mediated stimulation of cAMP production; this effect is
reversed by the PDE3 inhibitor milrinone. sGC is acitivated by nitric
oxide (NO), but we found no evidence for production of NO
by erythrocyte NO-synthase. However, embryonic hemoglobin releases NO
in an oxygen-linked manner that may activate guanylyl cyclase.
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