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Neuropeptide Y (NPY) and norepinephrine, found co-localized in
sympathetic neurons innervating blood vessels, exert synergistic
responses on vasoconstriction. To examine the signaling mechanisms
involved, free of complications associated with mixed receptor
populations, we have established a stable Chinese hamster ovary cell
line expressing both Y1-NPY and
Volume 270,
Number 20,
Issue of May 19, pp. 11789-11796, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-Adrenergic
Receptors in the Regulation of Phospholipase C, Protein Kinase C, and
Arachidonic Acid Production
-adrenergic
receptors. Occupation of either receptor species, with 100 nM
peptide YY (PYY) or 10 µM phenylephrine (PE),
respectively, resulted in a rapid increase in the cytoplasmic free
calcium concentration
([Ca
]
) as assessed
with Fura-2/AM. The rise due to PYY, but not that due to PE, was
abolished by pretreatment with pertussis toxin. Both responses were
largely maintained in the absence of extracellular
Ca
, but abolished by prior depletion of intracellular
Ca
pools with either thapsigargin or
2,5-di-(t-butyl)-1,4-benzohydroquinone. Using cells prelabeled
with myo-[
H]inositol, PE promoted a
rapid (5 s) rise in inositol 1,4,5-trisphosphate
(Ins(1,4,5)P) as analyzed by anion-exchange high pressure
liquid chromatography, whereas the response to PYY (first significant
at >15 s post-stimulation) was too slow to play a causative role in
Ca mobilization. Combination of PE and PYY resulted
in increases in [Ca
]
which were at best additive, whereas they promoted a clearly
synergistic rise in Ins(1,4,5)P
at both 15 and 60 s.
Co-stimulation also resulted in a synergistic activation of both
protein kinase C (PKC) and [H]arachidonic acid
release. In either instance PYY alone was without effect. The
potentiation of arachidonic acid release was abolished by depletion of
cellular PKC following chronic treatment with phorbol esters. It is
suggested that the ability of PYY to mobilize Ca in
an Ins(1,4,5)P
-independent fashion minimizes the functional
importance of the capacity to potentiate PE-stimulated
Ins(1,4,5)P generation. Instead the major conseqences of
the synergistic activation of phospholipase C are mediated via PKC, the
other route of the signaling pathway.
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