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The thrombin receptor agonist peptide SFLLRN was less effective
than thrombin in eliciting the liberation of arachidonic acid and the
generation of thromboxane A
Volume 270,
Number 24,
Issue of June 16, pp. 14816-14823, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
(cPLA
)
by Thrombin and Thrombin Receptor Agonist Peptide in Human Platelets
EVIDENCE FOR ACTIVATION OF cPLA
INDEPENDENT OF THE
MITOGEN-ACTIVATED PROTEIN KINASES ERK1/2
by human platelets. We found
that while SFLLRN evokes an initial transient increase in cytosolic
free calcium concentration
([Ca]
) of similar
magnitude as that caused by thrombin, the SFLLRN-induced elevation of
[Ca
]
declines more
rapidly to near resting levels than that evoked by thrombin, suggesting
that disparate levels of [Ca
]
may contribute to the attenuated arachidonic acid release.
Furthermore, we observed that SFLLRN is less effective than thrombin in
mediating the ``activating'' phosphorylation of cytosolic
phospholipase A
(cPLA). Both thrombin and
SFLLRN rapidly and transiently activated kinases that phosphorylate the
21-residue synthetic peptide Thr derived from the
epidermal growth factor receptor, but the maximal activation of
proline-directed kinases by SFLLRN was less pronounced than that by
thrombin. MonoQ chromatography and immunoblot analysis of extracts from
stimulated platelets revealed that while thrombin induced a prominent
activation of the mitogen-activated protein kinases ERK1 and ERK2,
SFLLRN completely failed to do so. On the other hand, SFLLRN, like
thrombin, stimulated the activity of a proline-directed kinase distinct
from ERK1/2, but the activation of this kinase was less pronounced
following stimulation of platelets with SFLLRN compared with thrombin.
We conclude 1) that the partial activation of cPLA
and the
subsequent attenuated mobilization of arachidonic acid in response to
SFLLRN may be the consequence of a less prolonged elevation of
[Ca]
and insufficient
activation of proline-directed kinase(s) by SFLLRN and 2) that the
ability of SFLLRN to mediate the activating phosphorylation of
cPLA
in the absence of ERK1/2 stimulation suggests that, at
least in human platelets, proline-directed kinases other than ERK1/2
may phosphorylate and activate cPLA.
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