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Vol. 280, Issue 2, 1109-1116, 1997
Hoechst-Marion-Roussel, Disease Group Cardiovascular, Frankfurt,
Germany (P.W., K.W., B.A.S., G.W.), and
University of Mainz, Institute
for Physiological Chemistry and Pathobiochemistry, Mainz, Germany
(J.D.)
In bovine aortic endothelial cells (BAECs), we previously demonstrated
B1 and B2 kinin receptor-mediated increases in
intracellular guanosine-3
,5-cyclic monophosphate (cGMP). In this
study, the B2 kinin receptor agonist bradykinin increased
cGMP in rat microvascular coronary endothelial cells (RMCECs) and human
umbilical vein endothelial cells (HUVECs), which could be prevented
with the specific B2 kinin receptor antagonist icatibant
but not with the B1 kinin receptor antagonist
des-Arg9-[Leu8]bradykinin or with the
nonpeptide kinin receptor antagonist WIN 64338. B2 kinin
receptor mRNA could be detected in all three cell types using reverse
transcription-polymerase chain reaction and subsequent Southern
blotting. The B1 kinin receptor agonist
des-Arg9-bradykinin increased cGMP in RMCECs but not in
HUVECs. The response in RMCECs could be prevented by
des-Arg9-[Leu8]bradykinin as well as by WIN
64338 but not by icatibant. In BAECs, the B1 kinin
receptor-mediated cGMP synthesis could be prevented by icatibant and
desensitized by preincubation with des-Arg9-bradykinin as
well as bradykinin. We detected B1 kinin receptor mRNA in
RMCECs and HUVECs but not in BAECs. In HUVECs, the detection of
B1 kinin receptor mRNA is in contradiction to the cGMP
measurements. In BAECs, the atypical B1 kinin receptor
pharmacology, the heterologous desensitization of the receptor and the
failure to detect B1 kinin receptor mRNA cannot be
explained by a typical B1 kinin receptor subtype. Thus,
B2 kinin receptors with similar pharmacology are constitutively expressed in each of the three endothelial cell types.
However, the endothelial cell types are heterogeneous in the expression
of typical B1 kinin receptors and the pharmacology of the
B1 kinin receptor-mediated responses.
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