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J Biol Chem, Vol. 275, Issue 17, 12639-12650, April 28, 2000
From the Rhodnius prolixus aggregation
inhibitor 1 (RPAI-1), a 19-kDa protein isolated from the salivary gland
of R. prolixus, was purified by strong cation exchange and
reverse-phase high performance liquid chromatographies. Based on 49 amino-terminal amino acid sequences of RPAI-1, primers were produced to
generate probes to screen an R. prolixus salivary gland
cDNA library. A phage containing the full-length clone of RPAI-1
codes for a mature protein of 155 amino acids. RPAI-1 shows sequence
homology to triabin and pallidipin, lipocalins from Triatoma
pallidipennis. The cDNA sequence was cloned in Pet17B
Escherichia coli expression vector, producing an active
peptide. RPAI-1 inhibits human platelet-rich plasma aggregation
triggered by low concentrations of ADP, collagen, arachidonic acid,
thromboxane A2 mimetics (U46619), and very low doses of
thrombin and convulxin. Here we show that ADP is the target of RPAI-1
since (i) RPAI-1 inhibits ADP-dependent large aggregation
formation and secretion triggered by U46619, without affecting
Ca2+ increase and shape change; (ii) ADP restored the
inhibition of U46619-induced platelet aggregation by RPAI-1, (iii)
PGE1-induced increase of cAMP (which is antagonized by
U46619 in an ADP-dependent manner) was restored by RPAI-1,
(iv) RPAI-1 inhibits low concentrations of ADP-mediated responses of
indomethacin-treated platelets, and (v) RPAI-1 binds to ADP, as
assessed by large zone chromatography. RPAI-1 affects neither integrin
Purification, Cloning, Expression, and Mechanism of Action of a
Novel Platelet Aggregation Inhibitor from the Salivary Gland of the
Blood-sucking Bug, Rhodnius prolixus*
,§,
Laboratory of Parasitic Diseases, NIAID,
National Institutes of Health, Bethesda, Maryland 20892-0425, the
¶ Department of Entomology, University of Georgia,
Athens, Georgia 30602, and the Department of Biochemistry,
University of Arizona, Tucson, Arizona 85721
2
1- nor glycoprotein VI-mediated platelet
responses. We conclude that RPAI-1 is the first lipocalin described
that inhibits platelet aggregation by a novel mechanism, binding to ADP.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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