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(Received for publication, December 24, 1996, and in revised form, March 17, 1997)
From the Department of Biochemistry, University of Georgia, Athens,
Georgia 30602, the The effect of two arginine-specific cysteine
proteinases (gingipain Rs) from Porphyromonas gingivalis, a
causative bacterium of adult periodontitis, on human blood coagulation
was investigated. Activated partial thromboplastin time and prothrombin
time were shortened by these proteinases, with a 95-kDa gingipain R
containing adhesin domains being 5-fold more efficient in comparison to
a 50-kDa gingipain R containing the catalytic domain alone. The 50-kDa
enzyme reduced each coagulation time in several plasmas deficient in
various coagulation factors, while it was ineffective in factor
X-deficient plasma unless reconstituted with this protein. Each
proteinase activated factor X in a dose- and time-dependent manner, with Michaelis constants (Km) being found
to be lower than the normal plasma factor X concentration, strongly suggesting that factor X activation by gingipain Rs, especially the
95-kDa form which is strongly activated by phospholipids, could occur
in plasma. This is the first report of factor X activation by bacterial
proteinases and indicates that the gingipain Rs could be responsible
for the production of thrombin and, indirectly, with the generation of
prostaglandins, interleukin-1, etc., which have been found to be
associated with the development of periodontitis induced by P. gingivalis infections. Furthermore, the data support the
hypothesis that induction of blood coagulation by bacterial proteinases
may be a causative agent in the pathogenesis of disseminated intravascular coagulation in sepsis.
Volume 272, Number 25,
Issue of June 20, 1997
pp. 16062-16067
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
and
Division of Molecular Pathology,
Department of Neuroscience and Immunology, Kumamoto University Graduate
School of Medical Sciences, Kumamoto 860, Japan, and the
§ Department of Microbiology and Immunology, Institute of
Molecular Biology, Jagiellonian University,
31-120 Kraków, Poland
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