Disseminated intravascular coagulation in septicemia caused by beta-hemolytic streptococci

Cronberg, S; Skånsberg, Per; Nivenius-Larsson, Kerstin

doi:10.1016/0049-3848(73)90034-0

Cited by 23 publications

(12 citation statements)

References 13 publications

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“…In severe periodontitis, P. gingi alis-derived products, including gingipains R, can easily access the circulation through the enlarged surface of the pocket epithelium (more than 72 cm#) [47][48][49]. Our findings that gingipains R, and especially HRgpA, can readily activate factor IX, factor X and\or prothrombin leading ultimately to the release of thrombin suggest the possibility of bacterial proteinase-induced disseminated intravascular coagulation (DIC), which occurs frequently in septic patients [50][51][52][53]. This possibility might be supported by the fact that a patient with dentoalveolar abscess developed both sepsis of Bacteroides melaninogenicus, a bacterium similar to P. gingi alis, and DIC [54].…”

Section: Discussionmentioning

confidence: 88%

Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis

et al. 2001

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The effect of two arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis, an aetiological factor of adult periodontitis, on the activation of human factor IX was investigated in the presence of ethylene glycol, an activity enhancer of activated factor IX (factor IXa), with the use of a fluorogenic oligopeptide substrate. Each gingipain R rapidly activated factor IX but the 95 kDa proteinase complex (HRgpA) that contains both haemagglutinin/adhesion and catalytic domains was 2.4-fold more efficient than the single-chain 50 kDa gingipain R (RgpB), which has only a catalytic domain. SDS/PAGE and N-terminal sequence analysis of factor IX digestion fragments indicated that, like all endogenous activators, gingipains R also produce factor IXabeta via an IXa intermediate. Significantly, phospholipids augmented the activation of factor IX by HRgpA but not by RgpB in a Ca(2+)-dependent manner. In the presence of both cofactors the kinetic efficiency of HRgpA to activate factor IX (k(cat)/K(m)=1.9x10(6) M(-1).s(-1)) was 8.5-fold higher than that of RgpB (k(cat)/K(m)=2.3x10(5) M(-1).s(-1)) and double that of the factor VIIa-tissue factor complex, but 8-fold lower than that for factor XIa. A comparison of the relative activation rates of factor IX, factor X and prothrombin directly in plasma by HRgpA suggests a significant contribution for factor IX conversion in blood coagulation induced by gingipains R. Taken together, gingipains R are the first-reported activators of factor IX of bacterial origin. By this effect they could be involved in the production of thrombin as well as the subsequent generation of prostaglandins and interleukin 1, all of which have been found to be associated with the development and progression of periodontitis.

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Section: Discussionmentioning

confidence: 88%

Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis

et al. 2001

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“…Following these observations, numerous gram-positive organisms were also noted to be asso ciated with DIC and, likewise, the mechanisms have been aptly described. 46,67 Bacterial coat mucopolysac charides may demonstrate exactly the same activity as endotoxin, namely, the activation of Factor XII to Factor XIIa, a platelet release reaction, endothelial sloughing, or the release of granulocyte procoagulant materials, any one of which may initiate DIC. How- ever, as with gram-negative endotoxemia, what is most likely seen is a clinical summation of several or all of these activation events.…”

Section: Etiology Acute Dicmentioning

confidence: 99%

Disseminated Intravascular Coagulation and Related Syndromes: A Clinical Review

Bick

1988

Semin Thromb Hemost

172

470

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“…Decreased plasma levels of PC have been reported in patients with disseminated intravascular coagulation (DIC) (Griffin et al, 1982;Francis and Seyfert, 1986;Kobayashi et al, 1988) or in sepsis (Alcaraz et al, 1995) which precedes DIC (Corrigan et al, 1968;Cronberg et al, 1973;Yoshikawa et al, 1973;Baker, 1989). In parallel with this effect, increased levels of APC complexed with ␣ 1proteinase inhibitor or APC inhibitor have been observed in septic patients (Alcaraz et al, 1995), indicating consumption of the active enzyme.…”

Section: Introductionmentioning

confidence: 96%

Activation of Protein C by Arginine-Specific Cysteine Proteinases (Gingipains-R) from Porphyromonas gingivalis

Hosotaki

Imamura²,

Potempa

et al. 1999

Biological Chemistry

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In order to determine the effect of bacterial proteinases on activation of the protein C system, a negative regulator of blood coagulation, two arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis, a causative bacterium of adult periodontitis, were examined. Each enzyme activated human protein C in a dose- and incubation time-dependent manner. Interestingly, the form of enzyme being composed of a non-covalent complex containing both catalytic and adhesion domains (RgpA) produced activated protein C 14-fold more efficiently than RgpB which contained the catalytic domain alone. The kcat/Km value of RgpA was 18-fold higher than that of RgpB and comparable to that of the thrombin-thrombomodulin complex, the physiological activator of protein C. RgpA catalyzed protein C activation was augmented 1.4-fold by phospholipids, ubiquitous cell membrane components. Furthermore, RgpA, but not RgpB, could activate protein C in plasma and this resulted in a decrease of the protein C concentration in plasma, which is often observed in patients with sepsis during the development of disseminated intravascular coagulation (DIC). These data indicate that RgpA is a more potent activator of protein C than RgpB and suggest that only the former enzyme can cause protein C activation in vivo. The present study further suggests that bacterial proteinases may possibly contribute to the consumption of plasma protein C which predisposes to DIC and/or promotes a thrombotic tendency towards DIC in sepsis.

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Disseminated intravascular coagulation in septicemia caused by beta-hemolytic streptococci

Cited by 23 publications

References 13 publications

Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis

Activation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis

Disseminated Intravascular Coagulation and Related Syndromes: A Clinical Review

Activation of Protein C by Arginine-Specific Cysteine Proteinases (Gingipains-R) from Porphyromonas gingivalis

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