The coagulation profile in hepatosplenic schistosomiasis

El-Bassiouni, Nora E.; Bassiouny, A. E. El; Hussein, Nadia; Elsayed, Hanaa; Ibrahim, Ibtihal; Lotfy, Mahmoud; Omran, S. A.

doi:10.1097/00001721-199803000-00011

Cited by 17 publications

(11 citation statements)

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“…It was reported that the progressive deterioration of liver function (matching the severity of the disease and the intensity of infection) led to a reduction in the blood levels of numerous coagulation proteins resulting in hypercoagulability and thrombin generation. This was subsequently followed by coagulation factor consumption, resulting in hypocoagulability and secondary fibrinolysis [12]. This last outcome is broadly akin to what is observed in this work: blood from 7-week infected mice forms strong clots much more rapidly than blood from controls but these clots are prone to break down very rapidly.…”

Section: Discussionsupporting

confidence: 54%

“…A study of 14 patients (also with hepatosplenic schistosomiasis) likewise revealed that all coagulation parameters were significantly reduced in this group compared to healthy controls [11]. In another study, the coagulation profile of 60 schistosomiasis patients, with hepatosplenomegaly whose liver disease was graded least to worst, was compared with 15 healthy controls [12]. It was reported that the progressive deterioration of liver function (matching the severity of the disease and the intensity of infection) led to a reduction in the blood levels of numerous coagulation proteins resulting in hypercoagulability and thrombin generation.…”

Section: Discussionmentioning

confidence: 99%

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The impact of schistosomes and schistosomiasis on murine blood coagulation and fibrinolysis as determined by thromboelastography (TEG)

Da’dara

Laforcade

Skelly

2015

J Thromb Thrombolysis

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Schistosomes are parasitic platyhelminths that currently infect over 200 million people and cause the chronic debilitating disease schistosomiasis. While these large intravascular parasites can disturb blood flow, surprisingly they do not appear to provoke thrombus formation around them in vivo. In order to determine if the worms can alter their local environment to impede coagulation, we incubated adult worms (50 pairs) in murine blood (500 μl) for 1 h at 37 °C and, using thromboelastography (TEG), we compared the coagulation profile of the blood with control blood that never contained worms. Substantial differences were apparent between the two profiles. Blood that had been exposed to schistosomes clotted more slowly and yielded relatively poor, though stable, thrombi; all TEG measures of blood coagulation (R, K, α-angle, MA, G and TMA) differed significantly between conditions. No fibrinolysis (as determined by LY30 and LY60 values) was detected in either case. The observed TEG profile suggests that the worms are acting as local anti-coagulants. Blood recovered from schistosome-infected mice, however, does not behave in this way. At an early time point post infection (4-weeks), the TEG profile of infected murine blood is essentially the same as that of control blood. However at a later time point (7-weeks) infected murine blood clots significantly faster than control blood but these clots also break down faster. The R, K, α-angle, and TMA measures of coagulation are all significantly different between the control versus infected mice as are the LY30 and LY60 values. This profile is indicative of a hypercoagulable state with fibrinolysis and is akin to that seen in human patients with advanced schistosomiasis.

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Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 99%

The impact of schistosomes and schistosomiasis on murine blood coagulation and fibrinolysis as determined by thromboelastography (TEG)

Da’dara

Laforcade

Skelly

2015

J Thromb Thrombolysis

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“…Thus, kallikrein-like protease activity from S. mansoni adults [12] and plasmin-like fibrinolytic activity from S. mansoni eggs [15] have been recorded previously. Both activities displayed trypsin type cleavage specificities and both may contribute to the phenomenon, whereby large occlusions of veins by schistosomes are not associated with intravascular deposition of fibrin and thrombus formation [52]–[54]. At the gene and primary sequence levels, however, only two SmSPs, namely SmSP1 [13], [14] and another [23], [24], which we term SmSP2, have been described.…”

Section: Discussionmentioning

confidence: 99%

Trypsin- and Chymotrypsin-Like Serine Proteases in Schistosoma mansoni – ‘The Undiscovered Country’

et al. 2014

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BackgroundBlood flukes (Schistosoma spp.) are parasites that can survive for years or decades in the vasculature of permissive mammalian hosts, including humans. Proteolytic enzymes (proteases) are crucial for successful parasitism, including aspects of invasion, maturation and reproduction. Most attention has focused on the ‘cercarial elastase’ serine proteases that facilitate skin invasion by infective schistosome larvae, and the cysteine and aspartic proteases that worms use to digest the blood meal. Apart from the cercarial elastases, information regarding other S. mansoni serine proteases (SmSPs) is limited. To address this, we investigated SmSPs using genomic, transcriptomic, phylogenetic and functional proteomic approaches.Methodology/Principal FindingsGenes encoding five distinct SmSPs, termed SmSP1 - SmSP5, some of which comprise disparate protein domains, were retrieved from the S. mansoni genome database and annotated. Reverse transcription quantitative PCR (RT- qPCR) in various schistosome developmental stages indicated complex expression patterns for SmSPs, including their constituent protein domains. SmSP2 stood apart as being massively expressed in schistosomula and adult stages. Phylogenetic analysis segregated SmSPs into diverse clusters of family S1 proteases. SmSP1 to SmSP4 are trypsin-like proteases, whereas SmSP5 is chymotrypsin-like. In agreement, trypsin-like activities were shown to predominate in eggs, schistosomula and adults using peptidyl fluorogenic substrates. SmSP5 is particularly novel in the phylogenetics of family S1 schistosome proteases, as it is part of a cluster of sequences that fill a gap between the highly divergent cercarial elastases and other family S1 proteases.Conclusions/SignificanceOur series of post-genomics analyses clarifies the complexity of schistosome family S1 serine proteases and highlights their interrelationships, including the cercarial elastases and, not least, the identification of a ‘missing-link’ protease cluster, represented by SmSP5. A framework is now in place to guide the characterization of individual proteases, their stage-specific expression and their contributions to parasitism, in particular, their possible modulation of host physiology.

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“…12 Low protein C activity has been described in patients with inflammatory hepatopathies, cirrhosis, portal venous obstruction, and infiltrative and neoplastic diseases and has been used as a prognostic indicator for monitoring hepatic transplant patients after surgery. [12][13][14][15][16][17] In our preliminary studies of protein C activity in dogs, we discovered that many dogs with acquired and congenital hepatobiliary disorders had low protein C activity and that dogs with PSS appeared to develop the lowest protein C activity. a The purpose of the study reported here was to evaluate the diagnostic use of protein C for detection of hepatobiliary disease and PSS in dogs.…”

mentioning

confidence: 99%

Evaluation of plasma protein C activity for detection of hepatobiliary disease and portosystemic shunting in dogs

Toulza

Brooks²,

Erb³

et al. 2006

javma

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The coagulation profile in hepatosplenic schistosomiasis

Cited by 17 publications

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The impact of schistosomes and schistosomiasis on murine blood coagulation and fibrinolysis as determined by thromboelastography (TEG)

The impact of schistosomes and schistosomiasis on murine blood coagulation and fibrinolysis as determined by thromboelastography (TEG)

Trypsin- and Chymotrypsin-Like Serine Proteases in Schistosoma mansoni – ‘The Undiscovered Country’

Evaluation of plasma protein C activity for detection of hepatobiliary disease and portosystemic shunting in dogs

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