Fibrin-stabilizing Factor (Factor XIII) in the Fetus and the Newborn Infant

Henriksson, P.; Hedner, Ulla; Nilsson, Inga Marie; Boehm, John J.; Robertson, Bertil; Lóránd, L.

doi:10.1203/00006450-197409000-00002

Cited by 29 publications

(6 citation statements)

References 11 publications

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“…Both factors XI and XII followed patterns similar to those reported for humans. Factor XIII was 92% of normal at term in the fetal lamb, which is similar to that reported by Fisher and co-workers in the newborn (72) but above the 50"/" level reported for human infants by Henriksson (73). In general, the lamb at term is somewhat more mature relative to achieving adult levels of coagulation factor activities than is the human newborn.…”

Section: Studies Of Blood Coagulation In the Fetal Lamb By Fantl Andsupporting

confidence: 86%

The Animal Models for Hemorrhage and Thrombosis in the Neonate

Ct¹

1987

Thromb Haemost

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SummaryAnimal models have added significantly to our understanding of adult hemorrhagic and thrombotic diseases. Few models, however, have been developed for studies of the hemostatic disorders in the fetus and newborn. This report reviews the current information on animal models of fetal and neonatal hemostasis. The requirements of a relevant model are addressed and previous studies using fetal and neonatal animal models are reviewed. A recommendation of a single animal for all studies of fetal and neonatal hemostasis is not possible. However, the lamb has been the most frequently studied and appears to provide relevant information regarding normal development and the factors which may adversely influence hemostasis in the fetus and newborn.

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Section: Studies Of Blood Coagulation In the Fetal Lamb By Fantl Andsupporting

confidence: 86%

The Animal Models for Hemorrhage and Thrombosis in the Neonate

Ct¹

1987

Thromb Haemost

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“…Besides cyanosis, developmental changes in coagulation factor have been accused to influence the activity of factor XIII. Because this factor is present at birth with little developmental changes , no adjustment for age was done in our study and we did not find any association between them in our population (Table ).…”

Section: Discussionmentioning

confidence: 80%

The perioperative course of factor XIII and associated chest tube drainage in newborn and infants undergoing cardiac surgery

Gertler

Martin

Hapfelmeier

et al. 2013

Pediatric Anesthesia

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“…Reactivity to Factor XIII a was probed by the incorporation of dansylcadaverine; reaction products were measured quantitatively (42)(43)(44) and were also documented on the SDS-PAGE profiles of the proteins photographically under UV illumination (17). Three partially degraded forms of human fibrinogen were used as substrates.…”

Section: Resultsmentioning

confidence: 99%

“…These experiments were carried out by a modification of a previously published procedure (42)(43)(44). Enzyme-catalyzed incorporation of the amine was terminated by adding 100 l of 20% (w/v) trichloroacetic acid to 20 l of experimental mixtures, followed by the addition of 80 l of fibrinogen (5 mg/ml stock) as a carrier.…”

Section: Probing the Factor XIII A Reactive Sites Of Truncated Fibrinmentioning

confidence: 99%

Contact with the N Termini in the Central E Domain Enhances the Reactivities of the Distal D Domains of Fibrin to Factor XIIIa

Samokhin

Lóránd

1995

Journal of Biological Chemistry

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The reaction of Factor XIII a with fibrin is the last enzyme-catalyzed step on the coagulation cascade, leading to the formation of a normal blood clot. The finding that fibrin is preferred by the cross-linking enzyme about 10-fold over the circulating fibrinogen suggests the operation of a unique substrate-level control for the orderly functioning of the physiological process in the forward direction. An important task is to elucidate the molecular mechanism for the transmission of the signal generated by the thrombin-catalyzed cleavage in the central E domain of fibrin to the distant Factor XIII areactive glutamine residues. By focusing on the substrate sites present in ␥ chain remnants of D type domains of fibrinogen and by employing the approach of fragment complementation with the regulatory E domain, which represents the thrombin-modified portion of fibrin, we have now succeeded in reconstructing in solution the phenomenon of kinetic enhancement for the reaction with Factor XIII a .Two D type preparations (truncated fibrinogen, ϳ250 kDa and D, ϳ105 kDa) were obtained by digestion of human fibrinogen with endo Lys-C. Neither product could be cross-linked by Factor XIII a , but as shown by the incorporation of dansylcadaverine, both were acceptor substrates for the enzyme. The plasmin-derived D (ϳ105-kDa) product, however, could be cross-linked into DD dimers. In all cases, the admixture of E fragments exerted a remarkable boosting effect on the reactions with Factor XIII a . Even with native fibrinogen as substrate, cross-linking of ␥ chains was enhanced in the presence of E. Nondenaturing electrophoresis was used to demonstrate the complex forming potential of E fragments with fibrinogen, truncated fibrinogen, D, or D. The GPRP tetrapeptide mimic of the GPRV N-terminal sequence of the ␣ chains in the E fragments, abolished both complex formation and the kinetic boosting effect of E on the reactions of substrates with Factor XIII a . Thus, the N-terminal ␣ chain sequences seem to act as organizing templates for spatially orienting the D domains, probably during the protofibrillar assembly of the fibrin units, for favorable reaction with Factor XIII a .

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Fibrin-stabilizing Factor (Factor XIII) in the Fetus and the Newborn Infant

Cited by 29 publications

References 11 publications

The Animal Models for Hemorrhage and Thrombosis in the Neonate

The Animal Models for Hemorrhage and Thrombosis in the Neonate

The perioperative course of factor XIII and associated chest tube drainage in newborn and infants undergoing cardiac surgery

Contact with the N Termini in the Central E Domain Enhances the Reactivities of the Distal D Domains of Fibrin to Factor XIIIa

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