Matches in SemOpenAlex for { <https://semopenalex.org/work/W2063900714> ?p ?o ?g. }
Showing items 1 to 98 of
98
with 100 items per page.
- W2063900714 endingPage "279" @default.
- W2063900714 startingPage "272" @default.
- W2063900714 abstract "SummaryFibrin gel structure has been shown to be dependent on the thrombin concentration as well as the rate of thrombin generation. Accordingly, factor VIII (FVIII)‐ and FIX‐deficient plasma (hemophilia A and B) form loose fibrin clots with high permeability constants. By adding rFVIIa in vitro to FVIII‐deficient plasma containing platelets (frozen and thawed), the fibrin gel permeability constant normalized, indicating that extra rFVIIa (1.2 µg mL−1 or higher) induced a tight fibrin structure. Thrombin generation is highly dependent on the number of platelets, and in this study it was demonstrated that the addition of rFVIIa (5 µg mL−1) normalizes the fibrin gel permeability in samples containing platelets (frozen‐thawed) in numbers of at least down to 20 × 106 mL−1. The effect of rFVIIa was not observed when unfrozen platelets instead of frozen‐thawed platelets were added. Neither was any effect on the fibrin permeability seen, in the presence of annexin V, known to block the effect of phospholipids on the platelet surface. This indicates an important role of platelet phospholipids for the effect of rFVIIa. A similar effect on the fibrin permeability of rFVIIa was observed when added to platelet‐rich plasma from a patient with Glanzmann thrombasthenia. Recombinant FVIIa has been found to induce hemostasis in patients with hemophilia and inhibitors against FVIII/FIX as well as in patients with Glanzmann thrombasthenia, indicating the importance of the formation of a tight fibrin gel structure, more resistant against premature proteolysis, for maintaining hemostasis. In conclusion, the addition of rFVIIa (5 µg mL−1) also substantially decreased the permeability constant of fibrin gels formed in FVIII‐deficient plasma in the presence of low numbers of frozen‐thawed platelets (down to 20 × 106 mL−1). A similar pattern was obtained in plasma from a Glanzmann patient. No effect was found in the presence of unfrozen instead of frozen‐thawed platelets. Annexin V blocked any effect of rFVIIa. A normalization of the overall fibrinolysis potential (OFP) during the same condition supports the effect of rFVIIa on the fibrin permeability in the presence of a limited number of platelets. Fibrin gel structure has been shown to be dependent on the thrombin concentration as well as the rate of thrombin generation. Accordingly, factor VIII (FVIII)‐ and FIX‐deficient plasma (hemophilia A and B) form loose fibrin clots with high permeability constants. By adding rFVIIa in vitro to FVIII‐deficient plasma containing platelets (frozen and thawed), the fibrin gel permeability constant normalized, indicating that extra rFVIIa (1.2 µg mL−1 or higher) induced a tight fibrin structure. Thrombin generation is highly dependent on the number of platelets, and in this study it was demonstrated that the addition of rFVIIa (5 µg mL−1) normalizes the fibrin gel permeability in samples containing platelets (frozen‐thawed) in numbers of at least down to 20 × 106 mL−1. The effect of rFVIIa was not observed when unfrozen platelets instead of frozen‐thawed platelets were added. Neither was any effect on the fibrin permeability seen, in the presence of annexin V, known to block the effect of phospholipids on the platelet surface. This indicates an important role of platelet phospholipids for the effect of rFVIIa. A similar effect on the fibrin permeability of rFVIIa was observed when added to platelet‐rich plasma from a patient with Glanzmann thrombasthenia. Recombinant FVIIa has been found to induce hemostasis in patients with hemophilia and inhibitors against FVIII/FIX as well as in patients with Glanzmann thrombasthenia, indicating the importance of the formation of a tight fibrin gel structure, more resistant against premature proteolysis, for maintaining hemostasis. In conclusion, the addition of rFVIIa (5 µg mL−1) also substantially decreased the permeability constant of fibrin gels formed in FVIII‐deficient plasma in the presence of low numbers of frozen‐thawed platelets (down to 20 × 106 mL−1). A similar pattern was obtained in plasma from a Glanzmann patient. No effect was found in the presence of unfrozen instead of frozen‐thawed platelets. Annexin V blocked any effect of rFVIIa. A normalization of the overall fibrinolysis potential (OFP) during the same condition supports the effect of rFVIIa on the fibrin permeability in the presence of a limited number of platelets." @default.
- W2063900714 created "2016-06-24" @default.
- W2063900714 creator A5067663034 @default.
- W2063900714 creator A5085200012 @default.
- W2063900714 creator A5085813098 @default.
- W2063900714 date "2005-02-01" @default.
- W2063900714 modified "2023-10-01" @default.
- W2063900714 title "The effect of platelets on fibrin gel structure formed in the presence of recombinant factor VIIa in hemophilia plasma and in plasma from a patient with Glanzmann thrombasthenia" @default.
- W2063900714 cites W1964319357 @default.
- W2063900714 cites W1970249515 @default.
- W2063900714 cites W1980260654 @default.
- W2063900714 cites W1990265878 @default.
- W2063900714 cites W1994378987 @default.
- W2063900714 cites W1996513809 @default.
- W2063900714 cites W1997907146 @default.
- W2063900714 cites W1998000461 @default.
- W2063900714 cites W2017313786 @default.
- W2063900714 cites W2021579133 @default.
- W2063900714 cites W2037652834 @default.
- W2063900714 cites W2046936517 @default.
- W2063900714 cites W2058372581 @default.
- W2063900714 cites W2066520692 @default.
- W2063900714 cites W2070586531 @default.
- W2063900714 cites W2082076083 @default.
- W2063900714 cites W2086955903 @default.
- W2063900714 cites W2088826683 @default.
- W2063900714 cites W2111255663 @default.
- W2063900714 cites W2144537409 @default.
- W2063900714 cites W2148505112 @default.
- W2063900714 cites W2168719124 @default.
- W2063900714 cites W2418390105 @default.
- W2063900714 doi "https://doi.org/10.1111/j.1538-7836.2005.01127.x" @default.
- W2063900714 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15670032" @default.
- W2063900714 hasPublicationYear "2005" @default.
- W2063900714 type Work @default.
- W2063900714 sameAs 2063900714 @default.
- W2063900714 citedByCount "34" @default.
- W2063900714 countsByYear W20639007142012 @default.
- W2063900714 countsByYear W20639007142013 @default.
- W2063900714 countsByYear W20639007142015 @default.
- W2063900714 countsByYear W20639007142016 @default.
- W2063900714 countsByYear W20639007142017 @default.
- W2063900714 countsByYear W20639007142018 @default.
- W2063900714 countsByYear W20639007142020 @default.
- W2063900714 countsByYear W20639007142021 @default.
- W2063900714 crossrefType "journal-article" @default.
- W2063900714 hasAuthorship W2063900714A5067663034 @default.
- W2063900714 hasAuthorship W2063900714A5085200012 @default.
- W2063900714 hasAuthorship W2063900714A5085813098 @default.
- W2063900714 hasBestOaLocation W20639007141 @default.
- W2063900714 hasConcept C126322002 @default.
- W2063900714 hasConcept C185592680 @default.
- W2063900714 hasConcept C203014093 @default.
- W2063900714 hasConcept C2777292125 @default.
- W2063900714 hasConcept C2778198917 @default.
- W2063900714 hasConcept C2778589496 @default.
- W2063900714 hasConcept C2778914503 @default.
- W2063900714 hasConcept C2778961111 @default.
- W2063900714 hasConcept C2911156200 @default.
- W2063900714 hasConcept C2993802102 @default.
- W2063900714 hasConcept C54173615 @default.
- W2063900714 hasConcept C71924100 @default.
- W2063900714 hasConcept C89560881 @default.
- W2063900714 hasConceptScore W2063900714C126322002 @default.
- W2063900714 hasConceptScore W2063900714C185592680 @default.
- W2063900714 hasConceptScore W2063900714C203014093 @default.
- W2063900714 hasConceptScore W2063900714C2777292125 @default.
- W2063900714 hasConceptScore W2063900714C2778198917 @default.
- W2063900714 hasConceptScore W2063900714C2778589496 @default.
- W2063900714 hasConceptScore W2063900714C2778914503 @default.
- W2063900714 hasConceptScore W2063900714C2778961111 @default.
- W2063900714 hasConceptScore W2063900714C2911156200 @default.
- W2063900714 hasConceptScore W2063900714C2993802102 @default.
- W2063900714 hasConceptScore W2063900714C54173615 @default.
- W2063900714 hasConceptScore W2063900714C71924100 @default.
- W2063900714 hasConceptScore W2063900714C89560881 @default.
- W2063900714 hasIssue "2" @default.
- W2063900714 hasLocation W20639007141 @default.
- W2063900714 hasLocation W20639007142 @default.
- W2063900714 hasOpenAccess W2063900714 @default.
- W2063900714 hasPrimaryLocation W20639007141 @default.
- W2063900714 hasRelatedWork W1510051502 @default.
- W2063900714 hasRelatedWork W1897057798 @default.
- W2063900714 hasRelatedWork W1997907146 @default.
- W2063900714 hasRelatedWork W2030271499 @default.
- W2063900714 hasRelatedWork W2036942644 @default.
- W2063900714 hasRelatedWork W2056355602 @default.
- W2063900714 hasRelatedWork W2069476835 @default.
- W2063900714 hasRelatedWork W2886256145 @default.
- W2063900714 hasRelatedWork W4254137938 @default.
- W2063900714 hasRelatedWork W2395723784 @default.
- W2063900714 hasVolume "3" @default.
- W2063900714 isParatext "false" @default.
- W2063900714 isRetracted "false" @default.
- W2063900714 magId "2063900714" @default.
- W2063900714 workType "article" @default.