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Inhibition of human factor VIIIa by anti-A2 subunit antibodies

Autor: S L Helgerson, J E Curtis, Pete Lollar, D Scandella, E T Parker, M E Scott, Leon W. Hoyer

Publikováno v: Journal of Clinical Investigation. 93:2497-2504

Human inhibitory alloantibodies and autoantibodies to Factor VIII (FVIII) are usually directed toward the A2 and/or C2 domains of the FVIII molecule. Anti-C2 antibodies block the binding of FVIII to phospholipid, but the mechanism of action of anti-A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bef7b4ad68006595b0c12051d698c0fa
https://doi.org/10.1172/jci117259

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Isolation and characterization of thrombin-activated human factor VIII

Autor: S L Helgerson, P Lollar, J E Curtis, E T Parker

Publikováno v: Journal of Biological Chemistry. 269:6246-6251

Recombinant human factor VIII (fVIII) was activated by thrombin at pH 7.4, followed by CM-Sepharose chromatography at pH values ranging from 3.5 to 7.4. Optimal coagulant activity was recovered at pH 5.5 and was associated with the isolation of an A1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::12a48f5b518b65b172bcc502ca362b6d
https://doi.org/10.1016/s0021-9258(17)37594-4

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Production of monoclonal antibodies that detect Hodgkin's high molecular weight transforming growth factor-beta

Autor: S R, Newcom, L H, Muth, E T, Parker

Publikováno v: Blood. 75:2434-2437

High molecular weight transforming growth factor-beta (TGF beta) is a physiologically active TGF secreted by nodular sclerosing Reed- Sternberg cells. Five monoclonal murine antibodies were prepared that distinguished Hodgkin's TGF beta from platelet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd3b9a61eb6fb1693e62815cd700d556
https://doi.org/10.1182/blood.v75.12.2434.bloodjournal75122434

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Factor VIII inhibitors

Autor: P, Lollar, J F, Healey, R T, Barrow, E T, Parker

Publikováno v: Advances in experimental medicine and biology. 489

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c4f306249a2f2166e9b05113d666487f
https://pubmed.ncbi.nlm.nih.gov/11554592

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Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator

Autor: R T, Barrow, E T, Parker, S, Krishnaswamy, P, Lollar

Publikováno v: The Journal of biological chemistry. 269(43)

The effect of heparin and other glycosaminoglycans on the activation of factor X by the phospholipid membrane-bound human factor IXa-factor VIIIa complex (intrinsic fXase) was studied. Standard heparin inhibited purified intrinsic fXase by 50% at app

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f173d520430a3514c8aa4428e312ecbe
https://pubmed.ncbi.nlm.nih.gov/7929416

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Isolation and characterization of thrombin-activated human factor VIII

Autor: J E, Curtis, S L, Helgerson, E T, Parker, P, Lollar

Publikováno v: The Journal of biological chemistry. 269(8)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dc8c41a237e5eaa7a60d03e98f92df01
https://pubmed.ncbi.nlm.nih.gov/8119969

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Coagulant properties of hybrid human/porcine factor VIII molecules

Autor: P, Lollar, E T, Parker, P J, Fay

Publikováno v: The Journal of biological chemistry. 267(33)

Human and porcine factor VIII (fVIII) are activated by thrombin to form a heterotrimer composed of subunits designated A1 and A2 derived from the fVIII heavy chain (HC) and a subunit designated A3-C1-C2 derived from the fVIII light chain (LC). Human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::446463f90e877135c1a58a216f7b176c
https://pubmed.ncbi.nlm.nih.gov/1429706

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Structural basis for the decreased procoagulant activity of human factor VIII compared to the porcine homolog

Autor: P, Lollar, E T, Parker

Publikováno v: The Journal of biological chemistry. 266(19)

The stability of activated human and porcine factor VIII (fVIII) differ, but a direct comparison of their structural and functional properties has not been made. Highly purified, heterodimeric human recombinant and porcine plasma-derived fVIII were e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::97a3d71504c30ee7d971f9af9f7a04d5
https://pubmed.ncbi.nlm.nih.gov/1905722

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