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Distinctive regulation of contact activation by antithrombin and C1-inhibitor on activated platelets and material surfaces.
Biomaterials. 2009 Dec; 30(34):6573-80.B

Abstract

Activated human plate lets trigger FXII-mediated contact activation, which leads to the generation of FXIIa-antithrombin (AT) and FXIa-AT complexes. This suggests that contact activation takes place at different sites, on activated platelets and material surfaces, during therapeutic procedures involving biomaterials in contact with blood and is differentially regulated. Here we show that activation in platelet-poor plasma, platelet-rich plasma (PRP), and whole blood induced by glass, kaolin, and polyphosphate elicited high levels of FXIIa-C1-inhibitor (C1INH), low levels of FXIa-C1INH and KK-C1INH, and almost no AT complexes. Platelet activation, in both PRP and blood, led to the formation of FXIIa-AT, FXIa-AT, and kallikrein (KK)-AT but almost no C1INH complexes. In severe trauma patients, FXIIa-AT and FXIa-AT were correlated with the release of thrombospondin-1 (TSP-1) from activated platelets. In contrast, FXIIa-C1INH complexes were detected when the FXIIa-AT levels were low. No correlations were found between FXIIa-C1INH and FXIIa-AT or TSP-1. Inhibition of FXIIa on material surfaces was also shown to affect the function of aggregating platelets. In conclusion, formation of FXIIa-AT and FXIIa-C1INH complexes can help to distinguish between contact activation triggered by biomaterial surfaces and by activated platelets. Platelet aggregation studies also demonstrated that platelet function is influenced by material surface-mediated contact activation and that generation of FXIIa-AT complexes may serve as a new biomarker for thrombotic reactions during therapeutic procedures employing biomaterial devices.

Authors+Show Affiliations

Department of Oncology, Radiology, and Clinical Immunology, Division of Clinical Immunology, Rudbeck Laboratory C5, Uppsala University, SE-751 85 Uppsala, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19783299

Citation

Bäck, Jennie, et al. "Distinctive Regulation of Contact Activation By Antithrombin and C1-inhibitor On Activated Platelets and Material Surfaces." Biomaterials, vol. 30, no. 34, 2009, pp. 6573-80.
Bäck J, Lang MH, Elgue G, et al. Distinctive regulation of contact activation by antithrombin and C1-inhibitor on activated platelets and material surfaces. Biomaterials. 2009;30(34):6573-80.
Bäck, J., Lang, M. H., Elgue, G., Kalbitz, M., Sanchez, J., Ekdahl, K. N., & Nilsson, B. (2009). Distinctive regulation of contact activation by antithrombin and C1-inhibitor on activated platelets and material surfaces. Biomaterials, 30(34), 6573-80. https://doi.org/10.1016/j.biomaterials.2009.07.052
Bäck J, et al. Distinctive Regulation of Contact Activation By Antithrombin and C1-inhibitor On Activated Platelets and Material Surfaces. Biomaterials. 2009;30(34):6573-80. PubMed PMID: 19783299.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distinctive regulation of contact activation by antithrombin and C1-inhibitor on activated platelets and material surfaces. AU - Bäck,Jennie, AU - Lang,Markus Huber, AU - Elgue,Graciela, AU - Kalbitz,Miriam, AU - Sanchez,Javier, AU - Ekdahl,Kristina Nilsson, AU - Nilsson,Bo, Y1 - 2009/09/24/ PY - 2009/06/16/received PY - 2009/07/24/accepted PY - 2009/9/29/entrez PY - 2009/9/29/pubmed PY - 2009/12/29/medline SP - 6573 EP - 80 JF - Biomaterials JO - Biomaterials VL - 30 IS - 34 N2 - Activated human plate lets trigger FXII-mediated contact activation, which leads to the generation of FXIIa-antithrombin (AT) and FXIa-AT complexes. This suggests that contact activation takes place at different sites, on activated platelets and material surfaces, during therapeutic procedures involving biomaterials in contact with blood and is differentially regulated. Here we show that activation in platelet-poor plasma, platelet-rich plasma (PRP), and whole blood induced by glass, kaolin, and polyphosphate elicited high levels of FXIIa-C1-inhibitor (C1INH), low levels of FXIa-C1INH and KK-C1INH, and almost no AT complexes. Platelet activation, in both PRP and blood, led to the formation of FXIIa-AT, FXIa-AT, and kallikrein (KK)-AT but almost no C1INH complexes. In severe trauma patients, FXIIa-AT and FXIa-AT were correlated with the release of thrombospondin-1 (TSP-1) from activated platelets. In contrast, FXIIa-C1INH complexes were detected when the FXIIa-AT levels were low. No correlations were found between FXIIa-C1INH and FXIIa-AT or TSP-1. Inhibition of FXIIa on material surfaces was also shown to affect the function of aggregating platelets. In conclusion, formation of FXIIa-AT and FXIIa-C1INH complexes can help to distinguish between contact activation triggered by biomaterial surfaces and by activated platelets. Platelet aggregation studies also demonstrated that platelet function is influenced by material surface-mediated contact activation and that generation of FXIIa-AT complexes may serve as a new biomarker for thrombotic reactions during therapeutic procedures employing biomaterial devices. SN - 1878-5905 UR - https://www.unboundmedicine.com/medline/citation/19783299/Distinctive_regulation_of_contact_activation_by_antithrombin_and_C1_inhibitor_on_activated_platelets_and_material_surfaces_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0142-9612(09)00791-1 DB - PRIME DP - Unbound Medicine ER -