Quality of thrombin produced from the patient's own plasma using the TPD, a new Thrombin-processing Device
(2005) In The Journal of the American Society of Extra-Corporeal Technology 37(2). p.196-200- Abstract
Thrombin derived from bovine sources commonly is used to arrest bleeding during surgical procedures. However, complications such as postoperative hemorrhage can occur because of the development of cross-reactive anti-bovine antibodies that inhibit human coagulation factor V. It would thus be advantageous to develop techniques to generate human thrombin. This study evaluated thrombin produced from human plasma using a new Thrombin-Processing Device (TPD). Plasma was introduced into the TPD, mixed with an ethanol/ CaCl2 reagent, incubated for 1 h, and the harvested thrombin was assayed for activity and the ability to activate platelets by in vitro assays. TPD-produced thrombin activity was found to be 51.8 +/- 12.4 IU/mL (n = 145).... (More)
Thrombin derived from bovine sources commonly is used to arrest bleeding during surgical procedures. However, complications such as postoperative hemorrhage can occur because of the development of cross-reactive anti-bovine antibodies that inhibit human coagulation factor V. It would thus be advantageous to develop techniques to generate human thrombin. This study evaluated thrombin produced from human plasma using a new Thrombin-Processing Device (TPD). Plasma was introduced into the TPD, mixed with an ethanol/ CaCl2 reagent, incubated for 1 h, and the harvested thrombin was assayed for activity and the ability to activate platelets by in vitro assays. TPD-produced thrombin activity was found to be 51.8 +/- 12.4 IU/mL (n = 145). TPD-produced thrombin also stimulated P-selectin (CD62) expression (83 +/- 13% of the platelet population) and Annexin V binding (10.3 +/- 2% of the platelet population) on platelets in a similar fashion to commercial thrombin (P-selectin expression: 88 +/- 3%; Annexin-V binding: 11.4 +/- 3%). Compared with CaCl2 and batroxobin, TPD-produced thrombin had a significantly greater ability to activate platelets. TPD-produced thrombin from human plasma has consistent activity and significantly activates platelets and, thus, may have attractive applications such as the production of autologous thrombin for surgical patients.
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- author
- Semple, Elisabeth ; Madsen, Trista and Semple, John W LU
- publishing date
- 2005-06
- type
- Contribution to journal
- publication status
- published
- keywords
- Blood Loss, Surgical/prevention & control, Blood Transfusion, Autologous/instrumentation, Canada, Diffusion of Innovation, Humans, Platelet Activation, Thrombin/chemical synthesis
- in
- The Journal of the American Society of Extra-Corporeal Technology
- volume
- 37
- issue
- 2
- pages
- 196 - 200
- publisher
- American Society of Extra-Corporeal Technology
- external identifiers
-
- scopus:22044457563
- pmid:16117459
- ISSN
- 0022-1058
- language
- English
- LU publication?
- no
- id
- d8aac062-3a3b-40a6-b40e-8972cdbbd736
- alternative location
- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682536/pdf/ject-37-196.pdf
- date added to LUP
- 2022-11-09 15:25:03
- date last changed
- 2024-03-17 10:45:11
@article{d8aac062-3a3b-40a6-b40e-8972cdbbd736,
abstract = {{<p>Thrombin derived from bovine sources commonly is used to arrest bleeding during surgical procedures. However, complications such as postoperative hemorrhage can occur because of the development of cross-reactive anti-bovine antibodies that inhibit human coagulation factor V. It would thus be advantageous to develop techniques to generate human thrombin. This study evaluated thrombin produced from human plasma using a new Thrombin-Processing Device (TPD). Plasma was introduced into the TPD, mixed with an ethanol/ CaCl2 reagent, incubated for 1 h, and the harvested thrombin was assayed for activity and the ability to activate platelets by in vitro assays. TPD-produced thrombin activity was found to be 51.8 +/- 12.4 IU/mL (n = 145). TPD-produced thrombin also stimulated P-selectin (CD62) expression (83 +/- 13% of the platelet population) and Annexin V binding (10.3 +/- 2% of the platelet population) on platelets in a similar fashion to commercial thrombin (P-selectin expression: 88 +/- 3%; Annexin-V binding: 11.4 +/- 3%). Compared with CaCl2 and batroxobin, TPD-produced thrombin had a significantly greater ability to activate platelets. TPD-produced thrombin from human plasma has consistent activity and significantly activates platelets and, thus, may have attractive applications such as the production of autologous thrombin for surgical patients.</p>}},
author = {{Semple, Elisabeth and Madsen, Trista and Semple, John W}},
issn = {{0022-1058}},
keywords = {{Blood Loss, Surgical/prevention & control; Blood Transfusion, Autologous/instrumentation; Canada; Diffusion of Innovation; Humans; Platelet Activation; Thrombin/chemical synthesis}},
language = {{eng}},
number = {{2}},
pages = {{196--200}},
publisher = {{American Society of Extra-Corporeal Technology}},
series = {{The Journal of the American Society of Extra-Corporeal Technology}},
title = {{Quality of thrombin produced from the patient's own plasma using the TPD, a new Thrombin-processing Device}},
url = {{https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682536/pdf/ject-37-196.pdf}},
volume = {{37}},
year = {{2005}},
}