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Bovine Thrombin (bovine + thrombin)
Selected AbstractsFactor V deficiency: a concise reviewHAEMOPHILIA, Issue 6 2008J. N. HUANG Summary., Factor V (FV; proaccelerin or labile factor) is the plasma cofactor for the prothrombinase complex that activates prothrombin to thrombin. FV deficiency can be caused by mutations in the FV gene or in genes encoding components of a putative cargo receptor that transports FV (and factor VIII) from the endoplasmic reticulum to the Golgi. Because FV is present in platelet ,-granules as well as in plasma, low FV levels are also seen in disorders of platelet granules. Additionally, acquired FV deficiencies can occur in the setting of rheumatologic disorders, malignancies, and antibiotic use and, most frequently, with the use of topical bovine thrombin. FV levels have limited correlation with the risk of bleeding, but overall, FV-deficient patients appear to have a less severe phenotype than patients with haemophilia A or B. The most commonly reported symptoms are bleeding from mucosal surfaces and postoperative haemorrhage. However, haemarthroses and intramuscular and intracranial haemorrhages can also occur. Because no FV-specific concentrate is available, fresh frozen plasma remains the mainstay of treatment. Antifibrinolytics can also provide benefit, especially for mucosal bleeding. In refractory cases, or for patients with inhibitors, prothrombin complex concentrates, recombinant activated FVIIa, and platelet transfusions have been successfully used. Some patients with inhibitors may also require immunosuppression. [source] Serological analysis of patients treated with a new surgical hemostat containing bovine proteins and autologous plasma ,JOURNAL OF BIOMEDICAL MATERIALS RESEARCH, Issue 6 2001Patricia A. Nelson Abstract A randomized, controlled clinical study of the management of diffuse bleeding with CoStasis® surgical hemostat, a new hemostat containing bovine thrombin and collagen with the patient's own plasma, included patients undergoing cardiac, hepatic, iliac, and general surgery. Sera from 92 patients treated with CoStasis and 84 control patients were collected preoperatively and at a post surgical follow-up of 8 weeks. Among the control group, 57 patients were treated with Instat® collagen sponge in noncardiac indications. Results showed that antibody responses in the CoStasis clinical study were similar to the reported literature for all antigens screened and were not associated with any adverse reactions. The bovine thrombin preparations in CoStasis and other commercially available thrombins were compared with the use of SDS-PAGE and Western blot analyses. Within this clinical study, CoStasis was shown to be a safe and effective hemostatic product containing bovine thrombin and bovine collagen and no pooled human blood products. © 2001 John Wiley & Sons, Inc. J Biomed Mater Res (Appl Biomater) 58: 710,719, 2001 [source] Antimicrobial activity of platelet-leukocyte gel against Staphylococcus aureusJOURNAL OF ORTHOPAEDIC RESEARCH, Issue 3 2008Dirk Jan F. Moojen Abstract Platelet-leukocyte gel (PLG) contains high concentrations of platelets and leukocytes. As leukocytes play an important role in the innate host-defense, we hypothesized that PLG might have antimicrobial properties. This study investigated the antimicrobial activity of PLG against Staphylococcus aureus and the contribution of myeloperoxidase (MPO), present in leukocytes, in this process. Platelet-rich plasma (PRP) and platelet-poor plasma (PPP) were obtained from whole blood of six donors. PLG was prepared by mixing PRP with autologous (PLG-AT) or bovine thrombin (PLG-BT). Antimicrobial activity of PLG-AT, PLG-BT, PRP, and PPP was determined in a bacterial kill assay. MPO release was measured by ELISA and activity was measured using a MPO activity assay. Cultures showed a rapid decrease in the number of bacteria for both PLG-AT and PLG-BT, which was maximal between 4 and 8 h, to approximately 1% of the bacteria in controls. The effect of PLG-AT was largest and significantly different compared to PRP (p,=,0.004) and PPP (p,<,0.001), however not compared to PLG-BT (p,=,0.093). PLG-AT, PLG-BT, and PRP showed a comparable, gradually increasing MPO release. MPO activity was comparable for all groups and remained stable. No correlation between MPO release, activity, and bacterial kill could be found. PLG appears to have potent antimicrobial capacity, but the role of MPO in this activity is questionable. PLG might represent a useful strategy against postoperative infections. However, additional research should elucidate its exact antimicrobial activity. © 2007 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res 26:404,410, 2008 [source] Topical bovine thrombin: a 21-year review of topical bovine thrombin spontaneous case safety reports submitted to FDA's Adverse Event Reporting SystemPHARMACOEPIDEMIOLOGY AND DRUG SAFETY, Issue 2 2010John A. Clark MD Abstract Purpose To review topical bovine thrombin spontaneous adverse event (AE) reports that were forwarded to the US Food and Drug Administration's (FDA) Adverse Event Reporting System (AERS) between January 1986 and December 2006. Methods Forty-one spontaneous AE reports were summarized for reported AE profile and chronological reporting patterns. Each AE report was adjudicated by a hematologist for the topical bovine thrombin product that was given and the AE(s) that were reported. AEs were grouped as allergic, coagulopathy/bleeding, and all other AEs combined. Grouped AE serial analyses were carried out using successive 3-year time increments between 1986 (the year an AE report was first noted for a bovine thrombin product) and 2006 (the first full year that was available at the time of initiation of the data summary). Main outcome measures The primary outcome measures were every 3-year trend lines for all-AE reports, all reporters, and topical bovine thrombin brand mentions for 2 AE groups of interest (allergic events and coagulopathy/bleeding events). Results The all-AE spontaneous reporter trend showed a downward appearance for AE reporting activity that started in 1995,1998 and continued through 2004,2006. The all-AE reports trend showed two potential safety signals that could be identified serially: (1) a prominent 1989,1991 peak that was attributable to allergic events (in particular, anaphylaxis), and (2) a small 1995,2000 broad peak that was attributable in part to coagulopathy/bleeding events. Allergic events were predominantly reported with products approved prior to 1995, were not temporally associated with prior medical literature case reports, and continued to be forwarded to the FDA at low levels up to the end of this study in 2006. Coagulopathy/bleeding events were reported only with products approved prior to 1995, were temporally associated with medical literature case reports, and were not forwarded to the FDA after 2000. Conclusions Overall, spontaneous AE reporting for topical bovine thrombin occurs at very low levels, and appears to have been decreasing since 1995. The serial reporting patterns for topical bovine thrombin are best explained as a strong safety signal for allergic events with ongoing, low level reporting, and a weak safety signal for coagulopathy/bleeding events that ceased on or before 2000. Although this descriptive trend analysis cannot measure associations or causation, the coagulopathy/bleeding signal may have been prompted by multiple, antecedent published case reports. The subsequent diminishment of signal attributed to thrombin likewise may coincide with lack of such reporting in larger follow-up clinical trials or, alternatively, in the introduction and growing market share of thrombin brands of greater purity. Currently marketed topical bovine thrombin formulations are rarely volunteered as possible causes of adverse events. Copyright © 2009 John Wiley & Sons, Ltd. [source] Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved proteinPROTEIN SCIENCE, Issue 6 2002Abel Baerga-Ortiz Abstract The epitope of a monoclonal antibody raised against human thrombin has been determined by hydrogen/deuterium exchange coupled to MALDI mass spectrometry. The antibody epitope was identified as the surface of thrombin that retained deuterium in the presence of the monoclonal antibody compared to control experiments in its absence. Covalent attachment of the antibody to protein G beads and efficient elution of the antigen after deuterium exchange afforded the analysis of all possible epitopes in a single MALDI mass spectrum. The epitope, which was discontinuous, consisting of two peptides close to anion-binding exosite I, was readily identified. The epitope overlapped with, but was not identical to, the thrombomodulin binding site, consistent with inhibition studies. The antibody bound specifically to human thrombin and not to murine or bovine thrombin, although these proteins share 86% identity with the human protein. Interestingly, the epitope turned out to be the more structured of two surface regions in which higher sequence variation between the three species is seen. [source] | ||||||||||