Journal: Clinical and Applied Thrombosis/Hemostasis

Article Title: C1-inhibitor influence on platelet activation by thrombin receptors agonists

doi: 10.1177/10760296221120422

Figure Lengend Snippet: Influence of C1INH on the kinetics of CD62P positive platelet populations upon activation with 5 μM SFLLRN. A. Representative experiment on a platelet suspension from a single healthy donor with addition of C1INH alone (black line), SFLLRN (red line) and combined SFLLRN and C1INH (blue line). B. Box plots for 6 experiments on different healthy donors. Black triangle represents the mean value. Upper and lower horizontal lines mean 25th and 75th percentile. The horizontal line in the middle of the box represents the median value. The whisker caps mean the minimal and maximal values. One-Way Repeated Measures ANOVA was used to obtain statistics at the p-value set at 0.05.

Article Snippet: C1INH (Berinert ® , CSL Behring, LLC, Kankakee, IL, USA) was kindly provided by Dr. Dominik J. Schaer, Department of Internal Medicine, The University of Zurich Hospital; C1INH was also obtained from Athens Research & Technologies, Inc. (Athens, GA, USA) and Calbiochem (San Diego, CA, USA).

Techniques: Activation Assay, Suspension, Whisker Assay

Journal: Clinical and Applied Thrombosis/Hemostasis

Article Title: C1-inhibitor influence on platelet activation by thrombin receptors agonists

doi: 10.1177/10760296221120422

Figure Lengend Snippet: Influence of C1INH on the kinetics of CD62P and PAC1 positive platelet populations upon activation with PAR1 agonists SFLLRN (A), TFLLR (B) and TFLLRN (C); PAR4 agonists AYPGKF (D) and GYPGQV (E); and ADP (F) is presented for platelet suspensions from each of 3 healthy donors. Donors differ between the experiments with different platelet activators.

Article Snippet: C1INH (Berinert ® , CSL Behring, LLC, Kankakee, IL, USA) was kindly provided by Dr. Dominik J. Schaer, Department of Internal Medicine, The University of Zurich Hospital; C1INH was also obtained from Athens Research & Technologies, Inc. (Athens, GA, USA) and Calbiochem (San Diego, CA, USA).

Techniques: Activation Assay

Journal: Complement Therapeutics

Article Title: Complement in Action: An Analysis of Patent Trends from 1976 Through 2011

doi: 10.1007/978-1-4614-4118-2_21

Figure Lengend Snippet: Activation and regulation of the complement system . Complement activation has traditionally been described as occurring through three initiation pathways (classical, lectin, and alternative). External proteases are also known to activate complement, independent of these pathways (at the level of C3 and C5), but for simplicity, they are not shown here. The classical and lectin pathways share common mechanisms and differ mainly in their initial activating components. The classical pathway is initiated by the binding of C1q to antigen-antibody complexes, while the lectin pathway is triggered by the binding of MBL or ficolins to pathogen surfaces. This binding leads in both cases to the cleavage of C2 and C4 to form the C4b2b complex (C2b refers to the protease fragment of C2, which has also been referred to as C2a in previous literature), though this activity can be blocked by the C1 inhibitor ( C1-INH ); C4b2b then promotes the cleavage of the central complement component C3 and generates both the anaphylatoxin C3a and the opsonin C3b. The production of C3b can also be promoted by the interaction of C3(H 2 O) with factor B ( fB ) and factor D ( fD ) to form an initial alternative pathway C3 convertase. C3b then combines with fB and fD to form the major alternative pathway C3 convertase ( C3bBb ), which leads to an amplification loop for further cleavage of C3. The combination of C3b with the C4b2b or C3bBb complexes leads to the formation of C5 convertases, which cleave C5 into the C5a anaphylatoxin and C5b. C5b then binds to C6, C7, C8, and C9 to form the membrane attack complex ( MAC ). To control the excessive activation of complement, soluble fH and membrane-associated regulators of complement activity ( mRCAs ) such as CR1, DAF, and MCP act as factor I ( fI ) cofactors and degrade C3b to iC3b. CD59, on the other hand, inhibits the assembly of the MAC by binding to C8 and/or C9

Article Snippet: One is the purified glycoprotein C1 esterase inhibitor (C1-INH; Cinryze/ViroPharma, Cetor/Sanquin, Berinert/CSL Behring, Lev Pharma), and the other is a C5 antibody (Eculizumab; Soliris/Alexion Pharmaceuticals).

Techniques: Activation Assay, Binding Assay, Activity Assay, Amplification, Membrane, Control