Surface plasmon resonance analysis of immobilized fibrinogen and fibrin and their interaction with thrombin and fibrinogen

Dyr, Jan E.; Jiroušková, Markéta; Ryšavá, Jitka; Tichý, Ivo; Tobiška, Petr; Slavı́k, Radan; Homola, Jiřı́; Suttnar, Jiřı́

doi:10.1117/12.336928

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“…37 It should be noted that both our results and those of others have previously indicated no lag phase (delay) in the thrombin-mediated release of FpB from the fibrinogen adsorbed on glass surfaces, and on negatively and positively charged or hydrophobic and hydrophilic surfaces. 27,28,31,38 Blombäck and Bark also found no delay in the release of FpB 24 in their experimentation with whole blood and platelet-rich plasma, in which FpB was released almost as quickly as FpA. To explain these observations, they suggested that the binding of fibrinogen to the platelet receptor GPIIb/IIIa may induce conformational changes in bound fibrinogen, resulting in the exposure of a thrombin-susceptible cleavage site and thus facilitating FpB release.…”

Section: Fibrinopeptide Release From Surface Fibrin 1703mentioning

confidence: 91%

“…The interaction of surface-bound fibrin with fibrinogen was proven previously. 31 Fibrinopeptide release from fibrinogen in solution (3 mg/mL) was performed using 2.5 U/mL of thrombin. The reaction was stopped by trichloroacetic acid (final concentration, 5% m/v) at selected times, the precipitates centrifuged, and the supernatants analyzed by HPLC.…”

Section: Preparation Of Adsorbed Fibrin(ogen) and Fibrinopeptide Samplesmentioning

confidence: 99%

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Fibrinopeptides A and B release in the process of surface fibrin formation

Riedel

Suttnar

Brynda

et al. 2011

Blood

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Fibrinogen adsorption on a surface results in the modification of its functional characteristics. Our previous studies revealed that fibrinogen adsorbs onto surfaces essentially in 2 different orientations depending on its concentration in the solution: "side-on" at low concentrations and "end-on" at high concentrations. In the present study, we analyzed the thrombin-mediated release of fibrinopeptides A and B (FpA and FpB) from fibrinogen adsorbed in these orientations, as well as from surface-bound fibrinogenfibrin complexes prepared by converting fibrinogen adsorbed in either orientation into fibrin and subsequently adding fibrinogen. The release of fibrinopeptides from surface-adsorbed fibrinogen and from surface-bound fibrinogen-fibrin complexes differed significantly compared with that from fibrinogen in solution. The release of FpB occurred without the delay (lag phase) characteristic of its release from fibrinogen in solution. The amount of FpB released from end-on adsorbed fibrinogen and from adsorbed fibrinogenfibrin complexes was much higher than that of FpA. FpB is known as a potent chemoattractant, so its preferential release suggests a physiological purpose in the attraction of cells to the site of injury. The N-terminal portions of fibrin ␤ chains including residues B␤15-42, which are exposed after cleavage of FpB, have been implicated in many processes, including angiogenesis and inflammation. (Blood. 2011;117(5):1700-1706) IntroductionFibrinogen, one of the most abundant proteins in blood, plays a key role in hemostasis, inflammation, wound healing, and additional physiological and pathological processes. Immediately after blood comes in contact with artificial materials or with an injured vessel wall subendothelium, fibrinogen rapidly adsorbs on the surface and interacts with adhered activated platelets and subendothelial proteins. Numerous studies have demonstrated that fibrinogen in solution and fibrinogen adsorbed on various surfaces exhibit different properties. [1][2][3][4] For example, surface-adsorbed fibrinogen changes its conformation and thus reveals multiple binding sites that interact with the receptors on platelets and leukocytes. 5,6 These reciprocal interactions participate in the process of blood clot formation and in the inflammatory response. Platelet adhesion promoted by the deposition of fibrinogen might contribute to the development of the inflammatory response during ischemia reperfusion. The structural properties of fibrinogen play a key role in its interactions with various biomolecules and cell types.Fibrinogen is a 340-kDa plasma glycoprotein with a complex structure. The fibrinogen molecule consists of 2 identical subunits, each composed of 3 nonidentical polypeptide chains, A␣, B␤, and ␥. These chains are linked together by 29 disulfide bonds and form several structural regions, 2 distal D regions, one central E region, and 2 ␣C regions. 7 Each pair of distal nodules is linked with the central nodule by a triple helical coiled-coil connector composed of the middle po...

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