Surface-dependent fibrinopeptide A accessibility to thrombin

Geer, Carri B.; Rus, Ioana A.; Lord, Susan T.

doi:10.1016/j.actbio.2007.03.004

Cited by 21 publications

(16 citation statements)

References 19 publications

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“…Our data, in accordance with data from many other studies, 2,5 suggest that the adsorption of fibrinogen causes changes in its conformation that may have a further impact on its behavior toward other proteins and cell surface receptors. In addition, the TEM experiments revealed that thrombin-treated fibrinogen molecules adsorbed side-on to the surface from the low-concentration fibrinogen solution promoted the formation of a surface-attached fibrin(ogen) network better than the layer of closely packed thrombintreated fibrinogen molecules adsorbed end-on from the higher concentration ( Figure 3).…”

Section: Fibrinopeptide Release From Surface Fibrin 1703supporting

confidence: 93%

“…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.…”

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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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Section: Fibrinopeptide Release From Surface Fibrin 1703supporting

confidence: 93%

mentioning

confidence: 99%

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

Riedel

Suttnar

Brynda

et al. 2011

Blood

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“…The accessibility of thrombin to FPA is required for the conversion of adsorbed fibrinogen to fibrin. To determine differences in the conformation or orientation of the adsorbed fibrinogen and to evaluate the possibility of thrombin-fibrinogen interactions, we assayed the binding of the site-specific anti-FPA [13,15]. We saw clear differences between the materials: the antibody binding, seen as increase in layer thickness was significant on -CH 3 surfaces, but not on -COOH surfaces.…”

Section: Fibrinogen Adsorptionmentioning

confidence: 96%

“…It is known that hydrophilic surfaces adsorb the lowest amount of fibrinogen and other blood proteins, whereas hydrophobic surfaces show elevated adsorption. However, new findings reveal that the same amount of fibrinogen adsorbed on various surfaces yields significantly different fibrin formation, indicating that in addition to the fibrinogen-cell interaction also the conversion of adsorbed fibrinogen by thrombin, the pivotal enzyme of the coagulation cascade, is influenced by physicalchemical substrate properties [9,[12][13][14][15].…”

Section: Introductionmentioning

confidence: 95%

Blood coagulation on biomaterials requires the combination of distinct activation processes

et al. 2009

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“…For example, liposomes, vehicles, micelles and polymeric nanoparticles have been widely used as nanocarrier systems for targeted delivery [4,5], but the size increase and serious particle agglomeration leaded by adsorbing protein C3b, fibrinogen or immunoglobulins G, may resulting in rapid clearance from blood circulation and concentration in liver and spleen and severely compromising drug delivery to the target tissue [1,[6][7][8]. The fibrinogen-cell interaction subsequently promotes thrombin, and coagulation cascade [9]. Actually, those reactions in biology mostly occur at interfaces [10,11], thus it is very necessary for surface modification to inhibit or prevent protein adsorption [12].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

Wang

et al. 2011

Colloids and Surfaces B: Biointerfaces

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Surface-dependent fibrinopeptide A accessibility to thrombin

Cited by 21 publications

References 19 publications

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

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

Blood coagulation on biomaterials requires the combination of distinct activation processes

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

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