Controlled preparation of thin fibrin films immobilized at solid surfaces

Riedel, Tomáš; Brynda, Eduard; Dyr, Jan E.; Houska, Milan

doi:10.1002/jbm.a.31755

Cited by 43 publications

(61 citation statements)

References 23 publications

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“…9,35 Fibrinogen at a concentration of 10 μg/mL in Tris buffer (consisting of 50 mM Tris-HCl, 100 nM NaCl, and 2.5 mM CaCl 2 ) was adsorbed on the membrane surface for 1 hour. After being rinsed with Tris buffer, the adsorbed fibrinogen was activated with thrombin (2.5 U/mL in Tris buffer) for 15 minutes.…”

Section: Preparation Of Fibrin and Collagen Nanocoating With Attachedmentioning

confidence: 99%

Protein nanocoatings on synthetic polymeric nanofibrous membranes designed as carriers for skin cells

Bačáková¹,

Pajorová²,

Stránská³

et al. 2017

IJN

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Protein-coated resorbable synthetic polymeric nanofibrous membranes are promising for the fabrication of advanced skin substitutes. We fabricated electrospun polylactic acid and poly(lactide- co -glycolic acid) nanofibrous membranes and coated them with fibrin or collagen I. Fibronectin was attached to a fibrin or collagen nanocoating, in order further to enhance the cell adhesion and spreading. Fibrin regularly formed a coating around individual nanofibers in the membranes, and also formed a thin noncontinuous nanofibrous mesh on top of the membranes. Collagen also coated most of the fibers of the membrane and randomly created a soft gel on the membrane surface. Fibronectin predominantly adsorbed onto a thin fibrin mesh or a collagen gel, and formed a thin nanofibrous structure. Fibrin nanocoating greatly improved the attachment, spreading, and proliferation of human dermal fibroblasts, whereas collagen nanocoating had a positive influence on the behavior of human HaCaT keratinocytes. In addition, fibrin stimulated the fibroblasts to synthesize fibronectin and to deposit it as an extracellular matrix. Fibrin coating also showed a tendency to improve the ultimate tensile strength of the nanofibrous membranes. Fibronectin attached to fibrin or to a collagen coating further enhanced the adhesion, spreading, and proliferation of both cell types.

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Section: Preparation Of Fibrin and Collagen Nanocoating With Attachedmentioning

confidence: 99%

Protein nanocoatings on synthetic polymeric nanofibrous membranes designed as carriers for skin cells

Bačáková¹,

Pajorová²,

Stránská³

et al. 2017

IJN

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“…41 Human fibrinogen and human thrombin are commercially available, and in our study both chemicals were purchased from international well-known companies and therefore no ethical approval was required.…”

Section: Preparation Of a Fibrin Nanocoating On Pla Membranesmentioning

confidence: 99%

The potential applications of fibrin-coated electrospun polylactide nanofibers in skin tissue engineering

Bačáková¹,

Musı́lková²,

Riedel³

et al. 2016

IJN

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Fibrin plays an important role during wound healing and skin regeneration. It is often applied in clinical practice for treatment of skin injuries or as a component of skin substitutes. We prepared electrospun nanofibrous membranes made from poly( l -lactide) modified with a thin fibrin nanocoating. Fibrin surrounded the individual fibers in the membrane and also formed a thin fibrous mesh on several places on the membrane surface. The cell-free fibrin nanocoating remained stable in the cell culture medium for 14 days and did not change its morphology. On membranes populated with human dermal fibroblasts, the rate of fibrin degradation correlated with the degree of cell proliferation. The cell spreading, mitochondrial activity, and cell population density were significantly higher on membranes coated with fibrin than on nonmodified membranes, and this cell performance was further improved by the addition of ascorbic acid in the cell culture medium. Similarly, fibrin stimulated the expression and synthesis of collagen I in human dermal fibroblasts, and this effect was further enhanced by ascorbic acid. The expression of beta 1 -integrins was also improved by fibrin, and on pure polylactide membranes, it was slightly enhanced by ascorbic acid. In addition, ascorbic acid promoted deposition of collagen I in the form of a fibrous extracellular matrix. Thus, the combination of nanofibrous membranes with a fibrin nanocoating and ascorbic acid seems to be particularly advantageous for skin tissue engineering.

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“…Fibrinogen layers were washed with buffer and contrasted with 5% uranyl acetate in water for 5 minutes, 32 washed with water, dehydrated with a series of water-ethanol solutions with an increasing ethanol concentrations (0%, 25%, 50%, 75%, 100%), and dried in a flow box. 33 The carbon film was floated from the mica at water level and deposited on a microscope grid. The samples were observed using JEOL JEM-1010 and JEOL 200CX transmission electron microscopes at 100 kV.…”

Section: Transmission Electron Microscopymentioning

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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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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Controlled preparation of thin fibrin films immobilized at solid surfaces

Cited by 43 publications

References 23 publications

Protein nanocoatings on synthetic polymeric nanofibrous membranes designed as carriers for skin cells

Protein nanocoatings on synthetic polymeric nanofibrous membranes designed as carriers for skin cells

The potential applications of fibrin-coated electrospun polylactide nanofibers in skin tissue engineering

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

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