Fibronectin purification from human plasma in a packed-bed column system with gelatin immobilized PHEMA microspheres

Kayirhan-Denizli, F; Arıca, M. Yakup; Deni̇zli̇, Adil

doi:10.1163/156856201300194225

Cited by 6 publications

(3 citation statements)

References 26 publications

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“…In this study, we prepared a magnetic bioaffinity adsorbent carrying HSA for selective removal of bilirubin from human plasma. We selected magnetic poly(2‐hydroxyethyl methacrylate) (mPHEMA) beads as the support, which is one of the most widely used hydrophilic and biocompatible polymer in biomedical applications 22–26. When dealing with highly viscous mediums such as blood, contact with the magnetic adsorbent in a magnetically stabilized fluidized bed is desirable because of high convective transport rates without cell damage (i.e., hemolysis).…”

Section: Introductionmentioning

confidence: 99%

Bilirubin Removal from Human Plasma with Albumin Immobilised Magnetic Poly(2‐hydroxyethyl methacrylate) Beads

Rad

Yavuz

Kocakulak

et al. 2003

Macromolecular Bioscience

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Bioaffinity separation has a unique and powerful role as a support tool in the removal of toxic substances from human plasma. Magnetic beads have advantages as supports in comparison to conventional nonmagnetic beads because of low pressure drop, high mass transfer rates, and good fluid‐solid contact. In addition, they eliminate internal diffusion limitations. Human serum albumin (HSA) immobilised onto magnetic poly(2‐hydroxyethyl methacrylate) (mPHEMA) beads were investigated as an adsorbent for the selective bilirubin removal from human plasma. The mPHEMA beads were prepared by a modified suspension polymerisation. HSA was covalently coupled to the mPHEMA beads. Bilirubin adsorption was investigated from hyperbilirubinemic human plasma on the mPHEMA beads containing different amounts of immobilised HSA, (between 11–100 mg/g). The nonspecific bilirubin adsorption on the unmodified mPHEMA beads was 0.47 mg/g. Higher bilirubin adsorption capacities, up to 64.7 mg/g, were obtained with the HSA‐immobilised magnetic beads. Bilirubin adsorption increased with increasing temperature.Effect of HSA loading on bilirubin adsorption.magnified imageEffect of HSA loading on bilirubin adsorption.

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Section: Introductionmentioning

confidence: 99%

Bilirubin Removal from Human Plasma with Albumin Immobilised Magnetic Poly(2‐hydroxyethyl methacrylate) Beads

Rad

Yavuz

Kocakulak

et al. 2003

Macromolecular Bioscience

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“…We removed FN from the serum used in cell culture media by affinity chromatography with gelatin-sepharose 10 . After culturing cells in media containing the FN-depleted serum, we found that there was much less intracellular FN accumulation and the motility of all cortactin-manipulated cells (control, KD and rescue) was equivalent and dampened.…”

Section: Fn Is Resecreted From a Late Endosomal/lysosomal (Le/lys) Comentioning

confidence: 99%

Regulation of lysosomal secretion by cortactin drives fibronectin deposition and cell motility

Sung

Weaver

2011

BioArchitecture

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Directional cellular movement is required for various organismal processes, including immune defense and cancer metastasis. Proper navigation of migrating cells involves responding to a complex set of extracellular cues, including diffusible chemical signals and physical structural information. In tissues, conflicting gradients and signals may require cells to not only respond to the environment but also modulate it for efficient adhesion formation and directional cell motility. Recently, we found that cells endocytose fibronectin (FN) and resecrete it from a late endosomal/lysosomal (LE/Lys) compartment to provide an autocrine extracellular matrix (ECM) substrate for cell motility. Branched actin assembly regulated by cortactin was required for trafficking of FN-containing vesicles from LE/Lys to the cell surface. These findings suggest a model in which migrating cells use lysosomal secretion as a versatile mechanism to modulate the ECM environment, promote adhesion assembly and enhance directional migration.

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“…p(EGDMA–HEMA–MAH)' beads were prepared by suspension polymerization of ethyleneglycol dimethacrylate (EGDMA), 2‐hydroxyethyl methacrylate (HEMA), and MAH monomers. Poly (HEMA) was selected as the basic support material, which is one of the most widely used hydrophilic polymers in biomedical applications, by considering possible applications in direct contact with plasma,12–15 in which blood compatibility is one of the main concerns 16, 17. We present the adsorption–desorption properties of HSA onto plain and Cu(II)‐chelated p(EGDMA–HEMA–MAH) beads from aqueous solutions, containing different amounts of HSA and at different pH, and also from human serum.…”

Section: Introductionmentioning

confidence: 99%

Preparation of a novel metal‐chelate affinity beads for albumin isolation from human plasma

Odabaşı

Gari̇pcan

Deni̇zli̇

2003

J of Applied Polymer Sci

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ABSTRACT:In this study, we developed a novel approach to obtain a high protein-adsorption capacity utilizing 2-methacryloylamidohistidine (MAH) as a biollgand. MAH was synthesized by reacting methacryloyl chloride and histidine. Spherical beads, with an average size of 150 -200 m, were obtained by the radical suspension polymerization of MAH, ethyleneglycol dimethacrylate (EGDMA), and 2-hydroxyethyl methacrylate (HEMA) conducted in an aqueous dispersion medium. p(EGDMA-HEMA-MAH) beads had a specific surface area of 17.6 m 2 /g. The synthesized MAH monomer was characterized by NMR. p(EGDMA-HEMA-MAH) beads were characterized by a swelling test, FTIR, and elemental analysis. Then, Cu(II) ions were incorporated into the beads and Cu(II) loading was found to be 0.96 mmol/g. These beads, with a swelling ratio of 65% and containing 1.6 mmol MAH/g, were used in the adsorption/ desorption of human serum albumin (HSA) from both aqueous solutions and human serum. The adsorption of HSA onto p(EGDMA-HEMA-MAH) was low (8.8 mg/g). Cu(II) chelation onto the beads significantly increased the HSA adsorption (56.3 mg/g). The maximum HSA adsorption was observed at pH 8.0 Higher HSA adsorption was observed from human serum (94.6 mg HSA/g). Adsorptions of other serum proteins were obtained as 3.7 mg/g for fibrinogen and 8.5 mg/g for ␥-globulin. The total protein adsorption was determined as 107.1 mg/g. Desorption of HSA was obtained using a 0.1M Tris/HCI buffer containing 0.5M NaSCN. High desorption ratios (to 98% of the adsorbed HSA) were observed. It was possible to reuse Cu(II)-chelated p(EGDMA-HEMA-MAH) beads without significant decreases in the adsorption capacities.

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Fibronectin purification from human plasma in a packed-bed column system with gelatin immobilized PHEMA microspheres

Cited by 6 publications

References 26 publications

Bilirubin Removal from Human Plasma with Albumin Immobilised Magnetic Poly(2‐hydroxyethyl methacrylate) Beads

Bilirubin Removal from Human Plasma with Albumin Immobilised Magnetic Poly(2‐hydroxyethyl methacrylate) Beads

Regulation of lysosomal secretion by cortactin drives fibronectin deposition and cell motility

Preparation of a novel metal‐chelate affinity beads for albumin isolation from human plasma

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