Surfaces modified with covalently-immobilized adhesive peptides affect fibroblast population motility

Olbrich, Kevin C.; Andersen, Thomas T.; Blumenstock, Frank A.; Bizios, Rena

doi:10.1016/0142-9612(96)81412-8

Cited by 78 publications

(38 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…40,41 Surface occupancy experiments have been utilized as an index of cell population motility. 42 The increased cell adhesion coupled with decreased cell motility, as well as enhanced proliferation and matrix mineralization has been observed on surfaces (for e.g., borosilicate glass and titanium) modified with immobilized peptide sequences (such as arginine-glycine-aspartic acid-serine (RGDS) and lysinearginine-serine-arginine (KRSR) [43][44][45] ) contained in extracellular matrix proteins such as vitronectin and collagen.…”

Section: Discussionmentioning

confidence: 99%

Fabrication of nanostructured hydroxyapatite and analysis of human osteoblastic cellular response

Guo

Gough

Xiao

et al. 2007

J Biomedical Materials Res

132

View full text Add to dashboard Cite

Nano-sized hydroxyapatite (HA) powders were produced by a hydrothermal method and a precipitation method. Spark plasma sintering (SPS) was used to fabricate nanostructured HA (NHA) using nano-sized HA powders as a precursor. Conventional sintering was employed to produce microstructured HA (MHA). Characteristics of HA powders and HA bulk ceramics after sintering were investigated by XRD, FTIR, SEM, TEM, particle size distribution, and AFM. Dense compacts consisting of equiaxed grains with an average grain size of approximately 100 nm were obtained by SPS. Human osteoblasts were cultured on both NHA and MHA and cell attachment, proliferation, and mineralization were evaluated. After 90 min incubation, the cell density on NHA surface was significantly higher than that of MHA and glass control, whereas average cell area of a spread cell was significantly lower on NHA surface compared to MHA and glass control after 4 h incubation. Matrix mineralization was determined after 7 and 14 days incubation by using alizarin red assay combined with cetylpyridinium chloride extraction. NHA shows significant enhancement (p < 0.05) in mineralization compared to MHA. Results from this study suggest that NHA may be a much better candidate for clinical use in terms of bioactivity.

show abstract

Section: Discussionmentioning

confidence: 99%

Fabrication of nanostructured hydroxyapatite and analysis of human osteoblastic cellular response

Guo

Gough

Xiao

et al. 2007

J Biomedical Materials Res

132

View full text Add to dashboard Cite

show abstract

“…The RGD sequence has been shown to enhance adhesion and spreading of fibroblasts, endothelial cells and smooth muscle cells when the peptide was grafted onto different surfaces [6]. Migration of smooth muscle cells and fibroblasts has been found to be biphasically dependent on the concentration of RGD attached to the migratory surface with intermediate loadings of RGD displaying maximal mobility [7,8].…”

Section: Introductionmentioning

confidence: 98%

The selective modulation of endothelial cell mobility on RGD peptide containing surfaces by YIGSR peptides

Fittkau¹,

Zilla²,

et al. 2005

View full text Add to dashboard Cite

“…Aminophase was generated by silanization of glass with amonipropyltrimethoxysilane (A). Coupling of the analytes to this second surface was done with EDC-activation (Olbrich et al, 1996). A third surface was created by attaching 3-mercapto-propyltrimethoxysilane (MTS) and N--maleimidobutyry-loxy-succinimideester (GMBS) (Shriver-Lake et al, 1997) to the glass slips (B).…”

Section: Glass Surfacesmentioning

confidence: 99%

Current Advances in Antibody Immobilization on Different Surfaces and Beads

Hahn¹,

Bakry²,

Huck³

et al. 2008

View full text Add to dashboard Cite

Antibody immobilization is of considerable interest for miscellaneous fields of interest, e.g. detecting biomarkers in cancer diagnostics, e.g. prostate specific antigen (PSA) for prostate cancer and pathogens like Escherichia coli, a foodborne pathogen. For this purpose, specific antibody captures are required and all of them should guarantee highest reproducibility and capacity possible. Especially in clinical applications very complex and specific immunoassays are needed. However, the complexity of pinning antibodies necessitates particular methods concerning the immobilization technique itself-because of their structure and specificity-and of course the analyzing methods. Glass, polymers, gold and even fullerene beads have been used as carriers, treated with various spacers and activation steps within the last few years. Furthermore, considerable attention is drawn to the regeneration of matrices and their capabilities for further antibody attachment. Commonly applied verification tools for the detection of the trapped antibodies include impedance spectroscopy (IS), atomic fluorescence microscopy (AFM), electrophoresis (EP), enzyme linked immunosorbent assays (ELISA), quartz crystal microbalance (QCM) and infrared spectroscopy (IR). Matrix assisted laser desorption/ionization-time-offlight mass spectrometry (MALDI-TOF/MS) is also a useful tool for proving the success of new antibody fixing procedures. Immobilization techniques have been improved concerning their reproducibility, binding capacity and high specificity. In this review, recent developments of antibody (Ab) immobilization are summarized, the individual applications are mentioned, advantages and disadvantages are discussed in detail.

show abstract

Surfaces modified with covalently-immobilized adhesive peptides affect fibroblast population motility

Cited by 78 publications

References 28 publications

Fabrication of nanostructured hydroxyapatite and analysis of human osteoblastic cellular response

Fabrication of nanostructured hydroxyapatite and analysis of human osteoblastic cellular response

The selective modulation of endothelial cell mobility on RGD peptide containing surfaces by YIGSR peptides

Current Advances in Antibody Immobilization on Different Surfaces and Beads

Contact Info

Product

Resources

About