Inkjet micropatterning through horseradish peroxidase-mediated hydrogelation for controlled cell immobilization and microtissue fabrication.

08:00 EDT 14th August 2019 | BioPortfolio

Summary of "Inkjet micropatterning through horseradish peroxidase-mediated hydrogelation for controlled cell immobilization and microtissue fabrication."

A simple fabrication method for cell micropatterns on hydrogel substrates was developed using an inkjet printing system that induced hydrogel micropatterns. The hydrogel micropatterns were created from inks resulting in cell-adhesive and non-cell-adhesive printed regions by horseradish peroxidase-catalyzed reaction onto non-cell-adhesive and cell-adhesive hydrogel substrates, respectively, to obtain the cell micropatterns. Cell-adhesive and non-cell-adhesive regions were obtained from gelatin and alginate derivatives, respectively. The cells on the cell-adhesive regions were successfully aligned, resulting in recognizable patterns. Furthermore, the proposed system permits the patterning of multiple cell types by switching the non-cell-adhesive region to the cell-adhesive region in the presence of growing cells. Also, we could fabricate disc- and filament-shaped small tissues by degrading the non-cell-adhesive substrates having dot- and line-shaped cell adhesive micropatterns using alginate-lyase. These results indicate that our system is useful for fabrication of tailor-made cell patterns and microtissues with the shape defined by the micropattern, and will be conducive to a diverse range of biological applications.


Journal Details

This article was published in the following journal.

Name: Biofabrication
ISSN: 1758-5090


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Medical and Biotech [MESH] Definitions

The lectin wheatgerm agglutinin conjugated to the enzyme HORSERADISH PEROXIDASE. It is widely used for tracing neural pathways.

An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.

A plant genus of the family BRASSICACEAE known for the root used in hot SPICES and is the source of HORSERADISH PEROXIDASE which is widely used in laboratories.

A 66-kDa peroxidase found in EOSINOPHIL granules. Eosinophil peroxidase is a cationic protein with a pI of 10.8 and is comprised of a heavy chain subunit and a light chain subunit. It possesses cytotoxic activity towards BACTERIA and other organisms, which is attributed to its peroxidase activity.

An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

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