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Methods for transducing the cellular activities of mammalian cells into measurable electronic signals are important in many biotechnical applications, including biosensors, cell arrays, and other cell-based devices. This manuscript describes an approach for functionally integrating cellular activities and electrical processes in an underlying substrate. The cells are engineered with a cell-surface chimeric receptor that presents the nonmammalian enzyme cutinase. Action of this cell-surface cutinase on enzyme substrate self-assembled monolayers switches a nonelectroactive hydroxyphenyl ester to an electroactive hydroquinone, providing an electrical activity that can be identified with cyclic voltammetry. In this way, cell-surface enzymatic activity is transduced into electronic signals. The development of strategies to directly interface the activities of cells with materials will be important to enabling a broad class of hybrid microsystems that combine living and nonliving components. [ABSTRACT FROM AUTHOR]

Focuses on a study which outlined several strategies that are based on electrical, photochemical, thermal and mechanical forces for designing interfaces that are active and can signal changes in the behaviors of attached cells. Methods of surface modification; Comparison of transduction strategies; Applications for dynamic substrates.

Presents a study which described the surfaces involve in contributing to the ligand-directed binding of cells, highlighting the resistance of cellular deposition of adhesive proteins. What these surfaces are based upon; Reference to the use of the surface plasmon resonance (SPR) spectroscopy; Influential characteristics of adhesion of cells to the extracellular matrix (ECM).

Describes a procedure based on the electrochemical desorption of self-assembled monolayers to release patterned mammalian cells from the constraints of the patterns. Method used to confine cells into patterns; Techniques used to accomplish the patterning of bovine capillary endothelial cells.

The development of arrays that can profile molecular activities in cells is important to understanding signaling pathways in normal and pathological settings. While oligonucleotide arrays are now routinely used to profile global gene expression, there is still a lack of tools for profiling enzyme activities in cell lysates. This paper describes the combination of peptide arrays formed on self-assembled monolayers and mass spectrometry to provide a label-free approach for identifying patterns of enzyme activities in cell lysates. The approach is demonstrated by profiling lysine deacetylase (KDAC) activities in cell lysates of the CHRF megakaryocytic (Mk) cell line. Class-specific deacetylase inhibitors were used to show that terminal Mk differentiation of CHRF cells is marked by a pronounced decrease in sirtuin activity and by little change in activity of KDACs 1-11. This work establishes a platform that can be used to identify changes in global activity profiles of cell lysates for a wide variety of enzymatic activities. [ABSTRACT FROM AUTHOR]