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Optical sectioning in wide-field microscopy is achieved by illumination of the object with a continuously moving single-spatial-frequency pattern and detecting the image with a smart pixel detector array. This detector performs an on-chip electronic signal processing that extracts the optically sectioned image. The optically sectioned image is directly observed in real time without any additional postprocessing.

Most current optical coherence tomography systems provide two-dimensional cross-sectional or en face images. Successive adjacent images have to be acquired to reconstruct three-dimensional objects, which can be time consuming. Here we demonstrate three-dimensional optical coherence tomography (3D OCT) at video rate. A 58 by 58 smart-pixel detector array was employed. A sample volume of 210x210x80 m3 (corresponding to 58x58x58 voxels) was imaged at 25 Hz. The longitudinal and transverse resolutions are 3 m and 9 m respectively. The sensitivity of the system was 76 dB. Video rate 3D OCT is illustrated by movies of a strand of hair undergoing fast thermal damage.

Isolated human hepatocytes provide a useful model for studying xenobiotic metabolism. However, in vitro studies using human hepatocytes are scarce due to the limited availability of this material. A new methodology is described for obtaining hepatocytes from a whole adult human liver. This procedure is based on (i) the rapid and intense in situ washing step of the organ with Eurocollins then glucose supplemented HEPES buffer (10 mM, pH 7.4) at 4 degrees in order to both minimize the warm ischemic period and remove erythrocytes, and (ii) a perfusion of collagenase solution (0.05% in 10 mM HEPES buffer at 37 degrees) throughout the portal vein according to a recirculated model. All perfused buffers are oxygenized. Hepatocyte viability averaged 85% as determined by Trypan Blue dye exclusion. The ability of these hepatocytes to catalyze certain metabolic transformations such as Phase I and Phase II reactions has been particularly investigated using the benzodiazepine drug, midazolam, as a substance probe. Freshly isolated human hepatocytes in suspension retained the ability to metabolize midazolam to its different hydroxylated derivatives--mainly the 1-hydroxy-midazolam--which was further conjugated with glucuronic acid. For a better understanding of the cytochrome P-450 mediated reactions, we studied the metabolism of midazolam in microsomal fractions prepared from twelve human livers. It was concluded that human microsomes (i) exhibited a Type I binding spectrum upon midazolam addition (Ks = 3.3 microM) and (ii) intensively metabolized the drug to its different derivatives. Furthermore, and since we demonstrated that midazolam was predominantly transformed by a single cytochrome P-450 enzyme, we could attribute the large inter-individual variations in midazolam metabolism to differences in human liver cytochrome P-450 content.