Three-dimensional optical coherence tomography of proliferative diabetic retinopathy.

Fourier-domain optical coherence tomography (OCT) was used to image the three-dimensional (3D) structures of the proliferative membrane in proliferative diabetic retinopathy. The case of a 51-year-old man with retinal detachment of the macula in his left eye is reported. The proliferative membrane covered the entire macular area. In the OCT image, the 3D structure of the proliferative membrane could be clearly visualised. The OCT image showed the presence of multiple adhesions between the retina and the proliferative membrane and separation of the proliferative membrane. The patient underwent three-port vitrectomy, and the extent and locations of the adhesions corresponded well with the findings during vitrectomy. Three-dimensional OCT is an effective tool for understanding the 3D structure of the proliferative membrane in diabetic retinopathy and is useful for training and planning of the surgical procedures in vitrectomy. To view the full report and accompanying video please go to: http://bjo.bmj.com/cgi/content/full/92/5/713/DC1. All videos from the BJO video report collection are available from: http://bjo.bmj.com/video/collection.dtl.

Structure-specific inhibition of cholesteryl ester transfer protein by azaphilones.

The effect of thirteen different fungal azaphilones, which have a common 6-iso-chromane-like ring, was tested on cholesteryl ester transfer protein (CETP) activity in vitro. Chaetoviridin B showed the most potent inhibitory activity with an IC50 value of < 6.2 microM, followed by sclerotiorin with an IC50 value of 19.4 microM. Rotiorin, chaetoviridin A and rubrorotiorin had moderate inhibitory activity (IC50 ; 30 approximately 40 microM), but others showed very weak or no inhibitory activity. The relationship between the structures and their inhibitory activity indicated that the presence of an electrophilic ketone(s) and/or enone(s) at both C-6 and C-8 positions in the isochromane-like ring is essential for eliciting CETP inhibitory activity. The transfer activity of both CE and TG was inhibited by sclerotiorin to approximately the same extent (IC50: 14.4 and 10.3 microM, respectively). A model of the reaction suggested that sclerotiorin reacts with a primary amine of amino acids such as lysine in the protein to form a covalent bond.