Faculty Bibliography

We propose a novel Active Volume Model (AVM) which deforms in a free-form manner to minimize energy. Unlike Snakes and level-set active contours which only consider curves or surfaces, the AVM is a deforming object model that has both boundary and an interior area. When applied to object segmentation and tracking, the model alternates between two basic operations: deform according to current object prediction, and predict according to current appearance statistics of the model. The probabilistic object prediction module relies on the Bayesian Decision Rule to separate foreground (i.e., object represented by the model) and background. Optimization of the model is a natural extension of the Snakes model so that region information becomes part of the external forces. The AVM thus has the efficiency of Snakes while having adaptive region-based constraints. Segmentation results, validation, and comparison with GVF Snakes and level set methods are presented for experiments on noisy 2D/3D medical images

We propose a novel meshless deformable model for in vivo Left Ventricle (LV) 3D motion estimation and analysis based on tagged MRI (tMRI). The meshless deformable model can capture global deformations such as contraction and torsion with a few parameters, while track local deformations with Laplacian representation. In particular, the model performs well even when the control points (tag intersections) are relatively sparse. We test the performance of the meshless model on a numeric phantom, as well as in vivo heart data of healthy subjects and patients. The experimental results show that the meshless deformable model can fully recover the myocardial motion and strain in 3D

The p75 neurotrophin receptor (p75(NTR)) is expressed by neurons particularly vulnerable in Alzheimer's disease (AD). We tested the hypothesis that non-peptide, small molecule p75(NTR) ligands found to promote survival signaling might prevent Abeta-induced degeneration and synaptic dysfunction. These ligands inhibited Abeta-induced neuritic dystrophy, death of cultured neurons and Abeta-induced death of pyramidal neurons in hippocampal slice cultures. Moreover, ligands inhibited Abeta-induced activation of molecules involved in AD pathology including calpain/cdk5, GSK3beta and c-Jun, and tau phosphorylation, and prevented Abeta-induced inactivation of AKT and CREB. Finally, a p75(NTR) ligand blocked Abeta-induced hippocampal LTP impairment. These studies support an extensive intersection between p75(NTR) signaling and Abeta pathogenic mechanisms, and introduce a class of specific small molecule ligands with the unique ability to block multiple fundamental AD-related signaling pathways, reverse synaptic impairment and inhibit Abeta-induced neuronal dystrophy and death

The gene encoding the dipeptidyl peptidase-like protein DPP6 (also known as DPPX) has been associated with human neural disease. However, until recently no function had been found for this protein. It has been proposed that DPP6 is an auxiliary subunit of neuronal Kv4 K(+) channels, the ion channels responsible for the somato-dendritic A-type K(+) current, an ionic current with crucial roles in the regulation of firing frequency, dendritic integration and synaptic plasticity. This view has been supported mainly by studies showing that DPP6 is necessary to generate channels with biophysical properties resembling the native channels in some neurons. However, independent evidence that DPP6 is a component of neuronal Kv4 channels in the brain, and whether this protein has other functions in the CNS is still lacking. We generated antibodies to DPP6 proteins to compare their distribution in brain with that of the Kv4 pore-forming subunits. DPP6 proteins were prominently expressed in neuronal populations expressing Kv4.2 proteins and both types of protein were enriched in the dendrites of these cells, strongly supporting the hypothesis that DPP6 is an associated protein of Kv4 channels in brain neurons. The observed similarity in the cellular and subcellular patterns of expression of both proteins suggests that this is the main function of DPP6 in brain. However, we also found that DPP6 antibodies intensely labeled the hippocampal mossy fiber axons, which lack Kv4 proteins, suggesting that DPP6 proteins may have additional, Kv4-unrelated functions