An automated framework for 3D serous pigment epithelium detachment segmentation in SD-OCT images.

Pigment epithelium detachment (PED) is an important clinical manifestation of multiple chorioretinal diseases, which can cause loss of central vision. In this paper, an automated framework is proposed to segment serous PED in SD-OCT images. The proposed framework consists of four main steps: first, a multi-scale graph search method is applied to segment abnormal retinal layers; second, an effective AdaBoost method is applied to refine the initial segmented regions based on 62 extracted features; third, a shape-constrained graph cut method is applied to segment serous PED, in which the foreground and background seeds are obtained automatically; finally, an adaptive structure elements based morphology method is applied to remove false positive segmented regions.

Inhibitory antibodies to human angiotensin-converting enzyme: fine epitope mapping and mechanism of action.

Angiotensin I-converting enzyme (ACE), a key enzyme in cardiovascular pathophysiology, consists of two homologous domains (N and C), each bearing a Zn-dependent active site. We modeled the 3D-structure of the ACE N-domain using known structures of the C-domain of human ACE and the ACE homologue, ACE2, as templates. Two monoclonal antibodies (mAb), 3A5 and i2H5, developed against the human N-domain of ACE, demonstrated anticatalytic activity.

Monoclonal antibodies 1B3 and 5C8 as probes for monitoring the integrity of the C-terminal end of soluble angiotensin-converting enzyme.

Angiotensin-converting enzyme (ACE) is a membrane-anchored ectoprotein that is proteolytically cleaved, yielding an enzymatically active soluble ACE. Two mouse monoclonal antibodies, MAbs 1B3 and 5C8, were generated to the C-terminal part of human soluble ACE. MAb 1B3 recognized the catalytically active ACE, as revealed by ELISA and precipitation assays, whereas Western blotting and immunohistochemisty on paraffin- embedded sections using MAb 5C8 detected denatured ACE.

Selective rat lung endothelial targeting with a new set of monoclonal antibodies to angiotensin I-converting enzyme.

We demonstrated previously that monoclonal antibody (mAb) 9B9 to angiotensin-converting enzyme (ACE) accumulates selectively in the rat lung after systemic injection and thus is a powerful tool for immunotargeting therapeutic agents/genes to the lung microvasculature. Bearing in mind the tremendous research and therapeutic potential of lung immunotargeting via ACE, we generated a novel set of mAbs to rat ACE in order to enhance the repertoire of mAbs suitable for targeting drugs/genes to the rat lung. Five new mAbs recognizing different epitopes on rat ACE were examined for their efficacy to bind rat ACE both in vitro and in vivo.