Erythropoietin Slows Photoreceptor Cell Death in a Mouse Model of Autosomal Dominant Retinitis Pigmentosa.

Purpose: To test the efficacy of systemic gene delivery of a mutant form of erythropoietin (EPO-R76E) that has attenuated erythropoietic activity, in a mouse model of autosomal dominant retinitis pigmentosa.

Methods: Ten-day old mice carrying one copy of human rhodopsin with the P23H mutation and both copies of wild-type mouse rhodopsin (hP23H RHO+/-,mRHO+/+) were injected into the quadriceps with recombinant adeno-associated virus (rAAV) carrying either enhanced green fluorescent protein (eGFP) or EpoR76E. Visual function (electroretinogram) and retina structure (optical coherence tomography, histology, and immunohistochemistry) were assessed at 7 and 12 months of age.

Interaction of novel thiocolchicine analogs with the tubulin isoforms from bovine brain.

The antimitotic alkaloid colchicine binds to tubulin and inhibits microtubule assembly. Recently a new series of colchicine derivatives has been synthesized in which the seven-membered B-ring was shortened to a six-membered ring. In an effort to study the role of the B-ring substituents in this new series, we have studied the interaction of two compounds of this series, THC 5 and THC 18, with tubulin isoforms from bovine brain.

Differential assembly kinetics of alpha-tubulin isoforms in the presence of paclitaxel.

The antitumor drug paclitaxel (PTX) inhibits cell growth by binding to microtubules, the eukaryotic structures consisting of alpha- and beta-tubulin. PTX also promotes the assembly to tubulin in the absence of microtubule-associated proteins. Although recent studies have implicated beta-tubulin as the site of PTX binding, no information is available that relates alpha-tubulin to the binding site.

Phenotypes and protein-epitope phenotypic variation among fresh isolates of Trichomonas vaginalis.

Fresh isolates of Trichomonas vaginalis were examined for reactions to a panel of five monoclonal antibodies (MAbs). Four MAbs (C20A3, DM126, DM116, and C55) were to distinct surface immunogens and one MAb (L64) was to a cytoplasmic component. The fresh isolates were evaluated by indirect immunofluorescence (IF), immunoblotting, and radioimmunoprecipitation.

Monoclonal antibody to a major glycoprotein immunogen mediates differential complement-independent lysis of Trichomonas vaginalis.

An immunoglobulin G type 2a (IgG2a) monoclonal antibody (MAb), designated C20A3, which reacts with a highly immunogenic trichomonad membrane glycoprotein (approximately 270,000 daltons), produced complement-independent cytolysis of Trichomonas vaginalis organisms. Time- and temperature-dependent lysis of parasites was observed following incubation of washed, live T. vaginalis with certain concentrations of C20A3 IgG.