Particularities of bone regeneration in rats after implantation of polycaprolactone scaffold mineralized with vaterite with adsorbed tannic acid

We studied the particularities of osteo- and angiogenesis in albino rats after implantation of polycaprolactone scaffolds mineralized with vaterite with adsorbed tannic acid in the femoral bone defect. It was found that the processes of angio- and osteogenesis in the bone tissue after scaffolds implantation depend on their biocompatibility. Implantation of non-biocompatible scaffolds was followed by activation of angio- and osteogenesis aimed at separation of these scaffold from surrounding tissues. Implantation of polycaprolactone/vaterite scaffolds containing tannic acid stimulated angio- and osteogenesis leading to vascularization and bone tissue formation in the matrix. This demonstrate prospects of clinical approbation of these scaffolds for stimulation of bone regeneration in traumatological and orthopedic patients

The architecture of Tetrahymena telomerase holoenzyme

Telomerase adds telomeric repeats to chromosome ends using an internal RNA template and specialized telomerase reverse transcriptase (TERT), thereby maintaining genome integrity. Little is known about the physical relationships among protein and RNA subunits within a biologically functional holoenzyme. Here we describe the architecture of Tetrahymena thermophila telomerase holoenzyme determined by electron microscopy. Six of the 7 proteins and the TERT-binding regions of telomerase RNA (TER) have been localized by affinity labeling. Fitting with high-resolution structures reveals the organization of TERT, TER, and p65 in the RNP catalytic core. p50 has an unanticipated role as a hub between the RNP catalytic core, p75-p19-p45 subcomplex, and the DNA-binding Teb1. A complete in vitro holoenzyme reconstitution assigns function to these interactions in processive telomeric repeat synthesis. These studies provide the first view of the extensive network of subunit associations necessary for telomerase holoenzyme assembly and physiological function