No abstract

The combination of oral contrast and polyethylene glycol solution improves the diagnostic value of MR rectography and is particularly useful when noncontrast examinations are inconclusive.

No abstract

Background: Protein transduction is a new evolving technology that allows direct delivery of proteins/peptides to cells, via fusion with small cationic cell penetrating peptides, known as protein transduction domains(PTDs). Full length proteins or peptides fused to TAT-PTD, a cell penetrating domain comprising 11 residues from transactivating domain of TAT-HIV protein, readily translocates into a wide variety of cells and tissues. We have generated a novel cytoprotective protein TAT-Ngb, consisting of human neuroglobin (Ngb) fused to TAT-PTD. Ngb is a member of oxygen binding globin family recently discovered in brain, retina and islets of Langerhans. The protein has been reported to protect neurons from hypoxia. Aims: To investigate whether TAT-Ngb could inhibit spontaneous cell death in cultured islets. Methods and Results: TAT-Ngb-FITC readily enters into cultured human islets. Efficiency of transduction was evaluated by flow cytometry and by confocal microscopy of live, unfixed islets. Human islets cultured in the presence of TAT-Ngb showed greatly improved viability and functionality of beta-cells. Islets were assessed by cell viability assay using 7AAD dye exclusion test, Newport Green-Zn binding to insulin and finally assessment of mitochondrial membrane potential by fluorescent probe TMRE. The glucose static insulin secretion assay was used to evaluate the functionality of long term-cultured islets. Conclusions: TAT-Ngb improves viability of beta cells and functionality of islets and therefore could be an asset in improvement of islets in culture conditions before transplantation.