Results: A stable complex of Re-188-HA was obtained with high radiochemical purity (>90%) and SBC-115076 low serum protein binding (2%). Biokinetic Studies showed a rapid blood clearance (T-1/2 alpha=21 min). Four hours after administration, Re-188-HA was almost totally removed from the blood by the liver due to
the selective uptake via HA-specific receptors (73.47 +/- 5.11% of the injected dose). The liver MTD in mice was similar to 40 Gy after 7.4 MBq of Re-188-HA injection.
Conclusions: Re-188-HA complex showed good stability, pharmacokinetic and dosimetric characteristics that confirm its potential as a new agent for HCC radiation therapy. (C) 2009 Elsevier Inc. All rights reserved.”
“APOBEC3 proteins are important cellular factors that restrict infection by a number of viruses, including human immunodeficiency virus type 1 (HIV-1). Previously, we found that the mouse APOBEC3 (mA3) restricts infection by mouse mammary tumor virus (MMTV) in its
natural host. Dendritic cells (DCs) are the first in vivo targets of MMTV infection. In this study, we demonstrate that mA3 expressed in target cells restricts MMTV infection in DCs ex vivo and in vivo. By comparing infection of DCs from mA3(+/+) and mA3(-/-) mice with one-hit viruses, we show that mA3 expression in target cells blocked MMTV infection at a postentry step and acted GSK2879552 together with virion-packaged mA3 to inhibit infection. Similar results were obtained upon infection of mouse DCs with HIV-1 cores pseudotyped with vesicular stomatitis virus G protein. In addition, treatment of cells or mice with lipopolysaccharide (LPS) caused increased levels of mA3 expression and rendered them resistant to MMTV infection. Alpha interferon treatment had a similar effect. This LPS-induced resistance to infection was seen only in mA3(-/-) mice and not in mA3(-/-) mice, arguing that mA3 is the major anti-MMTV restriction factor that is induced upon DC maturation. Thus, increasing the levels of this intrinsic antiretroviral factor
in vivo can lead to increased levels of restriction because of higher levels of both cell-intrinsic as well as virion-packaged APOBEC3.”
“Introduction: Aptamers previously selected against the protein core (AptA) or the tumour Talazoparib solubility dmso glycosylated (AptB) MUC1 glycoprotein have been conjugated to MAG2 and labelled with Tc-99m, for the potential use as radiopharmaceuticals for diagnostic imaging of breast cancer.
Methods: The conjugation was achieved in high yield using standard peptide coupling reactions between an amino modification oil the aptamer and the activated carboxylic group oil the ligands. The retention of the affinity of the MAG2 modified AptA for the MUC1 protein core was confirmed using a fluorescent intercalator displacement binding assay.