No racemisation was observed. The radiopharmaceutical formulation containing 0.04 M CaCl2 allows a shelf-life of about 6 h without significant radiodefluorination.

Conclusion:

The described synthetic route yields 40% of radiochemical pure NCA 2-[F-18]fluoromethyl-L-phenylalanine within 105 min. A solution was found to reduce considerably the radiodefluorination. Addition of CaCl2 prior to deprotection limits the loss of radiofluoride to less than 10%. The calcium ions present in the final radiopharmaceutical formulation PD0332991 concentration (0.04 M) assure a shelf-life of at least 6 h. (C) 2008 Elsevier Inc. All rights reserved.”
“The chaperone GRP78 is a member of the heat-shock protein 70 (HSP70) family and is responsible for cellular homeostasis by preventing stress-induced apoptosis. GRP78 is expressed in all cells of the body. In malignant cells, which are permanently exposed to environmental stress, GRP78 is overexpressed and increased levels can be found in the cytoplasm and on the

cell membrane. Thus, GRP78 promotes tumor proliferation, survival, metastases and resistance to a wide variety of therapies. Like other tumor-specific membrane molecules, GRP78 can also be present on cancer cells in a variant form. This modification qualifies it as a target for immune surveillance and antibody responses. The fully human monoclonal IgM antibody, XAV-939 research buy SAM-6, was isolated from a gastric cancer patient and it binds to a new variant of GRP78 with a molecular weight of 82 kDa. The epitope is an O-linked carbohydrate moiety and is specific for malignant cells. These data show that

cancer-specific modifications of cell-surface protection molecules are (a) subject of an immune response and (b) ideal targets for new therapeutical approaches.”
“Introduction: This study investigated radiolabeled bacteriophages for specific detection of infection through gamma imaging. Previously, a Tc-99m-labeled M13 phage demonstrated specific binding for its host Escherichia coli in vitro and in mice through imaging.

Methods: This study was extended to phages P22, E79, VD-13 and phage 60. Each was radiolabeled with Tc-99m using the chelator MAG(3), and were evaluated for binding to host and non-host Cyclosporin A molecular weight bacteria in vitro and in a mouse infection model.

Results: In vitro, each Tc-99m-phage bound to its host at least 4-fold higher than to non-host bacteria. For example, Tc-99m-E79 showed 10- to 20-fold greater binding to host Pseudomonas aeruginosa compared to non-host Escherichia coli and Salmonella enterica, and Tc-99m-phage 60 showed 20-fold greater binding to host Klebsiella pneumoniae over non-hosts. Mice received host or non-host bacteria in one thigh, and 3 h later, the Tc-99m-phages were administered intravenously. After a further 3 It, the tissues were counted. Liver accumulation was highest for Tc-99m-E79, averaging 39% compared to an average of 13% for the other Tc-99m-phages. Animals infected with host bacteria showed infected thigh/normal thigh ratios of 14.