Targeted biopsy strategies will require new risk stratification models that account for the increased likelihood of sampling the tumour. Crown Copyright (C) 2012 Published by Elsevier B.V. on behalf of European Association of Urology. All rights reserved.”
“Sorokina EM, Feinstein SI, Milovanova TN, Fisher AB. Identification

of the amino acid sequence that targets peroxiredoxin 6 to lysosome-like structures of lung epithelial cells. Am J Physiol Lung Cell Mol Physiol 297: L871-L880, 2009. First published August 21, 2009; doi: 10.1152/ajplung.00052.2009.-Peroxiredoxin 6 (Prdx6), an enzyme with glutathione peroxidase and PLA(2) (aiPLA(2)) activities, is highly expressed in respiratory epithelium, where it participates in phospholipid turnover and antioxidant defense. Prdx6 has been localized by immunocytochemistry and subcellular fractionation to acidic organelles (lung lamellar bodies and lysosomes) Taselisib chemical structure and cytosol. On the basis of their pH optima, we have postulated that protein Anlotinib in vivo subcellular

localization determines the balance between the two activities of Prdx6. Using green fluorescent protein-labeled protein expression in alveolar epithelial cell lines, we showed Prdx6 localization to organellar structures resembling lamellar bodies in mouse lung epithelial (MLE-12) cells and lysosomes in A549 cells. Localization within lamellar bodies/lysosomes was in the luminal compartment. Targeting to lysosome-like organelles was abolished by the deletion of amino acids 31-40 from the Prdx6 NH(2)-terminal region; deletion of the COOH-terminal region had no effect. A green fluorescent protein-labeled peptide containing only amino acids 31-40 showed lysosomal targeting that was abolished by mutation of S32 or G34 within the peptide. Studies

with mutated protein indicated that lipid binding was not necessary for Prdx6 targeting. This peptide sequence has no homology to known organellar targeting motifs. These studies indicate that the localization of Prdx6 in acidic organelles and consequent PLA(2) activity depend on a novel 10-aa peptide located at positions 31-40 of the protein.”
“Background: Studies have reported young ages at cancer diagnosis in HIV-infected persons and have suggested that HIV accelerates carcinogenesis. However, Elacridar manufacturer these comparisons did not account for differences in population age structures.\n\nObjective: To compare ages at diagnosis for non-AIDS-defining types of cancer that occur in both the AIDS and general populations, after adjustment for differences in age and other demographic characteristics between these populations.\n\nDesign: Registry linkage study.\n\nSetting: 15 HIV/AIDS and cancer registry databases in the United States.\n\nParticipants: 212 055 persons with AIDS enrolled in the U. S. HIV/AIDS Cancer Match Study from 1996 to 2007.