1,903 research outputs found

    Post cardiac surgery diaphragmatic spasm successfully treated with gabapentin

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    We describe the case of an 82 year old woman developing severe respiratory functional impairment after open heart surgery and subsequent surgical pericardial drainage inducing diaphragmatic spasm and successfully treated with gabapentin. (c) 2005 Elsevier Ireland Ltd. All rights reserved.We describe the case of an 82 year old woman developing severe respiratory functional impairment after open heart surgery and subsequent surgical pericardial drainage inducing diaphragmatic spasm and successfully treated with gabapentin. (c) 2005 Elsevier Ireland Ltd. All rights reserved. RI Corti, Angelo/F-7046-201

    Chromogranin A and the Tumor Microenvironment

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    Chromogranin A (CgA) is an acidic glycoprotein belonging to a family of regulated secretory proteins stored in the dense core granules of the adrenal medulla and of many other neuroendocrine cells and neurons. This protein is frequently used as a diagnostic and prognostic serum marker for a range of neuroendocrine tumors. Circulating CgA is also increased in patients with other diseases, including subpopulations of patients with non-neuroendocrine tumors, with important prognostic implications. A growing body of evidence suggests that CgA is more than a diagnostic/prognostic marker for cancer patients. Indeed, results of in vitro experiments and in vivo studies in animal models suggest that this protein and its fragments can affect several elements of the tumor microenvironment, including fibroblasts and endothelial cells. In this article, recent findings implicating CgA as a modulator of the tumor microenvironment and suggesting that abnormal secretion of CgA could play important roles in tumor progression and response to therapy in cancer patients are reviewed and discussed

    Lettere de' complimenti usate hora nelle gran corti

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    di monsignor abbate Angelo Gabrieli ... arrichite dallo stesso autore, e ridotte da lui à tutta perfettione, e poste sotto li infrascritti capiBogensignaturen: A-G¹

    How to improve exposure of tumor cells to drugs — Promoter drugs increase tumor uptake and penetration of effector drugs

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    Solid tumors are characterized by an abnormal architecture and composition that limit the uptake and distribution of antitumor drugs. Over the last two decades, drugs have been identified that improve the tumor uptake and distribution of drugs that have direct antitumor effects. We propose to refer to these drugs as promoter drugs, and as effector drugs to drugs that have direct antitumor effects. Some promoter drugs have received regulatory approval, while others are in active clinical development. This review gives an overview of promoter drugs, by classifying them according to their mechanism of action: promoter drugs that modulate tumor blood flow, modify the barrier function of tumor vessels, induce tumor cell killing, and overcome stromal barriers. Eventually, we discuss those that we feel are the main conclusions to be drawn from promoter drug research that has been performed so far, and suggest areas of future investigation to improve the efficacy of promoter drugs in cancer therapy. (C) 2011 Elsevier B.V. All rights reserved

    Isoaspartate-dependent molecular switches for integrin–ligand recognition

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    Integrins are cell-adhesion receptors that mediate cell–extracellular-matrix (ECM) and cell–cell interactions by recognizing specific ligands. Recent studies have shown that the formation of isoaspartyl residues (isoAsp) in integrin ligands by asparagine deamidation or aspartate isomerization could represent a mechanism for the regulation of integrin–ligand recognition. This spontaneous post-translational modification, which might occur in aged proteins of the ECM, changes the length of the peptide bond and, in the case of asparagine, also of the charge. Although these changes typically have negative effects on protein function, recent studies suggested that isoAsp formation at certain Asn-Gly-Arg (NGR) sites in ECM proteins have a gain-of-function effect, because the resulting isoAsp-Gly-Arg (isoDGR) sequence can mimic Arg-Gly-Asp (RGD), a well-known integrin-binding motif. Substantial experimental evidence suggests that the NGR-to-isoDGR transition can occur in vitro in natural proteins and in drugs containing this motif, thereby promoting integrin recognition and cell adhesion. In this Commentary, we review these studies and discuss the potential effects that isoAsp formation at NGR, DGR and RGD sites might have in the recognition of integrins by natural ligands and by drugs that contain these motifs, as well as their potential biological and pharmacological implications.</jats:p
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