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      Association between Inflammation and Malnutrition as Risk Factors of Cardiovascular Disease

      Blood Purification

      S. Karger AG

      High-density lipoprotein, Vascular endothelium, Sarcopenia

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          Abstract

          Cardiovascular disease is the leading cause of death among dialysis patients. The relative risk of mortality increases as serum albumin concentration and body mass index decline. While these are generally associated with nutritional status, inflammation causes sarcopenia and decreased albumin concentration by reducing synthesis of proteins and increasing their catabolic rate. While inflammation can arise from atherosclerotic blood vessels, systemic inflammation from any source can alter the vascular endothelium and plasma protein composition in ways that promotes vascular injury. High-density lipoprotein synthesis is decreased and the high-density lipoprotein present is less capable of reducing inflammation. Activation of neutrophils favors lipoprotein oxidation. Surprisingly, while obesity is associated with cytokine production in patients without renal failure, as well as among dialysis patients, increased body mass index, whether reflecting muscle mass or adipose tissue, is associated with a decline in mortality rates.

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          Most cited references 24

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          NF-kappaB-induced loss of MyoD messenger RNA: possible role in muscle decay and cachexia.

          MyoD regulates skeletal muscle differentiation (SMD) and is essential for repair of damaged tissue. The transcription factor nuclear factor kappa B (NF-kappaB) is activated by the cytokine tumor necrosis factor (TNF), a mediator of skeletal muscle wasting in cachexia. Here, the role of NF-kappaB in cytokine-induced muscle degeneration was explored. In differentiating C2C12 myocytes, TNF-induced activation of NF-kappaB inhibited SMD by suppressing MyoD mRNA at the posttranscriptional level. In contrast, in differentiated myotubes, TNF plus interferon-gamma (IFN-gamma) signaling was required for NF-kappaB-dependent down-regulation of MyoD and dysfunction of skeletal myofibers. MyoD mRNA was also down-regulated by TNF and IFN-gamma expression in mouse muscle in vivo. These data elucidate a possible mechanism that may underlie the skeletal muscle decay in cachexia.
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            Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase.

            We have investigated the Cu2+ induced generation of lipid peroxides in low density lipoprotein (LDL) incubated with high density lipoprotein (HDL) and with purified paraoxonase, an enzyme normally resident on HDL. HDL (1.5 mg) and paraoxonase (20 micrograms) inhibited lipid peroxide generation in LDL by 32% and 25%, respectively after 24 h of incubation (both P < 0.01). The decrease in LDL lipid peroxides both with HDL and with paraoxonase were concentration dependent. The degree of protection offered by HDL tended to relate to its paraoxonase activity (R = 0.47; P < 0.06). Neither purified paraoxonase nor HDL chelated Cu2+ sufficiently to account for the decrease in LDL oxidation. Purified paraoxonase did not affect LDL oxidation when it had been heat inactivated. Mass transfer of lipid peroxides from LDL to HDL did not explain the protection of LDL against oxidation: the total lipid peroxides accumulating during incubation was decreased both by HDL and by paraoxonase. These results suggest a direct role for HDL in preventing atherosclerosis probably by an enzymic process which prevents the accumulation of lipid peroxides on LDL. Paraoxonase is an example of an enzyme which might possibly be involved.
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              Increased expression of the DNA-binding cytokine HMGB1 in human atherosclerotic lesions: role of activated macrophages and cytokines.

              Atherosclerosis is a chronic inflammatory response of the arterial wall to injury. High-mobility group box 1 (HMGB1) is a DNA-binding protein, which on release from cells exhibits potent inflammatory actions. We examined its expression in atherosclerotic lesions and regulation by cytokines. In atherosclerotic lesions, HMGB1 protein is expressed by endothelial cells, some intimal smooth muscle cells, and macrophages. As atherosclerosis develops and progresses from fatty streaks to fibrofatty lesion, the number of HMGB1-producing macrophages increases markedly. Studies using the THP-1 cell line indicated that HMGB1 mRNA expression could be markedly upregulated by inflammatory cytokines, interferon (IFN)-gamma, tumor necrosis factor (TNF)-alpha and also transforming growth factor (TGF)-beta. IFN-gamma, TNF-alpha, TWEAK, and TGF-beta induced an intracellular redistribution of HMGB1 and stimulated secretion by THP-1 cells and human blood monocytes. Inhibitors of MEK1/MEK2, protein kinase C, and PI-3/Akt, which inhibit lysosomal degranulation and mRNA translation, attenuated cytokine-induced HMGB1 secretion. Macrophage is the major cell type responsible for HMGB1 production in human atherosclerotic lesions. Inflammatory cytokines and TGF-beta increase HMGB1 expression and secretion by monocyte/macrophages. HMGB1 appears to be a common mediator of inflammation induced by inflammatory cytokines and is likely to contribute to lesion progression and chronic inflammation.
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                Author and article information

                Journal
                BPU
                Blood Purif
                10.1159/issn.0253-5068
                Blood Purification
                S. Karger AG
                978-3-8055-8052-6
                978-3-318-01301-6
                0253-5068
                1421-9735
                2006
                December 2005
                23 December 2005
                : 24
                : 1
                : 51-55
                Affiliations
                Division of Nephrology, Departments of Medicine and Biochemistry, University of California, Davis, Calif., and Research Service Department of Veterans Affairs Northern California Health Care System, Mather, Calif., USA
                Article
                89437 Blood Purif 2006;24:51–55
                10.1159/000089437
                16361841
                © 2006 S. Karger AG, Basel

                Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug. Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

                Page count
                Figures: 1, References: 56, Pages: 5
                Product
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/89437
                Categories
                Paper

                Cardiovascular Medicine, Nephrology

                Sarcopenia, High-density lipoprotein, Vascular endothelium

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