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      Supplementation with Alfacalcidol Increases Protein Intake and Serum Albumin Concentration in Patients Undergoing Hemodialysis with Hypoalbuminemia: Possible Role of Tumor Necrosis Factor-α

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          Background: We have reported that vitamin D deficiency may be implicated in the pathogenesis of hypoalbuminemia observed in patients with end-stage renal disease, but the mechanism remains to be clarified. The aim of the present study was to determine whether supplementation with alfacalcidol might increase protein intake in hemodialyzed patients with hypoalbuminemia. Methods: Twelve patients with hypoalbuminemia under 3.5 g/dl undergoing maintenance hemodialysis and not taking active forms of vitamin D were orally supplemented with 0.5 µg of alfacalcidol daily for 8 weeks. Normalized protein catabolic rate (nPCR), an index of protein intake, and serum concentrations of albumin, interleukin-6 (IL-6), IL-1β, and soluble tumor necrosis factor-α receptor-II (sTNFR-II), an index of tumor necrosis factor-α activity, were determined before and after supplementation with alfacalcidol. Results: Supplementation with alfacalcidol increased nPCR from 0.96 ± 0.20 to 1.16 ± 0.15 g/kg/day (p < 0.005), thereby increasing serum albumin concentration from a baseline of 3.13 ± 0.35 to 3.32 ± 0.29 g/dl (p < 0.05). The baseline serum concentrations of sTNFR-II and IL-6 were markedly elevated, whereas those of IL-1β were under the detection limit. Supplementation with alfacalcidol significantly decreased serum concentration of sTNFR-II from 23.8 ± 4.38 to 19.7 ± 3.93 ng/ml (p < 0.001) but did not alter serum IL-6 concentration. Conclusion: Supplementation with alfacalcidol can increase protein intake and serum albumin concentration in hemodialyzed patients with hypoalbuminemia, probably through the suppressed tumor necrosis factor activity.

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          Most cited references 5

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          The urea reduction ratio and serum albumin concentration as predictors of mortality in patients undergoing hemodialysis.

          Among patients with end-stage renal disease who are treated with hemodialysis, solute clearance during dialysis and nutritional adequacy are determinants of mortality. We determined the effects of reductions in blood urea nitrogen concentrations during dialysis and changes in serum albumin concentrations, as an indicator of nutritional status, on mortality in a large group of patients treated with hemodialysis. We analyzed retrospectively the demographic characteristics, mortality rate, duration of hemodialysis, serum albumin concentration, and urea reduction ratio (defined as the percent reduction in blood urea nitrogen concentration during a single dialysis treatment) in 13,473 patients treated from October 1, 1990, through March 31, 1991. The risk of death was determined as a function of the urea reduction ratio and serum albumin concentration. As compared with patients with urea reduction ratios of 65 to 69 percent, patients with values below 60 percent had a higher risk of death during follow-up (odds ratio, 1.28 for urea reduction ratios of 55 to 59 percent and 1.39 for ratios below 55 percent). Fifty-five percent of the patients had urea reduction ratios below 60 percent. The duration of dialysis was not predictive of mortality. The serum albumin concentration was a more powerful (21 times greater) predictor of death than the urea reduction ratio, and 60 percent of the patients had serum albumin concentrations predictive of an increased risk of death (values below 4.0 g per deciliter). The odds ratio for death was 1.48 for serum albumin concentrations of 3.5 to 3.9 g per deciliter and 3.13 for concentrations of 3.0 to 3.4 g per deciliter. Diabetic patients had lower serum albumin concentrations and urea reduction ratios than nondiabetic patients. Low urea reduction ratios during dialysis are associated with increased odds ratios for death. These risks are worsened by inadequate nutrition.
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            Interactions of 1,25-dihydroxyvitamin D3 and the immune system.

            A series of recent discoveries indicate that the hormonal form of vitamin D3, namely, 1,25(OH)2D3 plays a role in the regulation of the immune system. Cells of the monocyte/macrophage lineage possess receptors for 1,25(OH)2D3 regardless of their activation stage; cells of the lymphoid lineage also express these receptors but only at certain stages of their differentiation pathway and upon activation. Further, 1,25(OH)2D3 promotes the differentiation of monocyte precursors towards monocyte/macrophages and enhances monocyte function in antigen presentation. In addition 1,25(OH)2D3 is a potent inhibitor of interleukin-2 (IL-2) and suppresses effector functions of both T and B lymphocytes via IL-2-dependent as well as via IL-2-independent mechanisms. The theoretical and clinical implications of these discoveries are discussed.
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              Shedding of tumor necrosis factor receptors by activated human neutrophils

               C. Nathan,  F. Porteu (1990)
              The capacity of human neutrophils (PMN) to bind tumor necrosis factor (TNF) was rapidly lost when the cells were incubated in suspension with agents that can stimulate their migratory and secretory responses. Both physiological (poly)peptides (FMLP, C5a, CSF-GM) and pharmacologic agonists (PMN, calcium ionophore A23187) induced the loss of TNF receptors (TNF-R) from the cell surface. Half-maximal loss in TNF-R ensued after only approximately 2 min with 10(-7) M FMLP at 37 degrees C, and required only 10(-9) M FMLP during a 30-min exposure. However, there were no such changes even with prolonged exposure of PMN to FMLP at 4 degrees or 16 degrees C. Scatchard analysis revealed loss of TNF- binding sites without change in their affinity (Kd approximately 0.4 nM) as measured at incompletely modulating concentrations of FMLP, C5a, PMA, or A23187. The binding of anti-TNF-R mAbs to PMN decreased in parallel, providing independent evidence for the loss of TNF-R from the cell surface. At the same time, soluble TNF-R appeared in the medium of stimulated PMN. This inference was based on the PMN- and FMLP-dependent generation of a nonsedimentable activity that could inhibit the binding of TNF to fresh human PMN or to mouse macrophages, and the ability of mAbs specific for human TNF-R to abolish inhibition by PMN-conditioned medium of binding of TNF to mouse macrophages. Soluble TNF-R activity was associated with a protein of Mr approximately 28,000 by ligand blot analysis of cell-free supernatants of FMLP-treated PMN. Thus, some portion of the FMLP-induced loss of TNF-R from human PMN is due to shedding of TNF-R. Shedding was unaffected by inhibitors of serine and thiol proteases and could not be induced with phosphatidylinositol- specific phospholipase C. Loss of TNF-R from PMN first stimulated by other agents may decrease their responsiveness to TNF. TNF-R shed by PMN may be one source of the TNF-binding proteins found in body fluids, and may blunt the actions of the cytokine on other cells.

                Author and article information

                Blood Purif
                Blood Purification
                S. Karger AG
                July 2004
                30 March 2004
                : 22
                : 2
                : 210-215
                aHemodialysis Unit and bFirst Department of Medicine, Hamamatsu University School of Medicine, Hamamatsu; cDepartment of Nephrology, Seirei Mikatagahara General Hospital, Hamamatsu and dDepartment of Nephrology, Iwata Municipal Hospital, Iwata, Japan
                76855 Blood Purif 2004;22:210–215
                © 2004 S. Karger AG, Basel

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                Figures: 1, Tables: 1, References: 39, Pages: 6
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