Lung albumin content after acid aspiration pulmonary injury
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Serum Albumin
Oncotic pressure
Purpose of review To describe the metabolism and function of albumin, and to scrutinize the evidence that infusion of albumin may be beneficial in disease. To explain why albumin infusion does not improve clinical outcome in most disease states, studied. Recent findings Albumin acts as a binding protein and an oncotic agent. However, albumin may also act as an extracellular scavenger, which leads to oxidation of albumin. It is likely that this compromises its function and it is possible that this drives its degradation. In disease, these useful processes are accelerated leading to rapid ageing of the molecule. Albumin infusion does not improve clinical outcome despite increasing oncotic pressure in chronic disease. It is not superior to nonprotein colloids or electrolyte solutions in acute hypovolemia with one or two exceptions (liver failure, possibly cerebral infarction). One potential explanation is that pharmaceutical albumin does not have the oxidative qualities that freshly synthesized albumin has. Summary Albumin infusion has not proven to achieve clinical benefit in many acute and chronic disease states with a few exceptions in acute hypovolemia (e.g. postparacentesis). Future studies should reveal whether infusion of freshly synthesized nonoxidized albumin is of greater clinical benefit.
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Abstract D ich , J., S. E. H ansen and H. I. D. T hieden . Effect of albumin concentration and colloid osmotic pressure on albumin synthesis in the perfused rat liver. Acta physiol. scand. 1973. 89. 352–358. The effect of the albumin concentration and the colloid osmotic pressure on the rate of albumin synthesis was investigated in the perfused rat liver. The albumin concentration and the colloid osmotic pressure were changed independently. With the same concentration of albumin the rate of albumin synthesis decreased 20 to 30 per cent when the colloid osmotic pressure was increased by addition of gammaglobulin. It is concluded that the rate of albumin synthesis may be regulated by the colloid osmotic pressure. The albumin concentration seems to play a role in regulation only through the contribution to the colloid osmotic pressure.
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Intravenous infusion of hyper-oncotic 20 % albumin expands the plasma volume by approximately twice the infused volume. We investigated whether the recruited fluid stems from accelerated flow of efferent lymph, which would add protein to the plasma, or from reversed transcapillary solvent filtration, where the solvent is expected to be low in protein.We analyzed data from 27 intravenous infusions of 20 % albumin (3 mL/kg; approximately 200 mL) over 30 min given to 27 volunteers and patients. Twelve of the volunteers were also given a 5 % solution and served as controls. The pattern of blood hemoglobin, colloid osmotic pressure, and the plasma concentrations of two immunoglobulins (IgG and IgM) were studied over 5 h.A decrease of the difference between the plasma colloid osmotic pressure and plasma albumin occurred during the infusions and was almost four times greater for 5 % albumin than for 20 % albumin at 40 min (P < 0.0036), which indicates that non-albumin protein enriched the plasma when 20 % was infused. Moreover, the difference between the infusion-derived dilution of the blood plasma based on hemoglobin and the two immunoglobulins amounted to -1.9 % (-6 to +0.2) for 20 % albumin and to -4.4 % (25th-75th percentile range - 8.5 to +0.2) during experiments with 5 % albumin (P < 0.001). This supports that the plasma was enriched by immunoglobulins, probably via the lymph, when 20 % was infused.Between half and two-thirds of the extravascular fluid that was recruited during infusion of 20 % albumin in humans consisted of protein-containing fluid consistent with efferent lymph.
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The passage from blood to peripheral lymph of 131I-labeled human serum albumin has been studied in 6 male patients (30-70 years) with malignancies without metastases. On the first day the concentration of radio-labeled albumin in the blood was kept almost constant by repeated i.v. injections. Lymph was collected continuously from a cannulated subcutaneous lymph vessel on the leg. Two hours after the first i.v. injection of radiolabeled albumin the lymph contained significant amounts of radioactivity in all patients. Equilibrium between radioactivity in blood and lymph was reached after 26 hrs. This indicates a long "wash out time" of unlabeled protein in the interstitial tissue from where lymph has been sampled.
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SUMMARY The albumin of liver lymph may derive entirely from the plasma or newly metabolized protein may be added directly to lymph by the liver cells. Following the injection of T‐1824 and 131 I‐albumin the disappearance of label from plasma and its appearance in liver lymph was studied. When specific activity curves were compared with similar curves for liver following injection of 131 I‐γ‐globulin, and for leg following 131 I‐albumin it was apparent that only minor amounts, if any, of new protein could be reaching the liver lymph directly from the synthesizing cells.
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The aim: to highlight the main points of albumin synthesis, posttranslational modifications and functions in normal conditions and in patients with liver cirrhosis. Key points. Albumin is the most abundant protein in blood plasma. Along with oncotic properties, albumin performs transport, antioxidant, immunomodulatory and endothelioprotective functions. Serum albumin in patient with liver cirrhosis undergoes modifications, leading to functional impairment. Human serum albumin is a compaund of human mercaptalbumin with cysteine residues having a reducing ability, and oxidized human non-mercaptalbumin. The proportion of irreversibly oxidized non-mercaptalbumin-2 with impaired functional activity increases in liver cirrhosis. Conclusion. The conformational structure of the albumin molecule plays an important role in maintaining its non-oncotic functions. Non-oncotic functions depend on albumin conformation. Further investigation of albumin conformation and albumin functions in patients with hepatic insufficiency can serve as an additional criterion for assessing the severity of cirrhosis and predictor of complications may become an additional criterion to new clinical applications and treatment strategies of liver failure.
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High-protein diets increase albumin synthesis in rats with Heymann nephritis but albuminuria increases also, causing serum albumin concentration to be suppressed further than in nephrotic animals eating a low-protein diet. Experiments were designed to determine whether dietary protein augmentation directly stimulates albumin synthesis, or whether instead increased albumin synthesis is triggered by the decrease in serum albumin concentration. Evidence is presented that dietary protein augmentation directly stimulates albumin synthesis, accompanied by a proportional increase in steady-state hepatic albumin mRNA concentration (AlbmRNA) and by an increase in AlbmRNA transcription. When the increased albuminuria resulting from dietary protein augmentation is blunted with enalapril, serum albumin concentration is shown to increase in nephrotic rats. Both albumin synthesis and AlbmRNA increase in these animals despite the greater serum albumin concentration. Albumin synthesis correlates inversely with both serum albumin and serum oncotic pressure in nephrotic rats fed 40% protein, but does not correlate with serum albumin concentration in nephrotic rats fed 8.5% protein (LP), even when serum albumin concentration is reduced. Albumin masses are preserved in LP primarily because of reduced albuminuria. Reduced serum oncotic pressure and dietary protein augmentation combine to stimulate albumin synthesis in nephrotic rats at the level of gene transcription.
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Albumin is the protein in the blood with the largest concentration. It is easy to measure, purify, and give to patients. Until recently, there has been little research on its role in the critically ill. Serum concentrations decrease rapidly with illness. Although it has several functions in healthy humans (maintenance of colloid oncotic pressure, drug transport, and free radical scavenging), how these functions change with illness is unknown. Indeed, how albumin itself changes is also unknown. To add to these difficulties in understanding the role of albumin there are relatively normal humans and also rats that lack the genes to make albumin in significant amounts. As well as the expected effects of albumin there are important other effects on blood clotting and the effects of diuretics that need to be evaluated.
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