Albumin Catabolism

Waldmann, Thomas A.

doi:10.1016/b978-0-08-019603-9.50018-1

Cited by 22 publications

(15 citation statements)

References 55 publications

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“…Human serum albumin has a turnover period of 21 days [27]. Therefore, the samples were incubated under physiologically elevated glucose concentration for the same period, prior to structural and functional analysis.…”

Section: Resultsmentioning

confidence: 99%

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Vitamin D prevents glycation of proteins: an in vitro study

2016

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Human serum albumin (HSA) is an important protein involved in the transport of hormones, fatty acids, drugs, and other macromolecules. Under hyperglycemic conditions, this molecule undergoes irreversible modification that affects its structure and function. In this study, we explored the effect of two forms of vitamin D, a nutraceutical, on glycation modification in HSA. The protein was incubated with a physiologically high concentration of glucose in the presence of vitamin D metabolites. After 21 days, samples were tested for secondary structural changes, side chain modification, and the presence of advanced glycation end products. Vitamin D metabolites could reduce glycation modification, albeit only to a small extent. Interaction studies reveal that Vitamin D interaction with HSA can prevent protein glycation.Keywords: calcitriol; glycation; protein Type 2 Diabetes is a global health issue growing at an unprecedented rate. The disease accounts for 90% of diabetes cases worldwide and is characterized by defects in glucose metabolism [1]. Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].Modification of protein structure and function by AGEs is consistent with the progression of diabetic complications and correlates positively with the severity of conditions like retinopathy, neuropathy, and nephropathy [3]. Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].Human serum albumin (HSA) frequently undergoes Maillard reaction to from covalently cross-linked composites [3]. In normal adults, 6-10% of lysine chains are modified by nonenzymatic glycation, however, this number increases by 2-3 folds in individuals suffering from diabetes [5]. This may interfere with HSA function [5]. Since HSA is involved in the transportation of several moieties: nutrients, steroids, and a wide variety of drugs this can have detrimental physiological effects [6].Research suggests that vitamin D is involved in controlling AGE-associated damage in both diabetes and heart disorders [7]. Vitamin D is a fat-soluble micronutrient which is produced in the body by UV irradiation of a precursor steroid stored in the skin. The functionally active form of vitamin D, calcitriol, has a wide array of health implications [8]. Multiple studies have demonstrated its ability in limiting oxidative damage and regulating the status of a potent cellular antioxidant-reduced glutathione (GSH) [7]. Vitamin D deficiency is thought to be a risk factor for the development of diabetes; Low vitamin D status is associated with increased insulin resistance, glycated hemoglobin (HbA1c), and AGE formation [9][10][11]. Previous reports have correlated low circulating concentrations of vitamin D with increased risk of diabetic macrovascular and microvascular complications: mainly nephropathy a...

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Section: Resultsmentioning

confidence: 99%

“…Calcitriol and cholecalciferol were docked to HSA using AutoDock Vina [25]. HSA has three domains [27,28]. Studies show that calcitriol and cholecalciferol can bind to domains 2 and 3 of HSA via noncovalent bonds (Figs 9 and 10) However, the binding affinity for both vitamin D metabolites is greater for domain 2.…”

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confidence: 99%

Vitamin D prevents glycation of proteins: an in vitro study

2016

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“…The effect of non anti-denaturants steroidal drugs, such as BS, on serum albumin denaturation and aggregation is currently studied by thermo-chemical, optical turbidity and HPLC methods [125,126]. It was shown that fatty acids and BS are by far more active than other substances and operate at very low surfactant/protein mass ratios.…”

Section: Discussionmentioning

confidence: 99%

Supra-molecular Association and Polymorphic Behaviour In Systems Containing Bile Acid Salts

2007

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A wide number of supra-molecular association modes are observed in mixtures containing water and bile salts, BS, (with, eventually, other components). Molecular or micellar solutions transform into hydrated solids, fibres, lyotropic liquid crystals and/or gels by raising the concentration, the temperature, adding electrolytes, surfactants, lipids and proteins. Amorphous or ordered phases may be formed accordingly. The forces responsible for this very rich polymorphism presumably arise from the unusual combination of electrostatic, hydrophobic and hydrogen-bond contributions to the system stability, with subsequent control of the supra-molecular organisation modes. The stabilising effect due to hydrogen bonds does not occur in almost all surfactants or lipids and is peculiar to bile acids and salts. Some supra-molecular organisation modes, supposed to be related to malfunctions and dis-metabolic diseases in vivo, are briefly reported and discussed.

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“…Albumin is catabolized through a first-order process at sites distributed throughout the vascular endothelium or in a compartment in rapid equilibrium with the plasma compartment [7,9,10]. When the plasma albumin concentration is decreased the absolute rate of albumin catabolism would be expected to decrease simply because the concentration of albumin having access to the catabolic sites is decreased.…”

Section: Albumin Catabolismmentioning

confidence: 99%

“…The remainder is distributed on interstitial spaces throughout the body, primarily muscle and skin. Albumin is synthesized exclusively in the liver, at a rate of between 12 and 15 g/day [4,8], and is catabolized by the vascular endothelium throughout the body with a half-life of approximately 16 days [9][10][11]. The albumin concentration may be decreased because of dilution of the plasma pool as a consequence of volume expansion, redistribution of the albumin from plasma into interstitial compartments, a decrease in the rate of albumin synthesis, an increased albumin catabolic rate, or from external albumin losses (e.g., urine, gut, transcutaneously in the case of trauma or burns, or into dialysate).…”

Section: Albumin Homeostasismentioning

confidence: 99%

Albumin Turnover in Renal Disease

Kaysen

1997

Mineral Electrolyte Metab

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Hypoalbuminemia is found in patients both with the nephrotic syndrome and with end-stage renal disease (ESRD) treated either with continuous ambulatory peritoneal dialysis (CAPD) or hemodialysis. In nephrotic patients the primary causes of hypoalbuminemia are urinary albumin losses, an inappropriate increase in the fractional catabolic rate (FCR) of albumin and an insufficient increase in the rate of albumin synthesis to replace these losses. Nevertheless, the albumin synthetic rate is increased significantly. In patients on CAPD, albumin losses into the urine and across the peritoneal membrane contribute significantly to hypoalbuminemia. In contrast to nephrotic patients, albumin FCR decreases as serum albumin falls and serum albumin levels are significantly greater than in nephrotic patients with the same external losses of albumin. CAPD patients, like nephrotic patients with normal renal function, can increase albumin synthesis to replace losses. Thus ESRD does not directly suppress albumin synthesis. In contrast, hypoalbuminemia in hemodialysis patients results from reduced albumin synthesis. The cause of decreased albumin synthesis is a combination of response to inflammation (acute-phase response) and, to a lesser extent, inadequate nutrition. There is no evidence that shifts of albumin to the extravascular space or that dilution of the plasma by volume expansion play any role in causing hypoalbuminemia in ESRD or nephrotic patients.

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Albumin Catabolism

Cited by 22 publications

References 55 publications

Vitamin D prevents glycation of proteins: an in vitro study

Vitamin D prevents glycation of proteins: an in vitro study

Supra-molecular Association and Polymorphic Behaviour In Systems Containing Bile Acid Salts

Albumin Turnover in Renal Disease

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