Serum albumin

About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.

Serum-proteins as nitrogen source for yeastlike fungi

Abstract: Investigations have been made on the growth of Candida albicans and Cryptococcus neoformans in relation to serum proteins. Auxanographic techniques showed that some strains of C. albicans utilised human albumin at pH 4·6–5·5 and others did not. All strains of C. neoformans were negative. Proteolysis was demonstrated on serum protein agar at pH 4·6–5·5 and was shown to be dependent on the pH value. The method afforded reliable strain differentiation of C. albicans. Strains with the strongest proteolytic action also grew in liquid media with serum albumin as the sole nitrogen source as well as in control media with peptone. The significance of these findings in relation to human infections with yeasts is discussed.

Topographical differences in the vascular permeability of the peripheral nervous system

Abstract: A comparative study was made on the permeability of blood vessels to serum albumin in spinal nerve roots, dorsal root ganglions and peripheral nerves of the rat. Differences in vascular permeability were demonstrated by fluorescence microscopic tracing of intravenously injected albumin labelled with fluoresceinisothiocyanate (FLA) or with Evans blue (EBA). The main findings were as follows: 1. Extramedullary parts of dorsal and ventral spinal nerve roots presented fluorescent albumin both in the walls of blood vessels and in the interstices between the nerve fibres, from the cord to the junction with the peripheral nerve. 2. Dorsal root ganglions displayed a rich accumulation of fluorescent albumin in and outside the walls of blood vessels in the capsule and in the endoneurium. In addition, large amounts of albumin were detected in the cortex, filling out the spaces between adjacent neurons. EBA was also traced in satellite cells and occasionally in neurons. 3. The endoneurium of peripheral nerves presented fluorescent albumin only in the lumen of the blood vessels, the remaining parts of the nerve fasciculi being devoid of fluorescence. The epineurium and perineurium, on the other hand, contained large amounts of fluorescent albumin both in and outside the blood vessels.

Urinary Excretion of Fatty Acid-Binding Protein Reflects Stress Overload on the Proximal Tubules

Abstract: Urinary excretion of human liver-type fatty acid-binding protein (hL-FABP), which is expressed in human proximal tubules and engaged in free fatty acid (FFA) metabolism, was reported to reflect the clinical prognosis of chronic kidney disease. Here we have investigated the pathophysiological significance of hL-FABP in a model of protein overload nephropathy. Because L-FABP is not expressed in the wild-type mice, we generated hL-FABP chromosomal gene transgenic (Tg) mice. Tg mice were intraperitoneally injected with bovine serum albumin (BSA) replete with FFAs (r-BSA group) or FFA-depleted BSA (d-BSA group). The r-BSA group developed significantly more severe tubulointerstitial damage than did the d-BSA group. Renal expression of the hL-FABP gene was more up-regulated, and urinary excretion of hL-FABP was significantly higher, in the r-BSA group than in the d-BSA group. Furthermore, compared with their wild-type littermates injected with r-BSA, the number of infiltrated macrophages was significantly attenuated in Tg mice injected with it on day 28. In patients with kidney disease (n = 50), urinary hL-FABP was correlated with both urinary protein and the severity of tubulointerstitial injury. In conclusion, our experimental model suggests that urinary excretion of hL-FABP reflects stresses, such as urinary protein overload, on the proximal tubules. The clinical observations support this hypothesis.

Conjugation of poly-L-lysine to albumin and horseradish peroxidase: a novel method of enhancing the cellular uptake of proteins

Abstract: The carbodiimide-catalyzed conjugation of a 6700 molecular weight fragment of poly-L-lysine to radiolabeled human serum albumin or to horseradish peroxidase enhances the membrane transport of each protein into cultured mouse fibroblasts approximately 11- and 200-fold, respectively. At least 50% of the peroxidase activity remained after conjugation. Trypsinization and carbamylation of the two conjugates demonstrates that the enhancement of their cellular uptake is related to their poly-L-lysine content. Simple addition to the medium of comparable amounts of free poly-L-lysine has no effect on the transport of either native protein. Addition of poly-L-ornithine (molecular weight 200,000) at 3-30 microgram/ml, a condition known to cause enhancement of 125I-labeled human serum albumin uptake by mouse sarcoma cells, has no visible effect on the cellular uptake of native horseradish peroxidase. The intracellular localization of the enzyme-poly-L-lysine conjugate can be demonstrated cytochemically by either light or transmission electron microscopy. A concentration of conjugate that increases the uptake more than 200-fold does not cause any detectable morphological change suggestive of cell toxicity. Furthermore, because poly-L-lysine is an excellent substrate for intracellular proteolytic enzymes, it can be expected to be broken down and reutilized in the cell.