Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: It is concluded that a simple, three-component free-energy rule adequately describes protein adsorption from aqueous solution, at least for materials bearing varying surface concentrations of anionic (not cationic) functional groups.
107 citations
TL;DR: It is proven that C-dots showed little influence on the conformation of HSA and γ-globulins, and the interaction between C- dots and two kinds of serum proteins was driven by hydrophobic and van der waals forces.
107 citations
TL;DR: Interaction of meso-substituted anionic thiacarbocyanines with HSA results in cis-->trans isomerization and, as a consequence, an appearance and a steep rise of dye fluorescence.
107 citations
TL;DR: S-nitrosated human serum albumin dimer (SNO-HSA Dimer) could enhance the therapeutic effect of nab-PTX even in low vascular permeability or intractable pancreatic cancers.
107 citations
TL;DR: In this paper, the function of albumin in the movement of cholesterol into and out of non-cholesterol-loaded fibroblasts has been investigated, and it was shown that albumin plays a significant role in cholesterol transfer between cells and lipoproteins.
Abstract: The function of albumin in the movement of cholesterol into and out of non-cholesterol-loaded fibroblasts has been investigated. Cholesterol efflux from cholesterol labeled normal human skin fibroblasts to fatty acid-free human serum albumin (HSA) is biphasic with a rapid first phase that plateaus at about 15 min followed by a nearly linear phase up to 90 min, the longest incubation in this study. Saturation of efflux is observed at about 10 mg of albumin/mL. Efflux is specific to albumin since other molecules, such as ovalbumin or gelatin, do not induce efflux. The ability of HSA to induce cellular cholesterol efflux is low compared to reconstituted discoidal lipoprotein A-I (LpA-I). HSA at 2 mg/mL produces a rate of cholesterol efflux similar to that of LpA-I at 45 micrograms of protein/mL; however, these concentrations are within the physiological range for both HSA and apolipoprotein A-I (apoA-I). The efflux to the medium containing both LpA-I and HSA is greater than that to each of them alone but does not show complete additivity, indicating a competition between HSA and LpA-I. The HSA-mediated cholesterol movement is bidirectional as demonstrated by the transfer of cholesterol from HSA-(3H)- cholesterol complexes to fibroblasts; moreover, the HSA-mediated transfer is much faster than that from cholesterol-containing LpA-I (0.8 versus 0.2 pmol (micrograms of cell protein)-1 (90 min)-1. However, the presence of either low-density lipoprotein (LDL) or LpA-I in the incubation medium significantly inhibits the transfer of cholesterol from HSA-(3H)-cholesterol complexes to fibroblasts, thus allowing the bidirectional transfer of cholesterol between HSA and cells to possibly operate as a net efflux. In conclusion, albumin plays a significant role in cholesterol transfer between cells and lipoproteins.
107 citations