scholarly journals Human serum albumin inhibits prostacyclin production by endothelial cells: The relation of the inhibitory activity to sulfhydryl groups in albumin.

1991 ◽  
Vol 55 (8) ◽  
pp. 777-788 ◽  
Author(s):  
YOSHIHARU MUROHARA ◽  
YOSHIKI YUI ◽  
RYUICHI HATTORI ◽  
KAZUSHIGE KADOTA ◽  
CHUICHI KAWAI
Keyword(s):  
Endothelial Cells ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inhibitory Activity ◽  
Sulfhydryl Groups ◽  
Prostacyclin Production

scholarly journals Chemically Modified Human Serum Albumin Potently Blocks Entry of Ebola Pseudoviruses and Viruslike Particles

2017 ◽  
Vol 61 (4) ◽  
Author(s):  
Haoyang Li ◽  
Fei Yu ◽  
Shuai Xia ◽  
Yufeng Yu ◽  
Qian Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inhibitory Activity ◽  
Ebola Virus ◽  
Virus Disease ◽  
African Countries ◽  
Tropical Regions

ABSTRACT Ebola virus (EBOV), the causative pathogen of the deadly Ebola virus disease (EVD), can be transmitted via contact with EVD patients, including sexual contact with EVD survivors. At present, no licensed vaccine or therapeutic is available. In this study, we compared eight anhydride-modified proteins for their entry-inhibitory activity against the pseudovirus (PsV) carrying the envelope glycoprotein (GP) of the EBOV Zaire or Sudan species (Zaire PsV and Sudan PsV, respectively). We found that 3-hydroxyphthalic anhydride-modified human serum albumin (HP-HSA) was the most effective in inhibiting the entry of both Zaire PsV and Sudan PsV, with the 50% effective concentration being at the nanomolar level and with HP-HSA being more potent than EBOV-neutralizing antibody MIL77-2 (4G7, a component antibody of the ZMapp drug cocktail). The combination of HP-HSA and MIL77-2 exhibited a synergistic effect. HP-HSA had no obvious in vitro or in vivo toxicity. The EBOV PsV entry-inhibitory activity of HP-HSA remained intact after storage at 45°C for 8 weeks, suggesting that HP-HSA has the potential for worldwide use, including tropical regions in African countries, as either a therapeutic to treat EBOV infection or a prophylactic microbicide to prevent the sexual transmission of EBOV.

STUDIES ON LAL INHIBITORY REACTION BY HUMAN SERUM ALBUMIN AND ATIII PRODUCT

1987 ◽  
Author(s):  
R Homma ◽  
Y Miura
Keyword(s):  
Heat Treatment ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Inhibitory Activity ◽  
The Other ◽  
Chromogenic Substrate ◽  
Blood Products ◽  
Security Test

Test for pyrogenicity in human blood products using rabbit has been authorized as one of the security test, but LAL ( Limu-lus Amebocyte Lysate ) test has not been approved in Japan. We have studied the problem by using the in vitro LAL test ( endotoxin test ) for the rabbit pyrogen test of blood products expecially human serum albumin ( commercial HSA and PPF ) or ATIII products. It is well known that the LAL inhibitory reaction has been detected, although slightly, in most human serum albumin products, and therefore, the factors participating in this inhibition were investigated using commercial HSA and PPF products, and also preparations without heating in their production process. ATIII activity was assayed by two methods clotting and chromogenic substrate method: the LAL activity was assayed by gelation method ( Toxinometer, Wako-Junyaku Kogyo Co.). We found that the LAL activity in lion-heated PPF preparation ( NHPPF ) was determined to be significantly lower than heated PPF preparation ( PPF product ) from one manufactuerer, but not from others. The ATIII activity of this particular NHPPF was extremely high as compared with the other PPF. Addition of ATIII to the PPF caused a significant decrease of the LAL activity in reciprocal proportion to its increase. The LAL inhibitory activity and ATIII activity of the NHPPF were inactivated by heating at 60° C for 2.5 hrs. We also found that ATIII products from the two manufactuerers possessed remarkable LAL inhibitory activity which also induced a decrease by heat treatment at 56° C for 30 min. The ATIII activity was considered to be one of LAL inhibitory factors from the corelation between LAL reactivity and ATIII activity.

Albumin and Hydroxyethyl Starch Modulate Oxidative Inflammatory Injury to Vascular Endothelium

2004 ◽  
Vol 100 (1) ◽  
pp. 51-58 ◽  
Author(s):  
John D. Lang ◽  
Mario Figueroa ◽  
Phillip Chumley ◽  
Mutay Aslan ◽  
John Hurt ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Endothelial Cells ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Hydroxyethyl Starch ◽  
Aortic Endothelial Cells ◽  
Bovine Aortic Endothelial Cells ◽  
Aortic Endothelial

Background Human serum albumin is used clinically to maintain colloid osmotic pressure and is viewed to serve an antioxidant role in the vascular compartment via binding of redox-active metal complexes, transport of nitric oxide, and the oxidant-scavenging reactions of the single thiol of human serum albumin, cys34. Because of these potentially desirable adjunctive actions, we evaluated the purity and thiol redox state and compared the relative effects of clinically available 25% human serum albumin preparations with a starch-derived colloid, 6% hydroxyethyl starch, in in vitro models of inflammatory vascular injury. Methods Bovine aortic endothelial cell responses to chemical, enzymatic, and cell-derived reactive inflammatory mediators in the presence of human serum albumin or hydroxyethyl starch were assessed. Results The cys34 thiol of fresh human serum albumin preparations was 70-85% oxidized and contained a population of human serum albumin (approximately 25% of total) having the cys34 resistant to reduction by 2-mercaptoethanol and NaBH4. Treatment of bovine aortic endothelial cells with human serum albumin dose-dependently protected from HOCl-mediated 14C-adenine release, with this protective effect of human serum albumin not dependent on protein thiol status. Addition of human serum albumin to cell media provided no protection from the cytotoxic actions of peroxynitrite and xanthine oxidase-derived reactive species. Binding of activated polymorphonuclear leukocytes to bovine aortic endothelial cells was significantly amplified by hydroxyethyl starch and inhibited by human serum albumin administration. The binding of neutrophil-derived myeloperoxidase to bovine aortic endothelial cells, a mediator of multiple oxidative and nitric oxide-consuming reactions, was also inhibited by human serum albumin and enhanced by hydroxyethyl starch. Conclusions Clinical human serum albumin preparations show modest intrinsic non-thiol-dependent antiinflammatory properties in vitro, a phenomenon that was not observed with hydroxyethyl starch.

scholarly journals Role of the Protein Corona Derived from Human Plasma in Cellular Interactions between Nanoporous Human Serum Albumin Particles and Endothelial Cells

2017 ◽  
Vol 28 (8) ◽  
pp. 2062-2068 ◽  
Author(s):  
Mikhail V. Zyuzin ◽  
Yan Yan ◽  
Raimo Hartmann ◽  
Katelyn T. Gause ◽  
Moritz Nazarenus ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Plasma ◽  
Protein Corona ◽  
Cellular Interactions
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