OBSERVATIONS OF THE EFFECT OF ORGANIC DYES AND DIPHENYLHYDANTOIN ON THE IN VITRO BINDING OF RADIOACTIVE 131I LABELED L-THYROXINE, L-TRIIODOTHYRONINE AND TETRAIODOTHYROACETIC ACID BY HUMAN ERYTHROCYTES AND SERUM PROTEINS

ABSTRACT The human erythrocyte is used as a model to study the in vitro binding of thyroid hormones to tissue proteins. Studies on the in vitro binding of 131I labeled 1-thyroxine, 1-triiodothyronine and tetraiodothyroacetic acid to human erythrocytes in buffered saline are reported. The effect of human serum, human serum albumin, the organic dyes, Evans Blue and Trypan Blue and diphenylhydantoin sodium on the binding of these labeled hormones to human erythrocytes has been studied. Evans Blue dye will block the in vitro uptake by the erythrocyte of 1-thyroxine and 1-triiodothyronine but not tetraiodothyroacetic acid. This suggests that the binding of the latter to the erythrocyte is qualitatively different than that of 1-thyroxine or 1-triiodothyronine. Trypan Blue decreased the serum binding of 1-thyroxine and tetraiodothyroacetic acid while 5,5-diphenylhydantoin reduced the serum binding of 1-thyroxine and 1-triiodothyronine. These results are in accord with the binding properties of human serum proteins for thyroid hormones as demonstrated by other techniques.

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A Peptide Found in Human Serum, Derived from the C-Terminus of Albumin, Shows Antifungal Activity In Vitro and In Vivo

Microorganisms ◽

10.3390/microorganisms8101627 ◽

2020 ◽

Vol 8 (10) ◽

pp. 1627

Author(s):

Tecla Ciociola ◽

Pier Paolo Zanello ◽

Tiziana D’Adda ◽

Serena Galati ◽

Stefania Conti ◽

...

Keyword(s):

Antifungal Activity ◽

Human Serum ◽

Fungicidal Activity ◽

Galleria Mellonella ◽

Serum Proteins ◽

Morphological Alterations ◽

C Terminus ◽

Different Sources

The growing problem of antimicrobial resistance highlights the need for alternative strategies to combat infections. From this perspective, there is a considerable interest in natural molecules obtained from different sources, which are shown to be active against microorganisms, either alone or in association with conventional drugs. In this paper, peptides with the same sequence of fragments, found in human serum, derived from physiological proteins, were evaluated for their antifungal activity. A 13-residue peptide, representing the 597–609 fragment within the albumin C-terminus, was proved to exert a fungicidal activity in vitro against pathogenic yeasts and a therapeutic effect in vivo in the experimental model of candidal infection in Galleria mellonella. Studies by confocal microscopy and transmission and scanning electron microscopy demonstrated that the peptide penetrates and accumulates in Candida albicans cells, causing gross morphological alterations in cellular structure. These findings add albumin to the group of proteins, which already includes hemoglobin and antibodies, that could give rise to cryptic antimicrobial fragments, and could suggest their role in anti-infective homeostasis. The study of bioactive fragments from serum proteins could open interesting perspectives for the development of new antimicrobial molecules derived by natural sources.

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Effect of Several Variables on the In Vitro Binding of Disopyramide to Serum Proteins

Clinical Pharmacokinetics ◽

10.2165/00003088-198400091-00025 ◽

1984 ◽

Vol 9 (Supplement 1) ◽

pp. 98-99 ◽

Cited By ~ 3

Author(s):

Leslie M. Shaw ◽

Roy Altman ◽

Bernard C. Thompson ◽

Leona Fields

Keyword(s):

Serum Proteins ◽

In Vitro Binding ◽

Several Variables ◽

Vitro Binding

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Reversible binding of 5- and 8-methoxypsoralen to human serum proteins (albumin) and to epidermis in vitro

British Journal of Dermatology ◽

10.1111/j.1365-2133.1979.tb05645.x ◽

1979 ◽

Vol 101 (6) ◽

pp. 669-677 ◽

Cited By ~ 36

Author(s):

M. ARTUC ◽

G. STUETTGEN ◽

W. SCHALLA ◽

H. SCHAEFER ◽

J. GAZITH

Keyword(s):

Human Serum ◽

Serum Proteins ◽

Reversible Binding ◽

Human Serum Proteins

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Capacity of human serum to depolymerize actin filaments

Blood ◽

10.1182/blood.v70.2.524.bloodjournal702524 ◽

1987 ◽

Vol 70 (2) ◽

pp. 524-530

Author(s):

PA Janmey ◽

SE Lind

Keyword(s):

Human Serum ◽

Actin Filaments ◽

Serum Proteins ◽

Normal Serum ◽

Slow Phase ◽

Rapid Phase ◽

Plasma Gelsolin ◽

Preferential Formation

Human blood depolymerizes filamentous (F-)actin. The interaction of actin filaments and monomers with human serum was studied by following the kinetics and extent of the depolymerization of pyrene-labeled F- actin and by analysis of serum proteins adhering to immobilized actin monomers. In physiologic Ca2+ concentrations, the depolymerization of F- actin proceeds in two stages: a rapid phase, attributed to direct severing of filaments by plasma gelsolin, and a slow phase attributed to the binding of actin monomers to vitamin D-binding protein (DBP). Without Ca2+, only the slow phase is observed. Human serum can completely depolymerize 10 to 18 mumol/L of actin, of which approximately 5 mumol/L occurs rapidly. Depolymerization can be accounted for by the normal serum concentrations of gelsolin and DBP. Fibrin(ogen) and fibronectin, which bind actin in vitro, do not contribute to the kinetics or extent of its depolymerization. Affinity chromatography and functional assays for the presence of gelsolin-actin complexes show that addition of G-actin to serum results in preferential formation of actin-DBP complexes, but that addition of F- actin to serum produces both gelsolin-actin complexes and DBP-actin complexes. The distinctive binding of actin monomers and polymers to these two serum proteins suggests a means by which their coordinated actions are maximized in vivo, from the standpoint of depolymerizing filaments and clearing monomers from the circulation.

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Evans blue dye as an indicator of albumin permeability across a brain endothelial cell monolayer in vitro

Neuroreport ◽

10.1097/wnr.0000000000001690 ◽

2021 ◽

Vol 32 (11) ◽

pp. 957-964

Author(s):

Meng-Chih Wu ◽

Jye-Lin Hsu ◽

Ted Weita Lai

Keyword(s):

Endothelial Cell ◽

Evans Blue ◽

Cell Monolayer ◽

Blue Dye ◽

Brain Endothelial Cell ◽

Endothelial Cell Monolayer ◽

Evans Blue Dye

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A Differential Interaction of Doxorubicin and Daunorubicin with Human Serum Proteins

Tumori Journal ◽

10.1177/030089168106700502 ◽

1981 ◽

Vol 67 (5) ◽

pp. 399-403 ◽

Cited By ~ 5

Author(s):

Franco Zunino ◽

Romolo A. Gambetta ◽

Adriano Zaccara ◽

Roberto Carsana

Keyword(s):

Human Serum ◽

Reaction Mechanisms ◽

Serum Proteins ◽

Covalent Bond ◽

Comparative Investigation ◽

Experimental Conditions ◽

Differential Interaction ◽

Bound Drug ◽

Human Serum Proteins

The results of a comparative investigation on the interaction of doxorubicin (adriamycin) and daunorubicin with serum proteins are reported. Whereas a strong interaction occurs in vitro between doxorubicin and human serum proteins, no appreciable binding to proteins could be detected for daunorubicin under similar experimental conditions. Since the protein-bound drug is only partially dissociated by physical procedures including gel-electrophoresis, column-chromatography and solvent extraction, the formation of a covalent bond is suggested. The doxorubicin binding to serum proteins is apparently nonselective for a class of proteins; it is strongly reduced in acid conditions and slightly dependent on the ionic strenght. Two tentative reaction mechanisms have been considered.

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Influence of antioxidant flavonoids quercetin and rutin on the in-vitro binding of neratinib to human serum albumin

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2020.118977 ◽

2021 ◽

Vol 246 ◽

pp. 118977

Author(s):

Tanveer A. Wani ◽

Ahmed H. Bakheit ◽

Seema Zargar ◽

Zahi Saad Alanazi ◽

Abdulrahman A. Al-Majed

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

In Vitro Binding ◽

Vitro Binding

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SERUM BINDING AND BILIARY CLEARANCE OF TRIIODOTHYRONINE IN COLD-ACCLIMATED RATS

Canadian Journal of Physiology and Pharmacology ◽

10.1139/y66-072 ◽

1966 ◽

Vol 44 (4) ◽

pp. 571-574 ◽

Cited By ~ 7

Author(s):

W. H. Cottle ◽

A. T. Veress

Keyword(s):

Thyroid Hormones ◽

Cold Acclimation ◽

Serum Proteins ◽

Binding Protein ◽

Biliary Clearance

The more rapid biliary clearance of thyroid hormones resulting from cold acclimation in rats may be the result of an increased capacity of the liver to remove hormone from the blood and (or) to a decreased affinity of the hormone for thyroid-binding protein. The binding of labelled L-triiodothyronine to serum proteins of cold- and warm-acclimated rats has been compared in vitro. Less label was found to bind to protein in sera from cold-acclimated rats, which suggests that a decrease in affinity of thyroid hormones for the binding protein may contribute to the increased biliary clearance found.

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