Investigation of Iodothyronine Binding to Plasma Proteins in Brook Trout, Salvelinus fontinalis, Using Precipitation, Dialysis, and Electrophoretic Methods

1973 ◽  
Vol 30 (8) ◽  
pp. 1131-1140 ◽  
Author(s):  
N. W. Falkner ◽  
J. G. Eales
Keyword(s):  
Brook Trout ◽  
Plasma Proteins ◽  
Trichloroacetic Acid ◽  
Salvelinus Fontinalis ◽  
In Vivo Studies ◽  
Electrophoretic Separation ◽  
Hormone Levels ◽  
Separation Of Proteins

Over 95% of 3,5,3′-triiodo-L-thyronine (T3) or L-thyroxine (T4) up to added hormone levels of at least 5 μg/ml, were precipitated by trichloroacetic acid with plasma proteins of brook trout using a semimicro method. Hormone recovery in the precipitate was higher than with precipitation methods previously used on fish plasma.Equilibrium dialysis showed over 99% of T4 or T3 bound to plasma proteins of trout up to added hormone levels of at least 5 μg/ml.Acrylamide gel was superior to paper and particularly cellulose polyacetate as a medium for electrophoretic separation of proteins responsible for binding T3 or T4. In vitro studies at high hormone levels showed that T3 and T4 bound mainly to prealbumin-like proteins. In vivo studies at more physiological levels showed T4 bound to fast prealbumin-like, albuminlike, and β-globulin-like proteins, while T3 bound to slow prealbumin-like and probably the same albumin-like and β-globulin-like proteins as T4.

Passive solute and fluid transport in brook trout (Salvelinus fontinalis) urinary bladder epithelium

1988 ◽  
Vol 66 (4) ◽  
pp. 912-918 ◽  
Author(s):  
William S. Marshall
Keyword(s):  
Hydraulic Conductivity ◽  
Urinary Bladder ◽  
Brook Trout ◽  
Fluid Transport ◽  
Salvelinus Fontinalis ◽  
Bladder Epithelium ◽  
Solute Permeability ◽  
Tight Epithelia

The passive transport of solutes across the brook trout (Salvelinus fontinalis) urinary bladder epithelium was examined in vitro in Ussing-style membrane chambers. The low transepithelial conductance (average 0.14–0.20 mS∙cm−2) and low mannitol permeability (6.9 ± 1.4 × 10−11 cm∙s−1, mean ± SE) indicate that both the transcellular and paracellular pathways have limited solute permeability. Fluid transport measurements in in vitro bag preparations indicate low hydraulic conductivity (1.6 ± 0.4 × 10−7 cm∙s−1∙atm−1; 1 atm = 101.325 kPa) and suggest that the absorbate is hyperosmotic, 5-fold more concentrated than the bathing solutions. Voltage clamping experiments with unidirectional 22Na+ and 36Cl− fluxes indicated that Na+ passive diffusion occurs primarily via a transcellular pathway, whereas the epithelium behaves as a simple resistive barrier to Cl−; thus, a diffusional portion of the Cl− flux may be paracellular. The balance of the Cl− serosa-to-mucosa flux is nonconductive and apparently represents anion exchange. Current–voltage relations were nonlinear as is typical of some tight epithelia. Bladder urine is highly hypotonic, with sodium, potassium and chloride contents of 2.00 ± 0.36, 0.76 ± 0.19 and 1.31 ± 0.20 mM, respectively. In addition to the previously demonstrated absorptive neutral NaCl active transport, present results indicate a barrier function of the urinary bladder epithelium in which hydraulic conductivity and ion and uncharged solute permeabilities are low. These characterisitics are in turn consistent with the production in vivo of a very dilute urine.

Osmotic interaction of plasma proteins with interstitial macromolecules

1976 ◽  
Vol 231 (2) ◽  
pp. 638-641 ◽  
Author(s):  
CA Wiederhielm ◽  
LL Black
Keyword(s):  
Plasma Proteins ◽  
Ringer Solution ◽  
In Vivo Studies ◽  
Tissue Fluid ◽  
Oncotic Pressure ◽  
Mixed Solutions ◽  
Probable Role

The osmotic interaction of plasma proteins with collagen and hyaluronate has been evaluated by measuring the oncotic pressure of mixed solutions of varying composition. Collagen, despite its insolubility, exhibits a pronounced volume exclusion effect on plasma proteins, and the oncotic pressure of mixed solutions is considerably higher than that of the plasma protein stock solution. The volume exclusion of collagen on small molecules such as sucrose is negligible. A solution composed of 1.6% plasma proteins, 20% collagen, and .4% hyaluronate in Ringer solution, approximating the composition of the interstitium, was found to yield higher oncotic pressures than those previously reported from the interstitium. The probable role of impurities and degradation in the isolation process is discussed. Results reported earlier from in vitro and in vivo studies indicated that tissue oncotic pressures are considerably higher than generally recognized and that tissue fluid is in probable osmotic equilibrium with lymph in skin and muscle.

Blood protein and blood cell interactions with gold nanoparticles: the need for in vivo studies

2013 ◽  
Vol 14 (1-2) ◽  
Author(s):  
Neha B. Shah ◽  
John C. Bischof
Keyword(s):  
Gold Nanoparticles ◽  
Plasma Proteins ◽  
Protein Corona ◽  
Reticuloendothelial System ◽  
In Vivo Studies ◽  
Blood Protein ◽  
Biological Interactions ◽  
And Control

AbstractGold nanoparticles (GNPs) have gained in prominence within the field of nanomedicine with recent advancement of several embodiments to clinical trials. To ensure their success in the clinic it has become increasingly clear that a deeper understanding of the biological interactions of GNPs is imperative. Since the majority of GNPs are intended for systemic intravenous use, an immediate and critical biological interaction is between the blood and the GNP. Blood is composed of plasma proteins and cells. Both of these components can induce downstream effects upon interacting with GNPs that ultimately influence their medical impact. For instance, proteins from the blood can cover the GNP to create a biological identity through formation of a protein corona that is quite different from the originally synthesized GNP. Once in the bloodstream this protein coated GNP evokes both positive and negative physiological responses such as biodistribution into tissue for therapy (i.e., cancer) and toxicity or off target accumulation in the reticuloendothelial system (RES) that must be controlled for optimal use. In this review, we summarize predominantly in vitro studies of GNP interactions with blood plasma proteins and blood cells and make the case that more in vivo study is urgently needed to optimal design and control GNP use in medicine. In some cases where no specific GNP blood studies exist, we draw the readers’ attention to studies conducted with other types of nanoparticles as reference.

Specific glycation of albumin depends on its half-life

1993 ◽  
Vol 39 (4) ◽  
pp. 625-628 ◽  
Author(s):  
E D Schleicher ◽  
B Olgemöller ◽  
E Wiedenmann ◽  
K D Gerbitz
Keyword(s):  
Plasma Proteins ◽  
In Vivo Studies ◽  
Poor Correlation ◽  
Diabetic Patients ◽  
Albumin Concentration ◽  
Plasma Albumin ◽  
Albumin Content ◽  
Mean Blood Glucose

Abstract Some suggest that measurements of plasma fructosamine concentration should be corrected for the plasma protein (or albumin) concentration because the extent of glycation per volume depends on both protein and glucose concentrations. Several reports, however, demonstrate a poor correlation between plasma fructosamine and albumin concentrations in diabetic patients. In vitro kinetic and in vivo studies have shown that glycation is also dependent on the half-lives of plasma proteins. Because a decrease in plasma albumin diminishes its catabolism, we speculated that low albumin concentrations are associated with a greater extent of glycation on a molar basis (specific glycation) and vice versa. To test this hypothesis, we studied plasma albumin, total protein, and fructosamine in 63 nondiabetic subjects with normal plasma fasting glucose concentrations and hemoglobin A1c between 5.1% and 5.9%. Plasma fructosamine was poorly correlated with albumin concentration (r = 0.348) but a logarithmic plot of the specific glycation of albumin vs albumin concentration showed a better correlation (r = -0.842), suggesting that the kinetic considerations were operating in vivo. Therefore, because lower specific glycation of plasma albumin "compensates" for higher concentration, correction of fructosamine for albumin content in patients will overestimate mean blood glucose when albumin is low and underestimate it when albumin is high.

In vitro and in vivo studies of new cationic Zn(II)‐benzonaphthoporphyrazines as photosensitizers for PDT

2001 ◽  
Vol 5 (8) ◽  
pp. 645-651
Author(s):  
M. Peeva ◽  
M. Shopova ◽  
U. Michelsen ◽  
D. Wöhrle ◽  
G. Petrov ◽  
...  
Keyword(s):  
In Vivo Studies

Effect of caffeine on theophyliine on cerebral blood flow response to brain activation: In vitro and in vivo studies

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S198-S198
Author(s):  
Joseph R Meno ◽  
Thien-son K Nguyen ◽  
Elise M Jensen ◽  
G Alexander West ◽  
Leonid Groysman ◽  
...  
Keyword(s):  
Blood Flow ◽  
Cerebral Blood Flow ◽  
Brain Activation ◽  
In Vivo Studies ◽  
Blood Flow Response ◽  
Flow Response

Purification of the Antihemophilic Factor by Gel Filtration on Agarose

1969 ◽  
Vol 22 (03) ◽  
pp. 577-583 ◽  
Author(s):  
M.M.P Paulssen ◽  
A.C.M.G.B Wouterlood ◽  
H.L.M.A Scheffers
Keyword(s):  
Factor Viii ◽  
Plasma Proteins ◽  
Large Scale ◽  
Gel Filtration ◽  
Large Scale Preparation ◽  
Scale Preparation ◽  
Antihemophilic Factor

SummaryFactor VIII can be isolated from plasma proteins, including fibrinogen by chromatography on agarose. The best results were obtained with Sepharose 6B. Large scale preparation is also possible when cryoprecipitate is separated by chromatography. In most fractions containing factor VIII a turbidity is observed which may be due to the presence of chylomicrons.The purified factor VIII was active in vivo as well as in vitro.

Effects of Unfractionated and Low Molecular Weight Heparins on Platelet Thromboxane Biosynthesis “In Vivo”

1994 ◽  
Vol 72 (06) ◽  
pp. 942-946 ◽  
Author(s):  
Raffaele Landolfi ◽  
Erica De Candia ◽  
Bianca Rocca ◽  
Giovanni Ciabattoni ◽  
Armando Antinori ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Unfractionated Heparin ◽  
Low Molecular Weight Heparin ◽  
Primary Source ◽  
In Vivo Studies ◽  
Low Molecular Weight ◽  
Heparin Administration ◽  
To Receive

SummarySeveral “in vitro” and “in vivo” studies indicate that heparin administration may affect platelet function. In this study we investigated the effects of prophylactic heparin on thromboxane (Tx)A2 biosynthesis “in vivo”, as assessed by the urinary excretion of major enzymatic metabolites 11-dehydro-TxB2 and 2,3-dinor-TxB2. Twenty-four patients who were candidates for cholecystectomy because of uncomplicated lithiasis were randomly assigned to receive placebo, unfractionated heparin, low molecular weight heparin or unfractionaed heparin plus 100 mg aspirin. Measurements of daily excretion of Tx metabolites were performed before and during the treatment. In the groups assigned to placebo and to low molecular weight heparin there was no statistically significant modification of Tx metabolite excretion while patients receiving unfractionated heparin had a significant increase of both metabolites (11-dehydro-TxB2: 3844 ± 1388 vs 2092 ±777, p <0.05; 2,3-dinor-TxB2: 2737 ± 808 vs 1535 ± 771 pg/mg creatinine, p <0.05). In patients randomized to receive low-dose aspirin plus unfractionated heparin the excretion of the two metabolites was largely suppressed thus suggesting that platelets are the primary source of enhanced thromboxane biosynthesis associated with heparin administration. These data indicate that unfractionated heparin causes platelet activation “in vivo” and suggest that the use of low molecular weight heparin may avoid this complication.

Effectiveness of the integration of quercetin, turmeric, and N-acetylcysteine in reducing inflammation and pain associated with endometriosis. In-vitro and in-vivo studies

2020 ◽  
Vol 72 (5) ◽  
Author(s):  
Mario Fadin ◽  
Maria C. Nicoletti ◽  
Marzia Pellizzato ◽  
Manuela Accardi ◽  
Maria G. Baietti ◽  
...  
Keyword(s):  
In Vivo Studies
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