Factors contributing to high levels of plasma iodide in brook trout, Salvelinus fontinalis (Mitchill)

1975 ◽  
Vol 53 (3) ◽  
pp. 267-277 ◽  
Author(s):  
Linda A. Gregory ◽  
J. G. Eales
Keyword(s):  
Protein Interactions ◽  
Brook Trout ◽  
Plasma Proteins ◽  
Iodine Concentration ◽  
High Plasma ◽  
Natural Food ◽  
Storage Site ◽  
Tissue Storage ◽  
Commercial Diet ◽  
Protein Levels

The influences of dietary iodine, ambient iodide, tissue storage of iodide, and iodide binding to plasma proteins have been related to the high plasma iodide in laboratory brook trout.Plasma iodide exceeded 1800 μg/100 ml (μg%) for trout acclimated at 13 °C and fed an Ewos commercial diet. This was largely due to (i) efficient iodide absorption from the gut, and (ii) an iodine concentration in Ewos food (31–35 μg I/g dry wt.) that was 20–78 times greater than that of four other artificial foods or that of several natural food items.Ambient iodide ranged seasonally from 1.26 to2.21 μg I/liter. This source probably contributed little to the high plasma iodide, but helped to maintain plasma levels during starvation or use of low-iodide diets.No major extrathyroidal iodide storage site was found in 15 organs or tissues examined.Iodide binds to brook trout plasma proteins, but the concentration of binding sites is less than that reported for other species. This binding aids maintenance of plasma iodide, particularly when iodide intake is low. Variation in plasma iodide between individual fish was not clearly related to variations in iodide–protein interactions nor to variations in plasma protein levels.

Intoxication with Phenprocoumon (Marcoumar) Pharmacokinetics and Side Effects

1969 ◽  
Vol 21 (02) ◽  
pp. 320-324 ◽  
Author(s):  
K Seiler ◽  
F Duckert
Keyword(s):  
Plasma Concentration ◽  
Side Effects ◽  
Half Life ◽  
Plasma Proteins ◽  
Repeated Administration ◽  
High Plasma ◽  
Vitamin K1 ◽  
Clotting Factors ◽  
Therapeutic Concentration ◽  
High Plasma Concentration

SummaryA case of severe Marcoumar intoxication is described. Eleven hours after the intake a plasma concentration of 15.75 µg/ml was found which corresponds approximately to the 5-fold therapeutic concentration. Repeated administration of vitamin K1 made it possible to avoid extreme lowering of the activity of the clotting factors II, VII and X and to prevent bleeding. Side effects were not observed. The biologic half-life of Phenprocoumon has been found to be shortened at high plasma concentration (3.7 instead of 5.9 days). It is probable that in extreme concentration the drug is less strongly bound to the plasma proteins.

scholarly journals The liver in regulation of iron homeostasis

2017 ◽  
Vol 313 (3) ◽  
pp. G157-G165 ◽  
Author(s):  
Gautam Rishi ◽  
V. Nathan Subramaniam
Keyword(s):  
Plasma Proteins ◽  
Iron Homeostasis ◽  
Vital Role ◽  
Regulatory Function ◽  
Hepatic Iron ◽  
Storage Site ◽  
Molecular Processes ◽  
Body Iron ◽  
Functionally Diverse ◽  
And Storage

The liver is one of the largest and most functionally diverse organs in the human body. In addition to roles in detoxification of xenobiotics, digestion, synthesis of important plasma proteins, gluconeogenesis, lipid metabolism, and storage, the liver also plays a significant role in iron homeostasis. Apart from being the storage site for excess body iron, it also plays a vital role in regulating the amount of iron released into the blood by enterocytes and macrophages. Since iron is essential for many important physiological and molecular processes, it increases the importance of liver in the proper functioning of the body’s metabolism. This hepatic iron-regulatory function can be attributed to the expression of many liver-specific or liver-enriched proteins, all of which play an important role in the regulation of iron homeostasis. This review focuses on these proteins and their known roles in the regulation of body iron metabolism.

scholarly journals Analysis of RAS protein interactions in living cells reveals a mechanism for pan-RAS depletion by membrane-targeted RAS binders

2020 ◽  
Vol 117 (22) ◽  
pp. 12121-12130
Author(s):  
Yao-Cheng Li ◽  
Nikki K. Lytle ◽  
Seth T. Gammon ◽  
Luke Wang ◽  
Tikvah K. Hayes ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Developmental Disorders ◽  
Degradation Pathway ◽  
Small Gtpases ◽  
Small Gtpase ◽  
Ras Proteins ◽  
Ras Protein ◽  
Protein Levels ◽  
Ras Family ◽  
Ras Isoforms

HRAS, NRAS, and KRAS4A/KRAS4B comprise the RAS family of small GTPases that regulate signaling pathways controlling cell proliferation, differentiation, and survival. RAS pathway abnormalities cause developmental disorders and cancers. We found that KRAS4B colocalizes on the cell membrane with other RAS isoforms and a subset of prenylated small GTPase family members using a live-cell quantitative split luciferase complementation assay. RAS protein coclustering is mainly mediated by membrane association-facilitated interactions (MAFIs). Using the RAS–RBD (CRAF RAS binding domain) interaction as a model system, we showed that MAFI alone is not sufficient to induce RBD-mediated RAS inhibition. Surprisingly, we discovered that high-affinity membrane-targeted RAS binding proteins inhibit RAS activity and deplete RAS proteins through an autophagosome–lysosome-mediated degradation pathway. Our results provide a mechanism for regulating RAS activity and protein levels, a more detailed understanding of which should lead to therapeutic strategies for inhibiting and depleting oncogenic RAS proteins.

In Silico Recognition of Protein-Protein Interaction

2011 ◽  
pp. 248-268
Author(s):  
Byung-Hoon Park ◽  
Phuongan Dam ◽  
Chongle Pan ◽  
Ying Xu ◽  
Al Geist ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Regulatory Networks ◽  
Machine Learning Techniques ◽  
Translation Regulation ◽  
Future Research ◽  
Protein Protein Interactions ◽  
Protein Protein Interaction ◽  
Protein Levels ◽  
Protein Functions ◽  
Model Protein

Protein-protein interactions are fundamental to cellular processes. They are responsible for phenomena like DNA replication, gene transcription, protein translation, regulation of metabolic pathways, immunologic recognition, signal transduction, etc. The identification of interacting proteins is therefore an important prerequisite step in understanding their physiological functions. Due to the invaluable importance to various biophysical activities, reliable computational methods to infer protein-protein interactions from either structural or genome sequences are in heavy demand lately. Successful predictions, for instance, will facilitate a drug design process and the reconstruction of metabolic or regulatory networks. In this chapter, we review: (a) high-throughput experimental methods for identification of protein-protein interactions, (b) existing databases of protein-protein interactions, (c) computational approaches to predicting protein-protein interactions at both residue and protein levels, (d) various statistical and machine learning techniques to model protein-protein interactions, and (e) applications of protein-protein interactions in predicting protein functions. We also discuss intrinsic drawbacks of the existing approaches and future research directions.

Hematologic response of fish to changes in gas or hydrostatic pressure

1980 ◽  
Vol 239 (1) ◽  
pp. R161-R167 ◽  
Author(s):  
E. Casillas ◽  
L. S. Smith ◽  
J. J. Woodward ◽  
B. G. D'Aoust
Keyword(s):  
Hydrostatic Pressure ◽  
Plasma Proteins ◽  
Fibrinolytic Activity ◽  
Coagulation System ◽  
Related Phenomenon ◽  
Protein Levels ◽  
Diffuse Intravascular Coagulation ◽  
Rapid Decompression ◽  
Increased Pressure ◽  
Increased Susceptibility

Hematologic changes were studied in fingering salmon after rapid decompression from combined or independent exposure to gas and hydrostatic pressure. After decompression, fingerling salmon saturated with excess gas under pressure (10.1-40.6 m of seawater) suffered a decrease in thrombocyte counts and fibrinogen, prolonged prothrombin (PT) times, and increased fibrinolytic activity, plasma proteins, and erythrocyte counts in proportion to severity of the dive. After decompression, fingerling salmon exposed to increased pressure experienced an increase in thrombocyte counts and available fibrinogen, shortened PT times, increased erythrocyte counts, and decreased plasma protein levels. It appeared that pressure causes activation of the blood coagulation system of fish. This activation may predispose the fish to increased susceptibility to bubble-induced diffuse intravascular coagulation after rapid decompression. Furthermore, hemoconcentration after decompression may be a pressure-related phenomenon and not a response to bubble-induced anoxia.

Using Rheology to Probe the Mechanism of Joint Lubrication: Polyelectrolyte/protein interactions in Synovial Fluid

2001 ◽  
Vol 711 ◽  
Author(s):  
Katherine M. N. Oates ◽  
Wendy E. Krause ◽  
Ralph H. Colby
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Protein Interactions ◽  
Plasma Proteins ◽  
Fluid Model ◽  
Structural Features ◽  
Protein Solutions ◽  
Shear Rates ◽  
Strong Shear ◽  
Γ Globulins

ABSTRACTThe outstanding lubricating properties of synovial fluid, found in freely moving mammalian joints, may be due to intermolecular associations between hyaluronic acid, an anionic polysaccharide, and the plasma proteins. A synovial fluid model comprised of hyaluronic acid and the plasma proteins albumin and γ-globulins, was constructed. Rheological measurements reveal a pronounced viscoelasticity with a strong shear history dependence for the synovial fluid model and the plasma protein solutions at low shear rates. The addition of the anti-inflammatory drug D-Penicillamine to the solution alters the rheology of the synovial fluid model. We present two ideas about the structural features of synovial fluid that may explain this viscoelasticity and suggest further experimental techniques that can be used to test these ideas.

scholarly journals Nanoparticle-protein interactions: from crucial plasma proteins to key enzymes

2011 ◽  
Vol 304 ◽  
pp. 012039 ◽  
Author(s):  
Elodie Sanfins ◽  
Julien Dairou ◽  
Fernando Rodrigues-Lima ◽  
Jean-Marie Dupret
Keyword(s):  
Protein Interactions ◽  
Plasma Proteins ◽  
Key Enzymes

scholarly journals High Plasma Phospholipid Transfer Protein Levels as a Risk Factor for Coronary Artery Disease

2003 ◽  
Vol 23 (10) ◽  
pp. 1857-1862 ◽  
Author(s):  
Axel Schlitt ◽  
Christoph Bickel ◽  
Prathima Thumma ◽  
Stefan Blankenberg ◽  
Hans J. Rupprecht ◽  
...  
Keyword(s):  
Coronary Artery Disease ◽  
Risk Factor ◽  
Coronary Artery ◽  
Plasma Phospholipid ◽  
High Plasma ◽  
Phospholipid Transfer Protein ◽  
Protein Levels ◽  
Transfer Protein ◽  
Phospholipid Transfer ◽  
Artery Disease

The Regulation of Natural Food Dyes Curcumin on the Amyloidogenic Pathway of APP

2013 ◽  
Vol 781-784 ◽  
pp. 1160-1163
Author(s):  
Xiong Zhang ◽  
Jie Yun Sun ◽  
Hong Mei Zhang ◽  
Lu Si ◽  
Yu Li
Keyword(s):  
Time Course ◽  
Mrna Level ◽  
Time Dependent ◽  
Hek293 Cells ◽  
Natural Food ◽  
Inhibition Effect ◽  
Dose Time ◽  
Protein Levels ◽  
Food Dyes

As a promising prevention and therapeutic intervention in Alzheimer’s disease, natural food dyes curcumin could obviously inhibit the generation of Aβ, but the mechanism is not fully defined. This study aims to investigate the effects of curcumin on the amyloidogenic pathway of APP in vitro. Plasmids APPswe and BACE1-mychis were transiently co-transfected into SH-SY5Y and HEK293 cells. Then, they were treated with curcumin at 0, 1.25, 5, 20 μmol/L for 24 h, or with curcumin at 5μmol/L for 0, 12, 24 and 48 h for the time course assay. Our findings showed that curcumin could inhibit the expression of the APP at mRNA level; the expression of the BACE1 and C99 at mRNA and protein levels, furthermore it could inhibit the generation of Aβ40/42, and those changes were dose-time dependent (p<0.05). Our study indicates that Aβ40/42 generation inhibition effect of curcumin might due to its influence on amyloidogenic pathway. This may provide important experimental basis for AD treatment with curcumin.

Plasma proteome changes in subjects with Type 2 diabetes mellitus with a low or high early insulin response

2008 ◽  
Vol 114 (7) ◽  
pp. 499-507 ◽  
Author(s):  
Tea Sundsten ◽  
Björn Zethelius ◽  
Christian Berne ◽  
Peter Bergsten
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Insulin Response ◽  
Β Cell ◽  
Protein Levels ◽  
Early Insulin Response

Circulating proteins contribute to the pathogenesis of T2DM (Type 2 diabetes mellitus) in various ways. The aim of the present study was to investigate variations in plasma protein levels in subjects with T2DM and differences in β-cell function, characterized by the EIR (early insulin response), and to compare these protein levels with those observed in individuals with NGT (normal glucose tolerance). Ten subjects with NGT+high EIR, ten with T2DM+high EIR, and ten with T2DM+low EIR were selected from the community-based ULSAM (Uppsala Longitudinal Study of Adult Men) cohort. Plasma protein profiling was performed using SELDI-TOF (surface-enhanced laser-desorption ionization–time-of-flight) MS. In total, nine plasma proteins differed between the three study groups (P<0.05, as determined by ANOVA). The levels of two forms of transthyretin, haemoglobin α-chain and haemoglobin β-chain were decreased in plasma from subjects with T2DM compared with subjects with NGT, irrespective of the EIR of the subjects. Apolipoprotein H was decreased in plasma from individuals with T2DM+high EIR compared with subjects with NGT. Four additional unidentified plasma proteins also varied in different ways between the experimental groups. In conclusion, the proteins detected in the present study may be related to the development of β-cell dysfunction.

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