scholarly journals Sphingosine 1-Phosphate Distribution in Human Plasma: Associations with Lipid Profiles

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Samar M. Hammad ◽  
Mohammed M. Al Gadban ◽  
Andrea J. Semler ◽  
Richard L. Klein
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Hdl Cholesterol ◽  
Physiological Significance ◽  
Plasma Lipoproteins ◽  
Total Plasma ◽  
Individual Subject ◽  
Sphingosine 1 Phosphate ◽  
Health And Disease ◽  
The Individual

The physiological significance of sphingosine 1-phosphate (S1P) transport in blood has been debated. We have recently reported a comprehensive sphingolipid profile in human plasma and lipoprotein particles (VLDL, LDL, and HDL) using HPLC-MS/MS (Hammad et al., 2010). We now determined the relative concentrations of sphingolipids including S1P in the plasma subfraction containing lipoproteins compared to those in the remaining plasma proteins. Sphingomyelin and ceramide were predominantly recovered in the lipoprotein-containing fraction. Total plasma S1P concentration was positively correlated with S1P concentration in the protein-containing fraction, but not with S1P concentration in the lipoprotein-containing fraction. The percentage of S1P transported in plasma lipoproteins was positively correlated with HDL cholesterol (HDL-C) concentration; however, S1P transport in lipoproteins was not limited by the concentration of HDL-C in the individual subject. Thus, different plasma pools of S1P may have different contributions to S1P signaling in health and disease.

Differential Human Plasma Proteomics Based on AniBal Quantification and Peptide-level Off-Gel Isoelectric Focussing

2010 ◽  
Vol 3 ◽  
pp. PRI.S4851 ◽  
Author(s):  
Laure F. Marvin-Guy ◽  
Tatiana Zinger ◽  
Sandrine Wagnière ◽  
Véronique Parisod ◽  
Michael Affolter ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Ion Trap ◽  
Quantitative Information ◽  
Proteome Coverage ◽  
Disease Biomarkers ◽  
Proteomics Approach ◽  
Peptide Level ◽  
Health And Disease ◽  
Human Plasma Proteome

Despite its enormous complexity, human plasma is still one of the most frequently used body fluids for identification and quantification of health and disease biomarkers. We have developed a new workflow for qualitative and quantitative analysis of human plasma proteins. The first step was to remove the seven most abundant plasma proteins (MARS). Moreover, in order to reduce the complexity of the sample and to increase protein and proteome coverage, Off-Gel fractionation was performed at peptide level. Our own stable isotope-based quantitative proteomics approach termed AniBAL was chosen for relative quantification of proteins between conditions. The method was developed with commercial human plasma and resulted in the identification of 85 proteins, of which 68 revealed quantitative information (Mascot database search combined with Peptide-/ProteinProphet validation). The combined methods consisting of MARS, AniBAL, Off-Gel and nano-LC-MS/MS on a Bruker HCT ion trap represent a new and efficient platform to quantify human plasma proteome differences between conditions. The method was also found technically compatible to a pair of human plasma pilot samples from the European FP6 project “DiOGenes”. Many of the identifiable/quantifiable proteins are relevant to obesity, diabetes and inflammation, which form the context of investigation within “DiOGenes”.

COMPETITIVE BINDING OF FREE AND CONJUGATED OESTROGENS TO PLASMA PROTEINS

1969 ◽  
Vol 44 (2) ◽  
pp. 219-230 ◽  
Author(s):  
ELEONORA P. GIORGI ◽  
P. G. CROSIGNANI
Keyword(s):  
Human Plasma ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Equilibrium Dialysis ◽  
Competitive Binding ◽  
Physiological Significance ◽  
Ovarian Vein ◽  
Oestrone Sulphate ◽  
Graafian Follicle ◽  
Number Of Binding Sites

SUMMARY Human plasma was dialysed against increasing concentrations of [4-14C]oestradiol-17β, [4-14C]oestrone, Na[6,7-3H]oestradiol-17β-glucuronide and Na[6,7-3H]oestrone sulphate. When the oestrogens were dialysed separately, binding to a protein with a limited number of binding sites (probably a globulin) could be shown. At comparable concentrations oestrone sulphate was bound to a greater extent than the free compounds and the glucuronide. When free and conjugated oestrogens were dialysed together a displacement of the conjugates from globulin to albumin was demonstrated. This observation was confirmed by the results of the equilibrium dialysis of plasma of ovarian vein blood obtained from a mare and a donkey after injection of [4-14C]oestradiol-17β and Na[6,7-3H]oestradiol-177β-glucuronide into a Graafian follicle of the homolateral ovary. The possible physiological significance of this competition between free and conjugated oestrogens is discussed.

Differential precipitation of isolated human plasma lipoproteins with heparin and manganese chloride.

1988 ◽  
Vol 34 (2) ◽  
pp. 240-243 ◽  
Author(s):  
J M Ruiz-Albusac ◽  
E Velázquez ◽  
A Montes
Keyword(s):  
Human Plasma ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Hdl Cholesterol ◽  
Plasma Lipoproteins ◽  
Low Density ◽  
Serum Lipoproteins ◽  
Supernatant Liquid ◽  
Differential Precipitation ◽  
Preparative Ultracentrifugation

Abstract We studied the precipitation of isolated lipoproteins with heparin and MnCl2. Lipoproteins were isolated from human plasma by preparative ultracentrifugation and their free cholesterol was labeled. Each lipoprotein fraction was then precipitated at various pHs, with or without bovine serum albumin (60 g/L) present. Under no set of conditions was one class of lipoproteins completely separated from the other two. Specifically, under standard conditions for precipitation of serum lipoproteins (pH 7.4 and protein 60 g/L), 12% of the very-low-density lipoprotein (VLDL) and 8% of the low-density lipoprotein (LDL) remained in the supernatant liquid, and 30% of the high-density lipoprotein (HDL) was precipitated. These results indicate that, under these conditions, so-called HDL cholesterol may be a mixture of VLDL, LDL, and HDL, although the sum of the amount of these three fractions remaining in the supernate is fortuitously very close to the value for HDL cholesterol isolated by ultracentrifugation.

scholarly journals Changes in lipoprotein lipase activity and plasma liver lipids in thiram intoxicated rats.

1993 ◽  
Vol 40 (4) ◽  
pp. 563-567 ◽  
Author(s):  
B Sadurska ◽  
B Boguszewski
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Plasma Cholesterol ◽  
Density Lipoprotein ◽  
Hdl Cholesterol ◽  
Plasma Lipoproteins ◽  
Total Plasma Cholesterol ◽  
Total Plasma ◽  
Lipoprotein Lipase Activity ◽  
Liver Lipids

Acute thiram (tetramethyl-bis-thiocarbamyl disulphide) poisoning of rat (a single dose of 50% LD50) caused decreased lipoprotein lipase (LPL) activity in adipose tissue, the greatest inhibition being observed at 72 h after administration of the pesticide. Simultaneously, the levels of total plasma cholesterol, triacylglycerols and the high density lipoprotein (HDL) cholesterol were increased. On repeated pesticide administration (5% LD50) decreased LPL activity was observed after 14 and 30 days of poisoning, whereas after 90 days the LPL activity was distinctly increased. The levels of total cholesterol (in all periods of poisoning) and HDL cholesterol (only after 30 days of poisoning) became increased. These changes were accompanied by decreased content of free fatty acids and increase of hepatic triacylglycerols. The changes observed in the lipoprotein lipase activity of thiram-poisoned rats correspond to the profiles of plasma lipoproteins typical of thyroid hypofunction.

Fast lipoprotein chromatography: new method of analysis for plasma lipoproteins

1993 ◽  
Vol 39 (11) ◽  
pp. 2276-2281 ◽  
Author(s):  
W März ◽  
R Siekmeier ◽  
H Scharnagl ◽  
U B Seiffert ◽  
W Gross
Keyword(s):  
Plasma Proteins ◽  
Ldl Cholesterol ◽  
Gel Filtration ◽  
Hdl Cholesterol ◽  
Plasma Lipoproteins ◽  
Precipitation Method ◽  
High Density Lipoproteins ◽  
Vldl Cholesterol ◽  
Novel Method ◽  
Fast Flow

Abstract Fast lipoprotein chromatography (FLPC) is a novel method for quantifying lipoproteins. Plasma proteins are separated by fast-flow gel filtration. Lipoproteins are detected by post-column derivatization with an enzymatic cholesterol reagent. FLPC resolves very-low-, low-, and high-density lipoproteins (VLDL, LDL, and HDL, respectively) and completely separates apolipoprotein Al- and apolipoprotein B-containing lipoproteins. CVs for VLDL-cholesterol, LDL-cholesterol, and HDL-cholesterol are 5.8%, 2.0%, and 1.9%, respectively. We compared FLPC with a combined ultracentrifugation and precipitation method and obtained correlation of r = 0.979, 0.978, and 0.933 for VLDL-cholesterol, LDL-cholesterol, and HDL-cholesterol, respectively. Triglyceride concentrations up to 9.00 g/L did not interfere with the quantification of lipoproteins by FLPC. We conclude that FLPC is a precise and reliable method for the analysis of plasma lipoproteins that complements conventional techniques.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Studies on the Thromboplastic Effect of Human Plasma Lipoproteins

1976 ◽  
Vol 35 (01) ◽  
pp. 178-185 ◽  
Author(s):  
Helena Sandberg ◽  
Lars-Olov Andersson
Keyword(s):  
High Density Lipoprotein ◽  
Human Plasma ◽  
Platelet Rich Plasma ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Plasma Lipoproteins ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Free Plasma ◽  
Good Agreement

SummaryHuman plasma lipoprotein fractions were prepared by flotation in the ultracentrifuge. Addition of these fractions to platelet-rich, platelet-poor and platelet-free plasma affected the partial thromboplastin and Stypven clotting times to various degrees. Addition of high density lipoprotein (HDL) to platelet-poor and platelet-free plasma shortened both the partial thromboplastin and the Stypven time, whereas addition of low density lipoprotein and very low density lipoprotein (LDL + VLDL) fractions only shortened the Stypven time. The additions had little or no effect in platelet-rich plasma.Experiments involving the addition of anti-HDL antibodies to plasmas with different platelet contents and measuring of clotting times produced results that were in good agreement with those noted when lipoprotein was added. The relation between structure and the clot-promoting activity of various phospholipid components is discussed.

An Evaluation of a Plasma Fractionation System

1960 ◽  
Vol 4 (01) ◽  
pp. 031-044
Author(s):  
George Y. Shinowara ◽  
E. Mary Ruth
Keyword(s):  
Biological Activity ◽  
Ionic Strength ◽  
Plasma Proteins ◽  
High Concentration ◽  
Significant Evidence ◽  
Native Proteins ◽  
Mobility Data ◽  
Fractionation Procedure ◽  
The Individual ◽  
Low Ionic Strength

SummaryFour primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S20, w and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S20, w classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

Observations on the in vitro Effects of Chylomicra, Low-Density Lipoproteins and Phospholipids on Human Plasma Euglobulin Lysis

1963 ◽  
Vol 09 (01) ◽  
pp. 164-174 ◽  
Author(s):  
Albert R Pappenhagen ◽  
J. L Koppel ◽  
John H Olwin
Keyword(s):  
Human Plasma ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Inositol ◽  
Plasma Lipoproteins ◽  
Low Density ◽  
Inhibitory Effects ◽  
Soybean Phospholipids ◽  
In Vitro Effects ◽  
Complete Precipitation

SummaryData have been presented on the in vitro effects of human chylomicra, low-density human plasma lipoproteins, and partially purified preparations of various phospholipids on human plasma euglobulin lysis. Euglobulin lysis was found to be accelerated by preparations of mixed soybean phospholipids (aso-lectin), cephalin, phosphatidyl inositol, phophatidyl serine and phosphatidyl ethanolamine. In contrast, it was found to be inhibited by preparations of human chylomicra, low-density human plasma liproproteins and lecithin. Inhibition of euglobulin lysis produced by any of these three agents could be diminished or completely overcome by the simultaneous presence of suitable levels of any one of the accelerating agents. In all cases studied, both inhibitory and accelerating effects were observed to be concentration-dependent. Evidence has been obtained to suggest that in the case of the accelerating agents the observed increased rate of euglobulin lysis is not a direct effect on lysis itself, but rather is due to more complete precipitation of plasminogen in the presence of these substances. On the other hand, it appears that the inhibitory effects observed are not related to the extent of plasminogen precipitation, but are actually true inhibitions of euglobulin lysis. The possible clinical significance of some of these observations has been briefly discussed.

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