Neurokinin receptor mediated plasma extravasation in guinea pig and rat airways: comparison of 125I-labelled human fibrinogen and 99mTc-labelIed human serum albumin as markers of leakage

1993 ◽  
Vol 71 (7) ◽  
pp. 506-511 ◽  
Author(s):  
Christine Tousignant ◽  
Chi-Chung Chan ◽  
Donna Young ◽  
Diane Guevremont ◽  
Ian W. Rodger
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum ◽  
Plasma Extravasation ◽  
Human Fibrinogen ◽  
Protein Extravasation ◽  
Neurokinin Receptor ◽  
Lower Airways ◽  
Dose Dependent

In the present study we have characterized NK-1 and NK-2 receptor induced microvascular leakage in guinea pig and rat airways, using 125I-labelled human fibrinogen ([125I]FN) versus 99mTc-labelled human serum albumin ([99mTc]HSA) as markers for plasma protein extravasation. Intravenous administration of the selective NK-1 agonist [Sar9, Met(O2)11]SP (1 nmol kg−1) caused a dose-dependent increase of [125I]FN extravasation in guinea pig trachea, main bronchi, secondary bronchi, and intraparenchymal airways. Extravasation of [125I]FN increased by up to 192 (trachea), 284 (main bronchi), 368 (secondary bronchi), and 271% (intraparenchymal bronchi) over control levels in these regions of the airways. Pretreatment of the animals with CP 99,994 and RP 67,580, two NK-1 nonpeptide antagonists, caused a dose-dependent inhibition of [Sar9, Met(O2)11]SP-induced leakage of [125I]FN. [Sar9, Met(O2)11]SP (1 nmol kg−1) did not induce specific leakage of [99mTc]HSA in the intraparenchymal bronchi. Specific NK-2 receptor induced leakage was detected in the lower airways but only when using [125I]FN as a marker. We have also compared the ability of CP 99,994 and RP 67,580 to inhibit [Sar9, Met(O2)11]SP induced extravasation of [125I]FN in rat airways. CP 99,994 was 40–50 (tracheobronchial region) to 75 (lower airways) times more potent in the guinea pig than the rat airways. In contrast, RP 67,580 had higher affinity for rat airways compared with guinea pig airways. The results of this study highlight the superiority of [125I]FN as a sensitive marker of plasma extravasation over [99mTc]HSA. Furthermore, the results strongly suggest that both NK-1 and NK-2 receptors mediate plasma extravasation in the guinea pig lower airways and that NK-1 receptors are different in guinea pig and rat airways.Key words: Leakage, tachykinins, NK-1 and NK-2 receptors, airway, asthma.

scholarly journals EVIDENCE FOR SPECIES' DIFFERENCES IN THE EFFECT OF SERUM γ-GLOBULIN CONCENTRATION ON γ-GLOBULIN CATABOLISM

1964 ◽  
Vol 120 (5) ◽  
pp. 967-986 ◽  
Author(s):  
Stewart Sell
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum ◽  
Guinea Pigs ◽  
Serum Proteins ◽  
Elevated Serum ◽  
Keyhole Limpet Hemocyanin ◽  
Normal Numbers ◽  
Γ Globulins

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig γ-globulins and human serum albumin were determined in mice and in guinea pigs whose serum γ-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum γ-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled γ-globulins from all species tested were markedly increased in mice with elevated γ-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit γ-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine γ-globulin were only partially effective, and injections of human serum albumin had no effect. The γ-globulin catabolic rates were decreased in mice with subnormal serum γ-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum γ-globulin levels. In contrast, elevation of the serum γ-globulin levels by injections of exogenous γ-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled γ-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum γ-globulin concentration appears to be operative in the mouse, but not in the guinea pig. Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum γ-globulin levels.

Further Studies on Guinea Pig and Rabbit Cytophilic Antibodies Directed Against Human Serum Albumin

1972 ◽  
Vol 42 (3) ◽  
pp. 399-429 ◽  
Author(s):  
P.C. Maginn ◽  
L. Sparr ◽  
K. Daniel ◽  
A.A. Blazkovec
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum

Presence of Soluble CD26 Peptidase Activity in Human Serum Albumin (FlexBumin): Implications for Cell Freezing and Thawing Protocols during Transplantation

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 3475-3475
Author(s):  
Laura A. Paganessi ◽  
Andrew L. Walker ◽  
Kent W. Christopherson
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Clinical Setting ◽  
Bovine Serum ◽  
Hematopoietic Cells ◽  
Peptidase Activity ◽  
Freezing And Thawing ◽  
Research Setting ◽  
Dose Dependent

Abstract Hematopoietic cells are commonly exposed to human serum albumin (HSA) in the clinical setting and fetal bovine serum (FBS) in the research setting. Serum is utilized as a standard reagent across multiple research disciplines for tissue culture (10–20% FBS). HSA is a common reagent in the clinical setting and is routinely added to hematopoietic cells (0.5–4% HSA) in preparation for cryopreservation. Many labs also wash cryopreserved hematopoietic stem cells with HSA (1–5%) prior to autologous or allogenic transplantation to rid the cells of the DMSO used during cryopreservation. Lastly, HSA is sometimes infused directly into patients in the clinic for such indications as the short-term treatment of nephrotic syndrome. We have generated data suggesting that the peptidase CD26 (dipeptidylpeptidase IV/DPPIV) regulates HSC/HPC function, release of HPC out of the bone marrow (BM) during G-CSF induced mobilization, and engraftment of HSC/HPC into the BM during transplantation. It is within this context that we evaluated the presence of CD26/DPPIV activity in HSA. HSA of 20%, 10%, 2.5%, and 1% were prepared by diluting Flexbumin 25% (Baxter Healthcare) with 0.9% NaCl. FBS (Hyclone) concentrations were prepared likewise. Bovine Serum Albumin Fraction V (BSA) concentrations were prepared weight by volume. CD26/DPPIV activity was assayed utilizing the Gly-Pro-p-nitroanilide substrate in a 96-well format. Standard p-nitroanilide (pNA) curves were created by serially diluting pNA with 5mM Tris-HCl pH 7.5. 4mM Gly-Pro-pNA substrate was then combined with each test solution in 5mM Tris-HCl. Absorbance readings (A405) were then taken at 37° C every 5 minutes for 60 minutes. CD26 inhibition was achieved by treating with Diprotin-A (Ile-Pro-Ile). Prior to measurement of CD26 activity, HSA, BSA, or FBS were combined with Diprotin-A incubated at 37° C for 15 minutes. Final Diprotin-A concentrations during treatment were 5000μM, 500μM, 50μM, 5μM, 0.5μM, 0.05μM, 0.005μM, and 0 μM. Evaluation of CD26 activity in 1%, 2.5%, 10%, and 20% HSA solutions revealed a statistically significant and dose dependent level of CD26 activity within the serum (p<0.05). CD26 activity of 10% HSA was quantitated at 49.62±1.5 pmoles/min and activity of 10% FBS was quantitated at 53.42±1.44 pmoles/min. Evaluation of CD26 activity in 2.5%, 10%, or 20% FBS also showed a quantifiable and dose dependent CD26 activity (p< 0.05). 1%, 2.5%, 10%, and 20% BSA Fraction V had no detectable levels of CD26 activity as compared to saline alone. Furthermore, treatment with the CD26 inhibitor, Diprotin A, actively inhibits CD26 activity ex vivo in a dose dependent manner (p< 0.05). These results suggest that significant levels of CD26 activity are present in HSA (Flexbumin) that is utilized routinely for clinical purposes. Additional evaluations are indicated to test whether this is an industry wide phenomenon across multiple preparation procedures and manufactures. Additionally, these results suggest that the CD26 activity that is present is specific and can be inhibited utilizing CD26 inhibitors. No clinical protocol methodology currently exists for the treatment of HSA in the clinical or research setting. Lastly, these results suggest that the use of HSA that may contain CD26 activity during clinical freezing and thawing procedures of transplant units should be reconsidered, especially if the HSA remains with the unit during infusion. Future studies will be needed to evaluate if the results these pre-clinical experiments necessitate changes to clinical methodologies.

THE EFFECT OF FREE FATTY ACIDS ON RESIN UPTAKE OF TRI-IODOTHYRONINE FROM HUMAN, RAT, RABBIT AND GUINEA-PIG SERUM AND HUMAN SERUM ALBUMIN

1969 ◽  
Vol 45 (4) ◽  
pp. 489-493 ◽  
Author(s):  
P. W. NATHANIELSZ
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Free Fatty Acids ◽  
Human Serum ◽  
Rat Serum ◽  
Pig Serum

SUMMARY Recently changes in plasma free fatty acids have been suggested as a possible regulator of the levels of free thyroxine in the plasma. Oleic acid has been shown to displace tri-iodothyronine from human serum, human serum albumin, rat serum, rabbit serum and guinea-pig serum. The extent of the displacement, much greater from human serum albumin than from whole serum, suggests that free fatty acid does not affect the globulin binding site. It would also appear that, in the rat, all the binding sites are sensitive to free fatty acids and hence there is probably only albumin binding in this species. The results with rabbit and guinea-pig serum were intermediate to those with human and rat serum. A significant rise in resin uptake of tri-iodothyronine in vitro occurred with an increase of free fatty acid level of 0·5 m-equiv./l., well within the physiological range.

Further Studies on Guinea Pig and Rabbit Cytophilic Antibodies Directed Against Human Serum Albumin

1972 ◽  
Vol 42 (3) ◽  
pp. 382-398
Author(s):  
P.C. Maginn ◽  
K. Daniel ◽  
L. Sparr ◽  
A.A. Blazkovec
Keyword(s):  
Human Serum Albumin ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Human Serum

scholarly journals Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction

2014 ◽  
Vol 122 ◽  
pp. 341-349 ◽  
Author(s):  
Sina Movaghati ◽  
Ali Akbar Moosavi-Movahedi ◽  
Fariba Khodagholi ◽  
Hadi Digaleh ◽  
Ehsan Kachooei ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Pc12 Cells ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Dependent Manner ◽  
Dose Dependent

scholarly journals Interaction of Carbon Dots from Grilled Spanish Mackerel with Human Serum Albumin, γ-Globulin and Fibrinogen

Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2336
Author(s):  
Guoxin Cui ◽  
Yukun Song ◽  
Kangjing Liu ◽  
Mingqian Tan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carbon Dots ◽  
Plasma Proteins ◽  
Biological Effects ◽  
Human Fibrinogen ◽  
Saturation State ◽  
Spanish Mackerel ◽  
Daily Diet

The potential biological effects of food-borne carbon dots (FCDs) generated during food heating procedures on human health has received great attention. The FCDs will be inevitably exposed to blood proteins along with our daily diet to produce unknown biological effects. In this study, the interaction between FCDs extracted from grilled Spanish mackerel and three main types of human plasma proteins including human serum albumin (HSA), human γ-globulin (HGG) and human fibrinogen (HF) was reported. It was found that the grilled Spanish mackerel FCDs could affect the morphology, size and surface electrical properties of the three proteins. The interaction between the FCDs and proteins had different effects on the secondary structure of the three proteins through a static mechanism. The tested HSA, HGG, and HF could adsorb FCDs to reach saturation state within 0.5 min after the adsorption happened. The binding affinity of the FCDs to the plasma proteins was sorted as follows: HF > HGG > HSA. The results of FCDs interacted with plasma proteins provided useful information in the assessment of the safety of FCDs in our daily diet.

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