scholarly journals Serum albumin enhances the uptake of [3H]cholesterol from phosphatidylcholine vesicles by cultured human fibroblasts

1984 ◽  
Vol 220 (2) ◽  
pp. 605-608 ◽  
Author(s):  
J P Slotte ◽  
S Björkerud
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Human Lung ◽  
Exchange Process ◽  
Human Fibroblasts ◽  
Lung Fibroblasts ◽  
Molar Ratio ◽  
Human Lung Fibroblasts ◽  
Cultured Human Fibroblasts

Cultured human lung fibroblasts, incubated with cholesterol/phosphatidylcholine vesicles (cholesterol: phosphatidylcholine molar ratio 1:1) incorporated vesicle [3H]-cholesterol linearly for at least 48 h by an exchange process without gaining sterol mass. The incorporation of [3H]cholesterol by the cells was markedly enhanced in the presence of purified bovine serum albumin. A fraction of the incorporated vesicle [3H]cholesterol was esterified by the cells.

Antibodies to Indolealkylamines; Serotonin and Melatonin

1974 ◽  
Vol 52 (3) ◽  
pp. 196-202 ◽  
Author(s):  
Lee J. Grota ◽  
Gregory M. Brown
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molar Ratio ◽  
Double Immunodiffusion ◽  
Protein Conjugates ◽  
Spectrophotometric Data ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant

Serotonin, N-acetyl serotonin, and 5-methoxy-N-acetyl serotonin (melatonin) were conjugated to bovine serum albumin (BSA) using formaldehyde. The molar ratio of hapten to protein was determined spectrophotometrically. Spectrophotometric data indicated that serotonin and N-acetyl serotonin but not melatonin were conjugated to bovine serum albumin. Selected hapten–protein conjugates were suspended in Freund's adjuvant and injected into rabbits. Antisera were harvested monthly and screened by double immunodiffusion. Immunodiffusion and inhibition tests indicated that antibodies raised to serotonin–BSA reacted with serotonin and 5-methoxytryptamine but failed to cross react with N-acetyl serotonin or melatonin. Inhibition tests indicated that antibodies to N-acetyl serotonin – BSA reacted with N-acetyl serotonin and cross reacted with melatonin but not with serotonin or 5-methoxytryptamine.

scholarly journals Platelet-activating factor exerts mitogenic activity and stimulates expression of interleukin 6 and interleukin 8 in human lung fibroblasts via binding to its functional receptor.

1996 ◽  
Vol 184 (1) ◽  
pp. 191-201 ◽  
Author(s):  
M Roth ◽  
M Nauck ◽  
S Yousefi ◽  
M Tamm ◽  
K Blaser ◽  
...  
Keyword(s):  
Pertussis Toxin ◽  
Tyrosine Kinases ◽  
Human Lung ◽  
Human Fibroblasts ◽  
Platelet Activating Factor ◽  
Lung Fibroblasts ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Human Lung Fibroblasts ◽  
Paf Receptor

Platelet-activating factor (PAF) is a potent proinflammatory phospholipid mediator of the lung. In this study, we demonstrate that PAF receptor mRNA and protein is expressed by human lung fibroblasts. Interaction of PAF with its specific receptor resulted in increases of tyrosine phosphorylation of several intracellular proteins, indicating that the PAF-receptor might be functionally active. PAF-induced transcription of protooncogenes c-fos and c-jun as well as of interleukin (IL)-6 and IL-8 genes in human fibroblasts. Transcription of the interleukins was followed by secretion of the respective proteins. Moreover, PAF enhanced proliferation of fibroblasts in a concentration-dependent manner. Using signaling inhibitors, we demonstrate that PAF-induced transcription of the c-fos, IL-6, and IL-8 genes, as well as proliferation, require activation of pertussis toxin-sensitive G proteins, tyrosine kinases, and protein kinase C (PKC). In contrast, transcription of c-jun was blocked by pertussis toxin, but not by inhibitors for tyrosine kinases or PKC. These data suggest that PAF stimulates distinct signaling pathways in human lung fibroblasts. In addition, the activation of human fibroblasts by PAF leads to enhanced proliferation and to the expression of proinflammatory cytokines, which may contribute to the pathophysiological changes in pulmonary inflammation.

scholarly journals Conductance Changes in Bovine Serum Albumin Caused by Drug-Binding Triggered Structural Transitions

Materials ◽  
2019 ◽  
Vol 12 (7) ◽  
pp. 1022 ◽  
Author(s):  
Jing Yu ◽  
Yun Chen ◽  
Liqun Xiong ◽  
Xiaoyue Zhang ◽  
Yue Zheng
Keyword(s):  
Secondary Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cd Spectroscopy ◽  
Drug Binding ◽  
Molar Ratio ◽  
Conductive Atomic Force Microscopy ◽  
Protein Secondary Structures ◽  
Drug Concentrations

Proteins, due to their binding selectivity, are promising candidates for fabricating nanoscale bio-sensors. However, the influence of structural change on protein conductance caused by specific protein-ligand interactions and disease-induced degeneration still remains unknown. Here, we excavated the relationship between circular dichroism (CD) spectroscopy and conductive atomic force microscopy (CAFM) to reveal the effect of the protein secondary structures changes on conductance. The secondary structure of bovine serum albumin (BSA) was altered by the binding of drugs, like amoxicillin (Amox), cephalexin (Cefa), and azithromycin (Azit). The CD spectroscopy shows that the α-helical and β-sheet content of BSA, which varied according to the molar ratio between the drug and BSA, changed by up to 6%. The conductance of BSA monolayers in varying drug concentrations was further characterized via CAFM. We found that BSA conductance has a monotonic relation with α-helical content. Moreover, BSA conductance seems to be in connection with the binding ability of drugs and proteins. This work elucidates that protein conductance variations caused by secondary structure transitions are triggered by drug-binding and indicate that electrical methods are of potential application in protein secondary structure analysis.

scholarly journals Membrane-associated chondroitin sulfate proteoglycans of human lung fibroblasts.

1989 ◽  
Vol 108 (3) ◽  
pp. 1165-1173 ◽  
Author(s):  
G David ◽  
V Lories ◽  
A Heremans ◽  
B Van der Schueren ◽  
J J Cassiman ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Human Lung ◽  
Core Protein ◽  
Human Fibroblasts ◽  
Chondroitin Sulfate Proteoglycans ◽  
Lung Fibroblasts ◽  
Hydrophobic Membrane ◽  
Human Lung Fibroblasts ◽  
Core Proteins

Cultured human fetal lung fibroblasts produce some chondroitin sulfate proteoglycans that are extracted as an aggregate in chaotropic buffers containing 4 M guanidinium chloride. The aggregated proteoglycans are excluded from Sepharose CL4B and 2B, but become included, eluting with a Kav value of 0.53 from Sepharose CL4B, when Triton X-100 is included in the buffer. Conversely, some of the detergent-extractable chondroitin sulfate proteoglycans can be incorporated into liposomes, suggesting the existence of a hydrophobic membrane-intercalated chondroitin sulfate proteoglycan fraction. Purified preparations of hydrophobic chondroitin sulfate proteoglycans contain two major core protein forms of 90 and 52 kD. A monoclonal antibody (F58-7D8) obtained from the fusion of myeloma cells with spleen cells of BALB/c mice that were immunized with hydrophobic proteoglycans recognized the 90- but not the 52-kD core protein. The epitope that is recognized by the antibody is exposed at the surface of cultured human lung fibroblasts and at the surface of several stromal cells in vivo, but also at the surface of Kupffer cells and of epidermal cells. The core proteins of these small membrane-associated chondroitin sulfate proteoglycans are probably distinct from those previously identified in human fibroblasts by biochemical, immunological, and molecular biological approaches.

scholarly journals Kinetics of Vibrio cholerae sialidase action on gangliosidic substrates at different supramolecular-organizational levels

1982 ◽  
Vol 203 (3) ◽  
pp. 735-742 ◽  
Author(s):  
Bruno Venerando ◽  
Benvenuto Cestaro ◽  
Amelia Fiorilli ◽  
Riccardo Ghidoni ◽  
Augusto Preti ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Vibrio Cholerae ◽  
Bovine Serum ◽  
Mixed Micelles ◽  
Molar Ratio ◽  
Free Carbohydrates ◽  
Triton X ◽  
Kinetics Of ◽  
Vibrio Cholerae Sialidase

Gd1a, Gd1b and Gt1b gangliosides were dispersed in the following membrane-mimicking systems: (a) homogeneous micelles; (b) mixed micelles with Gm1 ganglioside (which is resistant to the enzyme action), Triton X-100 or bovine serum albumin; (c) small unilamellar vesicles of egg phosphatidylcholine. The effect of dispersion on sialic acid release by Vibrio cholerae sialidase was studied. As reference substrates freely interacting with the enzyme the lipid-free carbohydrates of Gd1a and 3′-sialosyl-lactose were employed. The apparent Vmax. of the enzyme was, with all the gangliosides, dependent on the type of ganglioside dispersion. It was lowest for homogeneous micelles and mixed micelles with ganglioside Gm1, and increased about 6-fold for ganglioside/bovine serum albumin lipoprotein micelles, 15-fold for mixed-ganglioside/Triton X-100 micelles (optimal molar ratio 1:7.5) and 30-fold for phosphatidylcholine vesicles containing 2.5 mol% ganglioside (this proportion was optimal for enzyme activity on the vesicles). For ganglioside Gd1a, the activity on Triton X-100 mixed micelles and on mixed vesicles was even greater (3- and 6-fold respectively) than that displayed on Gd1a lipid-free carbohydrate. With each of the used gangliosides the apparent Km values were very similar values for homogeneous micelles and vesicular dispersions, but showed marked increases for Triton X-100 mixed micelles, approaching the values exhibited by reference oligosaccharides. Triton X-100 micelles and phosphatidylcholine vesicles did not appreciably alter the kinetics of sialidase action on 3′-sialosyl-lactose and on Gd1a lipid-free carbohydrate, indicating that the above effects are dependent on the intrinsic characteristics of the membrane-like systems containing gangliosides.

Surface-Enhanced Raman Scattering (SERS) Spectroscopy with Borohydride-Reduced Silver Colloids: Controlling Adsorption of the Scattering Species by Surface Potential of Silver Colloid

1993 ◽  
Vol 58 (11) ◽  
pp. 2682-2694 ◽  
Author(s):  
Kateřina Čermáková ◽  
Ondřej Šesták ◽  
Pavel Matějka ◽  
Vladimír Baumruk ◽  
Blanka Vlčková
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Potential ◽  
Bovine Serum ◽  
Colloidal Particles ◽  
Molar Ratio ◽  
Surface Enhanced ◽  
Surface Enhanced Raman ◽  
Enhanced Raman Scattering ◽  
Ag Colloid

Formation of Ag colloid/adsorbate SERS-active systems (upon adsorption of the selected adsorbates on the surface of Ag colloidal particles) as a function of (i) NaBH4 to AgNO3 molar ratio in the preparation protocol of Ag colloid, and (ii) aging of the colloid has been investigated by Surface-enhanced Raman scattering (SERS) spectroscopy. Oligomeric synthetic polypeptides, bovine serum albumin, phosphate coadsorbed with CuTMePyP [copper(II) derivative of 5,10,15,20-tetrakis-(N-methylpyridinium-4-yl)porphyrin chloride] and borates in systems with N-containing bases were selected as model adsorbates. Both (i) a decrease of NaBH4 to AgNO3 molar ratio upon preparation and (ii) aging of Ag colloid affect adsorption of the adsorbates and consequently, their SERS spectra, in the same manner. Aging of Ag colloid is thus viewed as a slow hydrolysis of BH4- anions. The actual concentration of BH4- in the system is identified as the most important factor controlling adsorption of all the selected adsorbates on the surface of Ag colloid. As this factor can be related to the surface potential, the conditions controlling adsorption of the selected adsorbates are specified in terms of a more negative and/or more positive surface potential of Ag colloidal particles. A more positive surface potential promotes adsorption of polypeptides, bovine serum albumin and phosphate while observation of spectral features of borates in the SERS spectra of N-containing bases in alkaline solutions is conditioned by a more negative surface potential.

Bovine Serum Albumin Interactive One Dimensional Hexanuclear Manganese (III) Complex: Synthesis, Structure, Binding and Molecular Docking Studies

2021 ◽  
Author(s):  
Mahammad Ali ◽  
Rousunara Khatun ◽  
Malay Dolai ◽  
Mihir Sasmal ◽  
Nayim Sepay
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ammonium Hydroxide ◽  
Docking Studies ◽  
Molar Ratio ◽  
One Dimensional ◽  
Molecular Docking Studies ◽  
Hexanuclear Complex

The reaction of MeO-salox (4-methoxy salicylaldehyde-oxime) with Mn(OAc)2.4H2O in methanol medium in 1:1 molar ratio and in the presence of tetra-butyl ammonium hydroxide affords a hexanuclear Complex [Mn6O2(4-MeO-salox)6(N3)2(MeOH)2(H2O)2.2H2O]n (1). Single...

scholarly journals LncRNA-RP11 Modulates TGF-β1-Activated Radiation-Induced Lung Injury Through Downregulating microRNA-29a

Dose-Response ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 155932582094907
Author(s):  
Xi Yang ◽  
Jianjiao Ni ◽  
Yida Li ◽  
Liqing Zou ◽  
Tiantian Guo ◽  
...  
Keyword(s):  
Lung Injury ◽  
Human Lung ◽  
Human Fibroblasts ◽  
Bioinformatic Analysis ◽  
Fine Tuning ◽  
Lung Fibroblasts ◽  
Human Lung Fibroblasts ◽  
Thoracic Radiation ◽  
Radiation Induced ◽  
Tgf Β1

Radiation-induced lung injury (RILI) is one of the most serious complications of thoracic radiation and TGF-β1 is a central regulator of RILI. However, the molecular mechanism underlying the fine tuning of TGF-β1 signaling in RILI has not been fully understood. In the current study, differentially expressed long non-coding RNAs (LncRNAs) among human lung fibroblasts cell lines HFL-1 and WI-38 treated with TGF-β1, were identified by microarray and validated by real time PCR. LncRNA-RP11 was found to be the most increased LncRNA and it mediated the promotion of fibrogenic activity in human lung fibroblasts after TGF-β1 treatment. Bioinformatic analysis revealed that TGF-β1 may be associated with the component and structure of extracellular matrix in lung fibroblasts cells, and LncRNA-RP11 was predicted and confirmed to be a competing endogenous RNA by directly binding to miR-29a. Functional experiments investigating the biological role of LncRNA-RP11/miR-29a axis in RILI, were then carried out in human fibroblasts. The results showed that radiation promoted the expression of LncRNA-RP11, but regressed the expression of miR-29a. Furthermore, radiation elevated the expression of various common collagenic proteins, which could be abolished by overexpression of miR-29a.

scholarly journals The novel behaviour of interactions between Ni2+ ion and human or bovine serum albumin

1994 ◽  
Vol 304 (1) ◽  
pp. 23-26 ◽  
Author(s):  
Y Zhou ◽  
X Hu ◽  
D Ouyang ◽  
J Huang ◽  
Y Wang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Conformational Transition ◽  
Electric Dipole Transition ◽  
Molar Ratio ◽  
The Novel ◽  
Dipole Interactions ◽  
Hysteretic Effect ◽  
Hypochromic Effect

We discovered a series of novel behaviours of interactions between Ni2+ ion and human or bovine serum albumin. Our results indicated that there exist two closely neighbouring identical prior binding sites in the binding of human or bovine serum albumin with Ni2+ ions, not only one. It is very likely that, after the binding of the first Ni2+ ion, an induced slow conformational transition happens, which leads to the binding of the second Ni2+ ion and shows itself as a hysteretic effect for a process of non-enzymic protein binding with metal ions. As the concentrations of the 1:1 (molar ratio of Ni2+ ion to protein) system increase, an increasing hypochromic effect is observed. Such a hypochromic effect has not been reported previously; however, it is in accord with the mechanism of dipole-dipole interactions between the electric dipole transition moments of chromophores.

Sensitive Radioimmunoassay for Detection of O6-Ethyldeoxyguanosine in D N A Exposed to the Carcinogen Ethylnitrosourea in vivo or in vitro

1978 ◽  
Vol 33 (11-12) ◽  
pp. 897-901 ◽  
Author(s):  
Rolf Müller ◽  
Manfred F Rajewsky
Keyword(s):  
Nucleic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Association Constant ◽  
High Specificity ◽  
Diploid Cell ◽  
Molar Ratio

O8-ethyl-2′-deoxyguanosine (O8-EtdGuo) is a major premutational product formed in both in­tracellular DNA and in purified DNA in vitro, after exposure to the potent alkylating carcinogen N-ethyl-N-nitrosourea (EtNU). Antibodies directed against O8-EtdGuo were obtained by immunizing rabbits with a conjungate of O6-EtGuo and bovine serum albumin. In a competitive radioimmuno­assay (RIA), with O8-Et[8,5′·3H]dGuo as a tracer and various alkylated and natural nucleic acid components as inhibitors, these antibodies show high specificity for O6-EtdGuo and detect this product at a level of 0.3 picomol (antibody association constant, 7×108l/mol). In a sample of 130 μg of hydrolyzed DNA, O6-EtdGuo can thus be measured at a molar ratio of O8-EtdGuo/2′- deoxyguanosine of about 3×10-8, i. e., about 5×103 O8-EtdGuo molecules per diploid cell. Exam­ples are given for the quantitation of Oe-EtdGuo in DNA exposed to EtNU in vivo or in vitro.

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