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Thermal Imaging for Arthritis Evaluation in a Small Animal Model
Published in U. Snekhalatha, K. Palani Thanaraj, Kurt Ammer, Artificial Intelligence-Based Infrared Thermal Image Processing and Its Applications, 2023
U. Snekhalatha, K. Palani Thanaraj, Kurt Ammer
Antigen-induced arthritis is a kind of mono-articular disease which affects only the injected joints. This type of arthritis is induced in knee joints of rats by means of injecting the protein antigen into intra-articular joints. The protein antigen is comprised of methylated bovine serum albumin. The histological results of antigen-induced arthritis closely resemble RA and depict synovial hyperplasia, pannus formation, cartilage erosions, and lymphoid follicles. Certainly, frequent antigen injection in rats causes ectopic lymphoid structures identical to those observed in RA patients.
Gold Nanomaterials at Work in Biomedicine *
Published in Valerio Voliani, Nanomaterials and Neoplasms, 2021
Xuan Yang, Miaoxin Yang, Pang Bo, Madeline Vara, Younan Xia
As one of the most abundant plasma proteins, bovine serum albumin (BSA) is widely used in an array of applications such as sensing, self-assembly, and imaging [81]. Ying and coworkers demonstrated the use of BSA as a template for the synthesis of Au clusters [82], similar to what was reported for the Ag clusters [78]. As shown in Fig. 5.7B, upon the addition of Au(III) ions into an aqueous BSA solution, the protein molecules sequestered Au(III) ions and entrapped them. When the pH value was increased to 12, the reduction power of BSA was enhanced and the entrapped ions would go through progressive reduction to generate Au clusters. Based on the photoluminescence property and the spherical jellium model, the BSA-stabilized Au clusters were proposed to contain a Au25 core, which was consistent with the MALDI-MS data. Due to the excellent biocompatibility and abundant functional groups of BSA, this class of Au clusters remains highly promising for various applications in biomedicine.
Antigens
Published in Roberto R. Kretschmer, Amebiasis: Infection and Disease by Entamoeba histolytica, 2020
Axenic medium commonly used to cultivate E. histolytica is supplemented with bovine serum. Even exhaustive washing of the trophozoites may not eliminate traces of proteins of this source from their surface. In fact the presence of anti-bovine albumin antibodies in the sera of rabbits immunized with axenically grown E. histolytica was shown by two independent groups of investigators in 1980.78,79 The titers were lower but did not disappear, when amebas were thoroughly washed prior to their inoculation. The serum of rabbits immunized with whole extract of axenically grown E. histolytica HK-9 revealed five contaminating antigens related to constituents of the culture medium, when used to identify membranal polypeptides of E. histolytica HK-9 by immunoblotting.80 The foremost contaminating antigen was bovine serum albumin (BSA). The presence of such antigens suggests a strong attachment to amebic membranal proteins, perhaps through hydrophobic bounds. Furthermore, this implies that E. histolytica can absorb and incorporate host antigens into its own membrane surface. This has been shown to occur with Schistosoma mansoni, a parasite that absorbs blood group and histocompatibility antigens of the host, perhaps as a mechanism to evade its immune response.81,82
Neuroprotective effects of quercetin on the cerebellum of zinc oxide nanoparticles (ZnoNps)-exposed rats
Published in Tissue Barriers, 2023
Shaimaa A. Abdelrahman, Amal S. El-Shal, Abeer A. Abdelrahman, Ebtehal Zaid Hassen Saleh, Abeer A. Mahmoud
Avidin biotin complex technique (ABC Peroxidase Staining Kits, Code No. 32020, Thermo Scientific, Rockford, IL, USA) was utilized for immunohistochemical staining of the calcium binding protein; Calbindin, GFAP, and Bax protein. Paraffin-embedded specimens were deparaffinized in xylene and hydrated in distilled water. Antigen retrieval was done in the microwave for 15 minutes using citrate buffer. Bovine serum albumin was used for tissue block. Sections were then incubated overnight at 4°C with the following primary antibodies: Anti-CbD28k (rabbit polyclonal antibody; Cat. No. PA5-85669; dilution 1/500; Thermo Scientific, San Jose, CA, USA). Anti-GFAP (Cat. No. MS- 280- R7, Lab Vision Corporation, Fremont, USA) was diluted to1:100 in Lab Vision antibody diluent (Cat. TA- 125- UD). Finally, Bax mouse monoclonal antibody (CAT. MAS-14003, Lab Vision Corporation, Fremont, USA) was diluted to 1:200 in PBS (for 30 min at room temperature). Recognition was accomplished by secondary antibodies and labeled horseradish peroxidase followed by colorimetric detection by 3′, 3-diaminobenzidine (DAB). As a counterstain, Mayer’s Hematoxylin was utilized. As a substitute for the primary antibody, negative control slides were immersed in phosphate-buffered saline. The brown color indicated the antigen location under light microscopy.39
PU.1 interaction with p50 promotes microglial-mediated inflammation in secondary spinal cord injury in SCI rats
Published in International Journal of Neuroscience, 2023
Mingchen Yu, Yiqing Ou, Hongmei Wang, Weidong Gu
The sections to be studied (sham operation, 3 days post-SCI) were heated in a 37 °C oven for 2 h, followed by two 5-min washes with 0.01 M PBS. Next, the sections were blocked with PBS containing 5% bovine serum albumin for 2 h and then permeated with 0.1% Triton X-100/PBS for 20 min. The sections were then incubated with the primary monoclonal antibody PU.1 (rabbit, 1:100; Abcam) or antibodies of different cellular markers, such as NeuN (neuron marker, mouse, 1:500; Chemicon, Temecula, CA, USA), GFAP (astrocyte marker, mouse, 1:100; Sigma), and Iba-1 (cytoplasmic marker of microglia, mouse, 1:100; Serotec, Oxford, UK), for 12 h. The antibodies were prepared in 1% bovine serum albumin. After incubation, the sections were washed 3 times with PBS, 10 min per wash, and then incubated with the secondary antibody (CY3-Donkey or FITC-Donkey, 1:1000; Jackson Laboratory, Bar Harbor, ME, USA) in the dark at RT for 2 h. The stained sections were observed with a Leica fluorescence microscope or Leica confocal microscope.
Insights into the potential mechanism underlying liver dysfunction in male albino rat exposed to gasoline fumes
Published in Egyptian Journal of Basic and Applied Sciences, 2021
Folarin Owagboriaye, Sulaimon Aina, Rasheed Oladunjoye, Titilola Salisu, Adedamola Adenekan, Gabriel Dedeke
Activities of membrane-bound ATPases enzymes including Na+/K+ -ATPase, Ca2+ -ATPase and Mg2+ -ATPase, in the liver homogenate of the rats were determined according to the method of [31–33],and as modified [34]. The assay was carried out by estimating the amount of phosphorus liberated from the incubation mixture containing the tissue homogenate, 5 mM of ATP, 2 Mm of CaCl2, 2 mM of MgCl2, 60 mM of NaCl, 20 mM of KCl and protein enzyme. Incubation of the tubes was at 37°C and enzyme inactivation was done by the addition of 1 mL of cold 10% (w/v) trichloroacetic acid (TCA) after 25 min. We kept the tubes in ice cold for 20 min and removed the precipitated proteins by centrifugation. A control was simultaneously set up by adding enzyme after TCA at the end of the incubation period. Protein concentration was estimated by the method of [29], with bovine serum albumin as standard.