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Unproven and epicutaneous and other investigational forms of immunotherapy
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Haig Tcheurekdjian, Abba I. Terr
In the early 1930s, several medical publications appeared claiming that a specific substance, called “proteose,” is present in the urine during the course of allergic disease [38,39]. Urinary proteose refers to a mixture of partially to completely hydrolyzed protein from the glomerular filtrate. It is therefore postulated to contain allergen peptide fragments, and in particular, those peptides that are “specific” or most allergenic for each individual allergic person. This substance was believed to be a source of allergen for therapy superior to the usual allergen vaccines used in immunotherapy.
Unproven and Controversial Forms of Immunotherapy
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2014
Haig Tcheurekdjian, Abba I. Terr
In the early 1930s, several medical publications appeared claiming that a specific substance, called “proteose,” is present in the urine during the course of allergic disease [38,39]. Urinary proteose refers to a mixture of partially to completely hydrolyzed protein from the glomerular filtrate. It is therefore postulated to contain allergen peptide fragments, and, in particular, those peptides that are “specific” or most allergenic for each individual allergic person. This substance was believed to be a source of allergen for therapy superior to the usual allergen vaccines used in immunotherapy.
Host-Parasite Interactions With Macrophages In Culture
Published in Hans H. Gadebusch, Phagocytes and Cellular Immunity, 2020
Lee S. F. Soderberg, Morris Solotorovsky
The various inducing agents used to stimulate exudation of macrophages are the primary source of variations among macrophages from the peritoneal cavity. In order of frequency of use, these are thioglycollate broth, mineral oil, proteose peptone, starch, glycogen, lysolecithin, endotoxin, triolein, and pyran copolymer. Mouse peritoneal cells can be harvested in useful number, 6 to 10 x 106 per mouse, without inducing agent, but in larger animals uninduced peritoneal exudates are disappointingly meager. In recent literature, thioglycollate, used at 1, 3, or 10%, is by far the most commonly used inducing agent for mice but is seldom used in other animals. Thioglycollateinduced macrophages tend to be sticky. For the guinea pig and rabbit, light mineral oil has been chosen most often. Mineral oil, however, must be separated from the aqueous phase of the exudate and the macrophages obtained are morphologically altered and have frequent intracellular oil droplets. Proteose peptone at 1 or 10%, casein at 5%, and starch at 2 to 5% also are frequently used inducing agents. Peptone, casein, and starch cause some morphological changes in macrophages and increase their stickiness. Dosage for the mouse has been 1 to 4ml, but most often 1 or 2 ml, for the rat up to 20 ml, for the guinea pig up to 30 mi, for sheep 250 mi, and for the rabbit up to 500 mi, but 25 to 30 mi is more usual. The period between administering the inducing agent and harvesting exudate cells has varied from 2 to 8 days, with 3 or 4 days most often reported as optimal. In mice, thioglycollate injected 4 days prior to harvest was reported to yield 25 to 30 x 106 exudate cells per mouse consisting of 85 to 88% macrophages, 5% granulocytes, and 10% lymphocytes.33 Proteose peptone in the amount of 1 or 2 mi or 2% starch 3 to 4 days before harvesting was reported to increase the percentage of phagocytes from 50 to 60% to 75 to 85% of the peritoneal exudate cells.33 Edelson et al.34 compared a number of inducing agents for the yield of mouse peritoneal exudate cells. Thioglycollate gave the largest increase in yield of 18.3 x 106 per mouse as compared with 5.7 x 106 for unstimulated exudates. Proteose peptone at 10% concentration yielded 10.6 x 106 macrophage per mouse and 1% concentration yielded 8.6 x 106 cells. Latex beads, agar, and endotoxin gave more modest increases in cell yield. In this study, increases in the pinocytic rate as measured by the uptake of horseradish peroxidase per 100 mg cell protein per hour was closely correlated with increases in cell yield by the various inducing agents. Over 4 days following injection of thioglycollate into mice, the yield of peritoneal exudate cells increased from 10 x 106 per mouse on day 0 to 29 x 106 on day 4.34 During this period the percentage of macrophages in the exudate increased at the expense of neutrophils and large lymphocytes
Absence of TNF Leads to Alternative Activation in Peritoneal Macrophages in Experimental Listeria Monocytogenes Infection
Published in Immunological Investigations, 2022
Xinying Li, Chen Chen, Lianjun Zhang, Xiaomin Cheng, Huiwu Geng, Qiang Ji, Chao Li, Huili Chen, Heinrich Körner, Xiaoying Liu
Peritoneal exudate cells (PECs) were harvested by injecting mice intraperitoneally with 2 ml of sterile 3% proteose peptone (Hopebio) for 3 days. Peritoneal macrophages were cultured in RPMI 1640 media (Thermo Fisher Scientific) supplemented with 10% heat-inactivated fetal bovine serum (FBS, Gibco) and 1% penicillin and streptomycin (Thermo Fisher Scientific) at 37°C with 5% CO2 for 3 h. Cultures were washed twice with PBS and the adherent macrophages were cultured with recombinant murine IL-4 (10 ng/ml, Peprotech) for 24 h to differentiate PEC into M2 macrophages. Recombinant murine TNF (Peprotech) was then added for a further 24 h at indicated concentrations. In blocking experiments, human TNFR: Fc (Enbrel, Sunshine Guojian) which is cross-reactive with mouse TNF (Markey et al. 2010), and peroxisome proliferator-activated receptor γ (PPARγ) agonist Rosiglitazone (Rosi; MedChemExpress) were added for 3 h before culturing with IL-4 .
A multiplatform strategy for the discovery of conventional monoclonal antibodies that inhibit the voltage-gated potassium channel Kv1.3
Published in mAbs, 2018
Janna Bednenko, Rian Harriman, Lore Mariën, Hai M. Nguyen, Alka Agrawal, Ashot Papoyan, Yelena Bisharyan, Joanna Cardarelli, Donna Cassidy-Hanley, Ted Clark, Darlene Pedersen, Yasmina Abdiche, William Harriman, Bas van der Woning, Hans de Haard, Ellen Collarini, Heike Wulff, Paul Colussi
The Kv1.3 pTRAS expression vector was introduced into conjugating B2086 and CU428 T. thermophila strains by biolistic transformation as described previously.37 Briefly, 20 μl of M17 tungsten beads (Bio-Rad Laboratories) were coated with 8 μg of expression vector DNA. Transformations were carried out using a Biolistic PDS-1000/He Particle Delivery System (Bio-Rad Laboratories) ∼ 10 hours following induction of conjugation. Following particle bombardment and recovery in NEFF medium (0.25% proteose peptone, 0.25% yeast extract, 0.55% glucose, 33 μM FeCl3) at 30°C for 18 h, cells were supplemented with paramomycin (100 μg/ml), aliquoted into 96-well microplates and incubated for 3–4 days at 30°C. Wells containing paromomycin-resistant cells were identified and transferred to stock tubes. To identify Kv1.3 expressing cell lines, drug-resistant clones were grown in 3 ml cultures to a cell density of at least 5 × 105 cells/ml and Kv1.3 expression was induced by the addition of 2 μg/ml CdCl2. Cells were harvested at 6 h post-induction and stored at −20°C. Cells expressing Kv1.3 were identified by Western blot analysis using anti-Kv1.3 and/or anti-tag antibodies. To establish clonal cell lines, single cells were isolated from Kv1.3-expressing stock tubes into drops of NEFF media containing 100 μg/ml paromomycin. Single cell clones were transferred to stock tubes and the best expressing cell lines were identified by Western blot analysis.
In situ spectroscopic analysis of Lactobacillus rhamnosus GG flow on an abiotic surface reveals a role for nutrients in biofilm development
Published in Biofouling, 2019
Man–Rogosa–Sharpe medium, MRS (ref. 288130) and Lactobacilli AOAC media (ref. 290110) were supplied by Difco (Sparks, MD, USA). Trypticase soy broth, TSB (ref. T8907) was purchased from Fluka (St Louis, MO, USA). Modified TSB (mTSB) composed of 20 g l−1 of Bacto proteose peptone no. 3 (Becton, Dickinson and Co., ref 211693) and 15 g l−1 of TSB. Sodium L-lactate and agar were purchased from Sigma (St Louis, MO, USA). Sodium dodecyl sulphate was purchased from Fluka. Ultra-pure water (18.2 MΩ.cm) was used for preparation all media (Elga, Purelab Option-Q).