scholarly journals Specific histamine binding activity of a new lipocalin from Hyalomma asiaticum (Ixodidae) and therapeutic effects on allergic asthma in mice

2016 ◽  
Vol 9 (1) ◽  
Author(s):  
Yanan Wang ◽  
Zhuang Li ◽  
Yongzhi Zhou ◽  
Jie Cao ◽  
Houshuang Zhang ◽  
...  
Keyword(s):  
Allergic Asthma ◽  
Binding Activity ◽  
Therapeutic Effects ◽  
Histamine Binding

Therapeutic effects of resveratrol in a mouse model of HDM-induced allergic asthma

2015 ◽  
Vol 25 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Jiaxiang Chen ◽  
Hao Zhou ◽  
Jinlei Wang ◽  
Baoping Zhang ◽  
Fen Liu ◽  
...  
Keyword(s):  
Mouse Model ◽  
Allergic Asthma ◽  
Therapeutic Effects

Therapeutic effects of 2B8T2M, a novel fusion of ALT-803, an IL-15 superagonist, with 4 single-chains of anti-CD20 antibody in combination with expanded natural killer cells against rituximab sensitive and resistant Burkitt lymphoma (BL).

2018 ◽  
Vol 36 (5_suppl) ◽  
pp. 32-32
Author(s):  
Yaya Chu ◽  
Nang Kham Su ◽  
Sarah Alter ◽  
Emily Jeng ◽  
Peter R. Rhode ◽  
...  
Keyword(s):  
Nk Cells ◽  
Granzyme B ◽  
Treatment Options ◽  
Binding Activity ◽  
In Vitro Cytotoxicity ◽  
Patient Treatment ◽  
Therapeutic Effects ◽  
Comparison Results

32 Background: Patients retreated with rituximab often relapse which limit patient treatment options (Goldman/Cairo, Leukemia, 2013). Our group has successfully expanded functional and active peripheral blood NK cells (exPBNK) to target BL (Chu/Cairo, et al, Can Imm Res, 2015). 2B8T2M was generated by fusing ALT-803, an IL-15 superagonist, to four single-chains of rituximab (Liu/Wong, et al, JBC, 2016). 2B8T2M displayed tri-specific CD20 binding activity, activated NK cells to enhance antibody-dependent cellular cytotoxicity, and induced apoptosis of B-lymphoma cells (Liu/Wong, et al, JBC, 2016). Methods: ALT-803 and 2B8T2M were generously provided by Altor BioScience Corporation. NK expansion, NK receptors expression and cytotoxicity were examined as we previous described (Chu/Cairo, et al, Can Imm Res 2015). IFNg and granzyme B levels were examined by ELISA assays. Equal doses of IgG, Rituximab, ALT-803, Rituximab+ALT-803, obinutuzumab (obinu, generously provided by Christian Klein, PhD from Roche) were used for comparison. Results: 2B8T2M significantly enhanced exPBNK cytotoxicity against rituximab-sensitive Raji cells compared to the controls IgG, Rituximab, ALT-803, Rituximab+ALT-803, obinu (p < 0.001, E:T = 1:1). 2B8T2M also significantly enhanced exPBNK cytotoxicity against rituximab-resistant Raji-2R cells (p < 0.001, E:T = 1:1) and resistant Raji-4RH cells (p < 0.001, E:T = 1:1). Furthermore, 2B8T2M significantly enhanced IFN-g and granzyme B production from exPBNK against Raji, Raji-2R and Raji-4RH compared to IgG (p < 0.001), rituximab (p < 0.001), ALT-803 (p < 0.001), Rituximab+ALT-803 (p < 0.001), and obinutuzumab (p < 0.001). Conclusions: 2B8T2M compared to rituximab, ALT-803 or obinutuzumab significantly enhanced exPBNK in vitro cytotoxicity against rituximab-sensitive and –resistant BL cells. The in vivo functions of 2B8T2M with exPBNK using humanized NSG models are under investigation.

scholarly journals A mechanism of resistance to glucocorticoids in multiple myeloma: transient expression of a truncated glucocorticoid receptor mRNA

Blood ◽  
1992 ◽  
Vol 79 (1) ◽  
pp. 213-222 ◽  
Author(s):  
PA Moalli ◽  
S Pillay ◽  
D Weiner ◽  
R Leikin ◽  
ST Rosen
Keyword(s):  
Multiple Myeloma ◽  
Glucocorticoid Receptors ◽  
Genomic Sequence ◽  
Binding Activity ◽  
Therapeutic Effects ◽  
Early Form ◽  
Ru 486 ◽  
Human Multiple Myeloma ◽  
Glucocorticoid Receptor Mrna ◽  
Allelic Variations

Abstract Despite their widespread use, little is known of either the mechanism of action of glucocorticoids in the treatment of multiple myeloma or why patients ultimately become resistant to their therapeutic effects. Here, we address these issues by examining the direct effects of the glucocorticoid dexamethasone (DEX) on a hormone-sensitive clone (MM.1S) of a human multiple myeloma line and compare them with those of its hormone-resistant counterpart (MM.1R). MM.1S expresses approximately 50,000 glucocorticoid receptors (GR) per cell, the full-length 7.1-kb GR mRNA at high levels, and is lysed by DEX. DEX-induced cytolysis is effectively blocked by the glucocorticoid antagonist, RU 486, indicating the specificity of this response for the GR. In contrast to MM.1S, MM.1R is not lysed by hormone, has little hormone-binding activity, and expresses the 7.1-kb GR mRNA at low levels. Interestingly, we have found that two distinct phenotypes emerge from MM.1R with increasing periods of growth in culture. The first or “early” form, MM.1Re, expresses high levels of a variant GR mRNA of 5.5 kb that has a deletion in its 3′ end. With further growth in the presence or absence of selective media, the expression of this transcript is repressed, resulting in the second or “late” phenotype characteristic of MM.1RL. No discernible differences in the organization of the genomic GR sequence in DEX-sensitive and -resistant cells were detectable by Southern analysis, suggesting that no gross deletions, rearrangements, or allelic variations in the genomic sequence account for the resistant phenotypes of MM.1R.

scholarly journals Synthetic bovine lactoferrin peptide Lfampin kills Entamoeba histolytica trophozoites by necrosis and resolves amoebic intracecal infection in mice

2019 ◽  
Vol 39 (1) ◽  
Author(s):  
César Díaz-Godínez ◽  
Ximena González-Galindo ◽  
Thuluz Meza-Menchaca ◽  
Raúl J. Bobes ◽  
Mireya de la Garza ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Oral Treatment ◽  
Public Health Problem ◽  
Annexin V ◽  
Docking Studies ◽  
Binding Activity ◽  
Bovine Lactoferrin ◽  
Therapeutic Effects ◽  
Intestinal Amoebiasis

AbstractAmoebiasis caused by the protozoan parasite Entamoeba histolytica remains a public health problem in developing countries, making the identification of new anti-amoebic compounds a continuing priority. Previously, we have shown that lactoferrin (Lf) and several Lf-derived peptides exhibit in vitro anti-amoebic activity independently of their iron-binding activity. Here, we evaluated the amoebicidal effect of synthetic Lf-derived peptides Lfcin-B, Lfcin 17-30, and Lfampin, analyzed the mechanism of death induced by the peptides and determined their therapeutic effects on murine intestinal amoebiasis. MTT assays in trophozoite cultures of E. histolytica exposed to each peptide (1–1000 μM) showed that Lfampin is far more amoebicidal than Lfcins. Lfampin killed 80% of trophozoites at doses higher than 100 μM in 24 h, and FACs analysis using Annexin V/propidium iodide showed that death occurred mainly by necrosis. In contrast, Lfcin-B and Lfcin 17-30 appeared to have no significant effect on amoebic viability. FACs and confocal microscopy analysis using FITC-labeled peptides showed that all three peptides are internalized by the amoeba mainly using receptor (PI3K signaling) and actin-dependent pathways but independent of clathrin. Docking studies identified cholesterol in the amoeba’s plasma membrane as a possible target of Lfampin. Oral treatment of intracecally infected mice with the abovementioned peptides at 10 mg/kg for 4 days showed that Lfampin resolved 100% of the cases of intestinal amoebiasis, whereas Lfcin 17-30 and Lfcin-B were effective in resolving infection in 80 and 70% of cases, respectively. These data show that although synthetic bovine Lf-derived peptides exhibit varying amoebicidal potentials in vitro, they do resolve murine intestinal amoebiasis efficiently, suggesting that they may be useful as a therapeutic treatment.

scholarly journals Glucosinolates With Their Hydrolysis Products from Two Cruciferous Plants with Study of Antidiabetic Activity Based on Molecular Docking

2020 ◽  
Author(s):  
Khaled Abdelshafeek ◽  
Walid E. Abdallah ◽  
Ahmed elhenawy ◽  
Abeer Alothami ◽  
Lila Alharby ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Docking Study ◽  
Binding Activity ◽  
Antidiabetic Activity ◽  
Therapeutic Effects ◽  
Spectroscopic Measurements ◽  
Hydrolysis Products ◽  
Aluminum Oxide Column ◽  
Cruciferous Plants ◽  
Drug Studies

Abstract The glucosinolates (Gls.) are natural bioactive compounds which lead to the formation of different metabolites called isothiocyanates(ITC) having various therapeutic effects. So, this study aim to isolate the glucosinolates of both Carrichtera annua L.(DC) (CA) and Farsetia aegyptia Turra (FA) belonging to Crucifereae family. The total Gls. were isolated from the aqueous methanolic extract of both plants and further purified on acidic aluminum oxide column. Some of the obtained Gls. was identified as it is using different spectroscopic measurements (UV, NMR and MS) and the rest were hydrolyzed using myrosinase enzyme to the corresponding isothiocyanates (ITC) which were identified by GC/MS. only one glucosinolate was identified in CA as: 4-methylthio-3-butenyl Gls ( MTBG). through chromatographic and spectroscopic measurements in addition to 6-methyl sulfonylhexyl isothiocyanates(ITC), while 6-methyl sulfonyl-6-hydroxy hexyl ITC, 4-pentenyl ITC, 3-Methylthio propyl ITC, 5-hydroxy pentyl ITC and 4-methylsulphinyl butyl ITC from FA. The docking study targeted a α-glucosidase and amylase, to examine a mode of action of the 4-methylthio-3-butenylglucosinolate. Molecular docking was performed to identify potency of Gls. against hyperglycemia. The data obtained revealed that the Gls. has high binding activity Via α-glucosidase and amylase. Furthermore, further Drug studies as likeness and ADME/T were performed, which proposed that their ligands may be have a good pharmacokinetic character, with no carcinogenesis effect.

scholarly journals A mechanism of resistance to glucocorticoids in multiple myeloma: transient expression of a truncated glucocorticoid receptor mRNA

Blood ◽  
1992 ◽  
Vol 79 (1) ◽  
pp. 213-222 ◽  
Author(s):  
PA Moalli ◽  
S Pillay ◽  
D Weiner ◽  
R Leikin ◽  
ST Rosen
Keyword(s):  
Multiple Myeloma ◽  
Glucocorticoid Receptors ◽  
Genomic Sequence ◽  
Binding Activity ◽  
Therapeutic Effects ◽  
Early Form ◽  
Ru 486 ◽  
Human Multiple Myeloma ◽  
Glucocorticoid Receptor Mrna ◽  
Allelic Variations

Despite their widespread use, little is known of either the mechanism of action of glucocorticoids in the treatment of multiple myeloma or why patients ultimately become resistant to their therapeutic effects. Here, we address these issues by examining the direct effects of the glucocorticoid dexamethasone (DEX) on a hormone-sensitive clone (MM.1S) of a human multiple myeloma line and compare them with those of its hormone-resistant counterpart (MM.1R). MM.1S expresses approximately 50,000 glucocorticoid receptors (GR) per cell, the full-length 7.1-kb GR mRNA at high levels, and is lysed by DEX. DEX-induced cytolysis is effectively blocked by the glucocorticoid antagonist, RU 486, indicating the specificity of this response for the GR. In contrast to MM.1S, MM.1R is not lysed by hormone, has little hormone-binding activity, and expresses the 7.1-kb GR mRNA at low levels. Interestingly, we have found that two distinct phenotypes emerge from MM.1R with increasing periods of growth in culture. The first or “early” form, MM.1Re, expresses high levels of a variant GR mRNA of 5.5 kb that has a deletion in its 3′ end. With further growth in the presence or absence of selective media, the expression of this transcript is repressed, resulting in the second or “late” phenotype characteristic of MM.1RL. No discernible differences in the organization of the genomic GR sequence in DEX-sensitive and -resistant cells were detectable by Southern analysis, suggesting that no gross deletions, rearrangements, or allelic variations in the genomic sequence account for the resistant phenotypes of MM.1R.

scholarly journals Histamine Binding Activity of Surface-Modified Yeast by Histamine Binding Protein (HBP)

2021 ◽  
Author(s):  
Hyewon Jang ◽  
Geun Woo Lee ◽  
Yang-Hoon Kim ◽  
Jiho Min
Keyword(s):  
Cell Concentration ◽  
Binding Protein ◽  
Inhibitory Effect ◽  
Mite Species ◽  
Binding Activity ◽  
The Body ◽  
Dead Cell ◽  
Inhibitory Ability ◽  
Histamine Binding ◽  
Histamine Binding Protein

Abstract Histamine is an immune mediator that is mainly secreted when an immediate, rapid response is needed in the body, and an excessive secretion of histamine or lack of enzymes that degrade histamine can result in various side effects. Histamine binding protein (HBP) is secreted by a mite species to prevent the host’s histamine-induced immune responses by binding the histamine molecule in the blood. Cloning was performed to express HBP on the yeast surface (MBTL-GWL-1), and immunofluorescence (IF) and western blot was performed to confirm the expression of the recombinant protein. The histamine inhibitory ability of GWL-1 cells was tested according to the cell concentration. The highest inhibitory ability of 1.30×107 CFU/ml of GWL-1 cells was of about 60%. The GWL-1 cell concentration and the degree of histamine inhibition were confirmed to be dose-dependent, and dead cell debris was shown to have a histamine inhibitory effect, although not as much as that of whole cells. Phagocytosis assays were performed to determine whether histamine affected the RAW 264.7 cell’s phagocytosis, and to indirectly confirm the GWL-1 cell’s histamine inhibition. By confirming that, we found that GWL-1 captures histamine. Therefore, it can be expected to become a competitive material in the anti-allergy market.

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