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Tachykinin Antagonists in Asthma and Inflammation
Published in Sami I. Said, Proinflammatory and Antiinflammatory Peptides, 2020
Studies on isolated mast cells have led to various general conclusions about mast cell degranulation by SP: (a) It requires the N-terminal region of the SP molecule and does not involve NK1 NK2, or NK3 receptors; (b) it is produced by relatively high concentrations of SP, in the micromolar range; (c) it is not shared by other TKs which lack the basic N-terminal residues of SP; (d) it is not uniformly observed in mast cells from different species, nor from mast cells of the same species but from different organs (155–161). Regarding the mechanisms involved, a direct activation of G proteins (receptor-independent mechanism) by the cluster of positively charged amino acid residues at the N-terminal end of the SP molecule is the currently available explanation for this effect; this mechanism would be common to the mast cell-degranulating activity of compound 48/80, bradykinin, mastoparan, and other cationic amphiphilic peptides (see Ref. 162 for review). Certain mast cell lines may express specific TK receptors which recognize the C-terminal sequence of TKs (163,164), but the general significance of these findings remains to be assessed. Recently, Ansel et al. (165) showed that SP, at concentrations ranging between 1 and 100 nM, activates the expression of tumor necrosis factor-⍺ mRNA in murine peritoneal mast cells; owing to the relatively low concentration of peptide used, it is possible that a typical TK receptor is involved, but no attempt at characterization was presented.
Hymenoptera allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Rafael I. Monsalve, Te Piao King, Miles Guralnick
Yellow jacket venom was found to be lethal in mice when injected intraperitoneally but not subcutaneously [65]. The toxic action was shown to require the synergistic action of the venom peptide mastoparan and the venom protein phospholipase A1. This toxin action has also been taken into account in recent studies on the venom components of diverse Hymenoptera [60,66].
Hymenoptera Allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2014
Yellow jacket venom was found to be lethal in mice when injected intraperitoneally, but not subcutaneously [46]. The toxic action was shown to require the synergistic action of the venom peptide mastoparan and the venom protein phospholipase A1.
MRGPRX2 activation as a rapid, high-throughput mechanistic-based approach for detecting peptide-mediated human mast cell degranulation liabilities
Published in Journal of Immunotoxicology, 2020
Marc A. Lafleur, Jonathan Werner, Madeline Fort, Edward K. Lobenhofer, Mercedesz Balazs, Ana Goyos
Cell surface expression of mature human mast cell markers c-kit (Valent et al. 1992) and FcεRI (Stone et al. 2010) in addition to the pan-leukocyte marker CD45 were assessed by flow cytometry at 10 weeks for three separate human donors. A flow cytometry dot-plot is shown for one representative donor (Figure 1(c)). The mean percentage of singlet, live, c-kit+, FcεRI+, and CD45+ cells for the three separate human donors was 97.0 (± 1.5)%. Functional responsiveness was determined in a human MCD assay by mast cell treatment with agents that cause MCD via different receptors/mechanisms and evaluated for histamine release. FcεRI crosslinking by pre-loading cells with human IgE and treatment with an anti-IgE antibody caused histamine release, but not when IgE was absent (Figure 1(d)). Additionally, histamine release (Figure 1(e)) was observed when mast cells were stimulated with three known MCD peptides/agents (compound 48/80 [Mousli et al. 1991], MCDP [Tatemoto et al. 2006], and mastoparan [McNeil et al. 2015]), but not by C-peptide (negative control). Using these positive and negative control peptides/agents, EC50 donor variability was assessed in three separate human donors. Low variability was seen between donors with a maximum EC50 difference ≤ 2.3-fold for the positive controls (Figure 1(f)). These results demonstrate that the mast cell granules contained histamine and were functionally responsive to multiple classes of MCD agents.
Calcium-dependent, non-apoptotic, large plasma membrane bleb formation in physiologically stimulated mast cells and basophils
Published in Journal of Extracellular Vesicles, 2019
C. Jansen, C Tobita, E. U. Umemoto, J. Starkus, N. M. Rysavy, L. M. N. Shimoda, C. Sung, A.J. Stokes, H Turner
General chemicals were from VWR (West Chester, PA, USA) and Sigma Aldrich (St. Louis, MO, USA). Phorbol myristate acetate (PMA) and ionomycin were from Calbiochem (Gibbstown, NJ, USA). IgE anti-di-nitro phenol (anti-DNP) is from Sigma and KLH-DNP was from Calbiochem. Bee venom was from HollisterStier (Spokane, WA, USA). To mitigate batch-to-batch variation in venom, three independent batches were selected on the basis of similar potency for induction of histamine release in control experiments, mixed, aliquoted and used for the duration of the studies presented here. Mastoparan and mellitin were from Sigma Aldrich. Arachidonic acid was from Enzo (Farmingdale, NY, USA). 2-Aminoethoxydiphenyl borate (2-APB) was from Calbiochem (LaJolla, CA, USA). Capsaicin and capsazepine were from Sigma Aldrich.
Cytotoxic, necrotic, apoptotic, and autophagic properties of venom sac extract of Vespa orientalis in T47D and MCF10A breast cell lines
Published in Toxin Reviews, 2023
Seyed Mohammad-Hossein Shetab-Boushehri, Asieh Hosseini, Javad Rafinejad, Alireza Ebadollahi-Natanzi, Seyed Vahid Shetab-Boushehri
Honey bee, Apis mellifera, is classified in the Apidae family while wasps and hornets are classified in the Vespidae family (Lee et al. 2007; Moreno and Giralt 2015; Frangieh et al. 2019). Although a plethora of studies have been conducted on honey bee venom to show it's cytotoxic (Lee et al. 2007; Moreno and Giralt 2015; Frangieh et al. 2019), apoptotic (Tipgomut et al. 2018; Zarrinnahad et al. 2018; Ceremuga et al. 2020), necrotic (Ownby et al. 1997; Florea and Crăciun 2012; Rady et al. 2017), and autophagic (Rodríguez-Acosta et al. 2004; Lv et al. 2019) properties, less similar works have done on hornets’ venoms. Honey bee venom contains biologically active peptides such as apamine, melittin, mast cell-degranulating peptide and others, in addition to phospholipases A2 and B, hyaluronidase, histamine, dopamine, monosaccharides, and lipids (Strong and Wadsworth 2000; Biló et al. 2005; Ollert and Blank 2015; Watkins 2019). Bee stings typically produce immediate, sharp or burning pain, slight local erythema, and edema followed by itching (Watkins 2019). Venoms of wasps and hornets contain a high content of peptides including mastoparan in wasps and hornets, and crabrolin in hornets which release histamine from mast cells (Watkins 2019). These venoms also contain phospholipases and hyaluronidases which contribute to the breakdown of membranes and connective tissue to facilitate diffusion of the venom. These proteins also contribute to the allergenicity of the venoms (Watkins 2019). Other peptides called wasp kinins induce immediate pain, vasodilation, and increased vascular permeability leading to edema (Watkins 2019).