Melittin as an Epithelial Permeability Enhancer I: Investigation  of Its Mechanism of Action in Caco-2 Monolayers

Maher, Sam; Feighery, Linda; Brayden, David J.; McClean, Siobhán

doi:10.1007/s11095-007-9288-2

Cited by 37 publications

(32 citation statements)

References 49 publications

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“…The increased lytic effects of melittin over conventional cationic antimicrobial peptides results from a higher hydrophobicity (17). Although the use of this antimicrobial peptide in the treatment of systemic infections is not feasible due to interaction with eukaryotic plasma membranes (9,15) at concentrations equivalent to antimicrobial activity, melittin has demonstrated potent ability to enhance the absorption of a range of molecules, including macromolecules in Caco-2 monolayers with minimal cytotox- 10.1007/s11095-007-9246-z icity in the polarized target cells (18)(19)(20). Melittin resulted in a rapid concentration-dependant decrease and subsequent recovery in TER in Caco-2 monolayers (20) with 1000-fold greater potency than that of C10 (5,21).…”

Section: Introductionmentioning

confidence: 99%

Melittin as a Permeability Enhancer II: In Vitro Investigations in Human Mucus Secreting Intestinal Monolayers and Rat Colonic Mucosae

et al. 2007

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Section: Introductionmentioning

confidence: 99%

Melittin as a Permeability Enhancer II: In Vitro Investigations in Human Mucus Secreting Intestinal Monolayers and Rat Colonic Mucosae

et al. 2007

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“…Andersson et al [44] proved that the rigidity of membrane can have considerable effect on melittin-membrane interaction. The apically added melittin can cause transepithelial electrical resistance reductions on dectrans flux [45]. Another study reported [46] that although amino acid sequence of Japanese frogs has similarity with that of melittin, their evolutionary relationship is not orthologous.…”

Section: Discussionmentioning

confidence: 99%

Production of antibacterial peptide from bee venom via a new strategy for heterologous expression

et al. 2014

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Honey bee is important economic insect that not only pollinates fruits and crops but also provides products with various physiological activities. Bee venom is a functional agent that is widely applied in clinical treatment and pharmacy. Secapin is one of these agents that have a significant role in therapy. The functions of secapin from the bee venom have been documented, but little information is known about its heterologous expression under natural condition. Moreover, few scholars verified experimentally the functions of secapin from bee venom in vitro. In this study, we successfully constructed a heterologous expression vector, which is different from conventional expression system. A transgenic approach was established for transformation of secapin gene from the venom of Apis mellifera carnica (Ac-sec) into the edible fungi, Coprinus cinereus. Ac-sec was encoded by a 234 bp nucleotide that contained a signal peptide domain and two potential phosphorylation sites. The sequence exhibited highly homology with various secapins characterized from honey bee and related species. Southern blot data indicated that Ac-sec was present as single or multiple copy loci in the C. cinereus genome. By co-transformation and double-layer active assay, Ac-sec was expressed successfully in C. cinereus and the antibacterial activity of the recombinants was identified, showing notable antibacterial activities on different bacteria. Although Ac-sec is from the venom of Apidae, phylogenetic analysis demonstrated that Ac-sec was more closely related to that of Vespid than to bee species from Apidae. The molecular characteristics of Ac-sec and the potential roles of small peptides in biology were discussed.

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“…Cleavage of E-cadherin likely provokes loss of epithelial cell-cell contacts and may contribute to the genesis of eczematous dermatitis (41). Thus, an explanation retrospectively emerges for the recent finding that melittin enhances permeability of CaCo-2 epithelial cell monolayers (60). ADAM17 cleaves a large number of substrates including cytokines (e.g.…”

Section: Discussionmentioning

confidence: 99%

Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

Sommer

Fries

Cornelsen

et al. 2012

Journal of Biological Chemistry

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Background:Melittin is an antimicrobial peptide that is also being considered as anti-inflammatory and anti-cancer agent. Results: Melittin provokes P2 receptor activation, which leads to ADAM-dependent transactivation of the EGFR and augments keratinocyte proliferation and migration. Conclusion: Melittin modulates cellular functions through activation of ADAM-mediated shedding. Significance: The use of melittin may elicit unexpected and unwanted effects via ADAM activation.

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Melittin as an Epithelial Permeability Enhancer I: Investigation of Its Mechanism of Action in Caco-2 Monolayers

Abstract: Apically-added melittin opens tight junctions, causing dramatic TER reductions with significant increases in flux of dextrans. These effects appear mediated in part via PLA2 and involve alterations in specific tight junction proteins.

Cited by 37 publications

References 49 publications

Melittin as a Permeability Enhancer II: In Vitro Investigations in Human Mucus Secreting Intestinal Monolayers and Rat Colonic Mucosae

Melittin as a Permeability Enhancer II: In Vitro Investigations in Human Mucus Secreting Intestinal Monolayers and Rat Colonic Mucosae

Production of antibacterial peptide from bee venom via a new strategy for heterologous expression

Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

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